|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-879 |
0e+00 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 850.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 1 MKIERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAILVGLYWSKRMRLRGLKKDEFTRTGTRGAIIEITFEED 80
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 81 GTKYKVLRDFARNVSYLKRLDGREwrhVTETSMESVSSFIDRIIPYNVFLNAIYVRQGQIDAILESDETRDKIVKEILNL 160
Cdd:PRK03918 81 GRKYRIVRSFNRGESYLKYLDGSE---VLEEGDSSVREWVERLIPYHVFLNAIYIRQGEIDAILESDESREKVVRQILGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 161 DKLEKAYDNLGKIRKYIKYSIEEKEKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEATF 240
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 241 NSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKETEYRRLIEFKDEYLVKKNELEKRLG 320
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 321 ILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRLKAQMESLKSKLGGLEPEKINEKLLYLE 400
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 401 NRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGKCPVCGRELTEEHKADLLRKYSLELSSIEKEIQEAKALERQ 480
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERK 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 481 LRAEFRKVENEL---SRLSSLKTIADQIIEIRERLSKINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDYKNE 557
Cdd:PRK03918 478 LRKELRELEKVLkkeSELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 558 STKLEIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIRELEKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEELAK 637
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAE 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 638 IETDIEKVTSQLNELQRKFDQKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEKLN 717
Cdd:PRK03918 638 TEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLE 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 718 IAIKRIEELRGKIKEYKALIKEEALNKIGEIASEIFSEFTDGKYSGIAIRAEDNKVKLFVIYDGVERPLTFLSGGERIAL 797
Cdd:PRK03918 718 KALERVEELREKVKKYKALLKERALSKVGEIASEIFEELTEGKYSGVRVKAEENKVKLFVVYQGKERPLTFLSGGERIAL 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 798 GLAFRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEELKDAADHVIRIRLEGGASKVEV 877
Cdd:PRK03918 798 GLAFRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDEELKDAADYVIRVSLEGGVSKVEV 877
|
..
gi 18202079 878 VS 879
Cdd:PRK03918 878 VS 879
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
1-879 |
5.49e-75 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 262.73 E-value: 5.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 1 MKIERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAILVGLYwskRMRLRGLKKDeFTRTGTRGAIIEITFEED 80
Cdd:NF041034 1 MKIERIFLENFLSHESSEVNFKGSINAIIGHNGAGKSSIIDGIVFSLF---RESSRGNNED-LIKKGKKTATVELKLEDN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 81 GTKYKVLRDFARNVSYLKRLDGREwrhVTETSMESVSSFIDRIIPYN--VFLNAIYVRQGQIDAILESdetRDKIVKEIL 158
Cdd:NF041034 77 GKTYLIKRNIPNSYSDDDTISNLK---TIARGSTEVNQKIQEILNLDkdVLLSTVIVRQGEIESIFKN---LPDVMKKIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 159 NLDKLEKAYDNLGKIRKYIKysieEKEKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEA 238
Cdd:NF041034 151 KIENLEKLTDSNGPIYSVIK----EIENKLKYLESEKERYESKEAEKEKLEKEIEESKNKLEDLEIKKEEKEKELNDLKK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 239 TFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKETEYRRLIEFKdeylvkknELEKR 318
Cdd:NF041034 227 EFEELEKKRERYDELTGRLSSLNKRINEIEEDLKDLEKLKKEKEKLEKEIKEKEKLEEKNEIISELK--------ELIKS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 319 LGILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRLKAQMESLKSKLGGLEPE----KINE 394
Cdd:NF041034 299 IKELKRQLNTLEKEIEEYKENLKKKKELEDKAKKYEELKREKEELEEKENEYNSLKSRLNSLKKKLEEIENEisklGIII 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 395 KLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARG-KCPVCGRELTEEHKADLLRKYSLELSSIEKEIQE 473
Cdd:NF041034 379 NIEELKKKLDKLSEEINNKNNEKGEIKGRKEQLLKILKNLNNVKGnKCPVCGRELDEEHKKKIREEIEEKIKDLNKQISK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 474 AKALERQLRAEFRKVENELSRLSSLKTiadqiieIRERLSKINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELND 553
Cdd:NF041034 459 LEKEVNSLNKEKEELENKINKLQEEKL-------IKLEKLLKELQRLKKEIEEIEKELKELEESHEEYEEIKEELKELEP 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 554 YKNESTKL----EIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIRELEKFHNKYIEAKNAEKE---LRDILESLKDERE 626
Cdd:NF041034 532 KYKEYLKVsnvtEEELEELERRLSEIKSELDELEKKYSELKEKIGDDREELTQIEKKIEKKIKEikeLKNKLEKLKEEIA 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 627 ELDKAFEELAKIETDIEKVTSQLNELqrKFDQKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKER 706
Cdd:NF041034 612 KIEKEKEEIEKIENEIKELEEEISSL--NFDEERYQNLKEKIEKLNKELNRIEQEISKLEGKIEALENDIDNLNSELEKI 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 707 ESAKMELEKLNIAIKRIEELRGKIKEYK--ALIKEEALNKIGEIASEIFSEFtDGKYSGIAI------RAEDNKVKLFVI 778
Cdd:NF041034 690 KEKLNKIPKLENAIKKLEKLREDLSGSGlqNYIISNVKSKIENNLNDILSKF-DLSFSRVEIdfeiggKTKKGKSEIKAY 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 779 YD-GVERPLTFLSGGERIALGLAFRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEELK 857
Cdd:NF041034 769 NTaGQDLDVNALSGGERISIALALRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHDEELK 848
|
890 900
....*....|....*....|..
gi 18202079 858 DAADHVIRIRLEGGASKVEVVS 879
Cdd:NF041034 849 EISDYIISVEKKGDSSKVKVGS 870
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-878 |
8.07e-62 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 225.55 E-value: 8.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 1 MKIERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAILVGLYWSKRMRlrglKKDEFTRTGTRGAIIEITFEED 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDKRTE----KIEDMIKKGKNNLEVELEFRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 81 GTKYKVLRdfarnvSYLKRLDGREWRHVTETSMESVSSFIDRIIPY----------NVFLNAIYVRQGQIDAILESD-ET 149
Cdd:PRK01156 77 GHVYQIRR------SIERRGKGSRREAYIKKDGSIIAEGFDDTTKYieknilgiskDVFLNSIFVGQGEMDSLISGDpAQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 150 RDKIVKEILNLDKLEKAYDNLGKIRKYIKYSI-------EEKEKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSNLPRL 222
Cdd:PRK01156 151 RKKILDEILEINSLERNYDKLKDVIDMLRAEIsnidyleEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 223 RRELEGIKEEVKTLEATFNSITELKLRLGELNGKKGRLEERIRQLeSGIEEKRKKSKELEEVVK-----ELPELEKKETE 297
Cdd:PRK01156 231 MDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYY-KELEERHMKIINDPVYKNrnyinDYFKYKNDIEN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 298 YRRLIEFKDEYLVKKNELEKRLGILS---NRLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRLK 374
Cdd:PRK01156 310 KKQILSNIDAEINKYHAIIKKLSVLQkdyNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERM 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 375 AQMESLKSKLGGLEPEKINEkllylenRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKK------ARGKCPVCGREL 448
Cdd:PRK01156 390 SAFISEILKIQEIDPDAIKK-------ELNEINVKLQDISSKVSSLNQRIRALRENLDELSRnmemlnGQSVCPVCGTTL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 449 TEEHKADLLRKYSLELSSIEKEIQEAKALERQLRAEFRKVENELSRLSS-----LKTIADQIIEIRERLS--KINLEDLK 521
Cdd:PRK01156 463 GEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeeinkSINEYNKIESARADLEdiKIKINELK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 522 RDKEEYELLKSESNKLKgeVESLKKEVNELNDYKNESTKLEIE-----IDKAKKELSEIEDRL--LRLGFKTIDE-LSGR 593
Cdd:PRK01156 543 DKHDKYEEIKNRYKSLK--LEDLDSKRTSWLNALAVISLIDIEtnrsrSNEIKKQLNDLESRLqeIEIGFPDDKSyIDKS 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 594 IRELEKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQ--KKYEEKREKMMKL 671
Cdd:PRK01156 621 IREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKsrKALDDAKANRARL 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 672 SMEIKGLETKLEELERRRDEIKSTIEKLKeerkeresakmELEKLNIAIKRIEELRGKiKEYKALIKEEALNKIGEIASE 751
Cdd:PRK01156 701 ESTIEILRTRINELSDRINDINETLESMK-----------KIKKAIGDLKRLREAFDK-SGVPAMIRKSASQAMTSLTRK 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 752 IFSEFtDGKYSGIAIraeDNKVKLFVIYDGVERPLTFLSGGERIALGLAFRLAMSMYLIGKVDLLILDEPTPFLDEERRR 831
Cdd:PRK01156 769 YLFEF-NLDFDDIDV---DQDFNITVSRGGMVEGIDSLSGGEKTAVAFALRVAVAQFLNNDKSLLIMDEPTAFLDEDRRT 844
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 18202079 832 KLIEIMERHLRK---ISQVIIVSHDEELKDAADHVIRIRLEGGASKVEVV 878
Cdd:PRK01156 845 NLKDIIEYSLKDssdIPQVIMISHHRELLSVADVAYEVKKSSGSSKVIPL 894
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-867 |
6.49e-49 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 187.17 E-value: 6.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 1 MKIERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAILVGLYWSKRmrLRGLKKDEFTrTGTRGAIIEITFEED 80
Cdd:PRK02224 1 MRFDRVRLENFKCYADADLRLEDGVTVIHGVNGSGKSSLLEACFFALYGSKA--LDDTLDDVIT-IGAEEAEIELWFEHA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 81 GTKYKVLRDFARnvSYLKRLDGREWRHVTETSMESVSSFIDRI-----IPYNVFLNAIYVRQGQIDA-ILESDETRDKIV 154
Cdd:PRK02224 78 GGEYHIERRVRL--SGDRATTAKCVLETPEGTIDGARDVREEVtellrMDAEAFVNCAYVRQGEVNKlINATPSDRQDMI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 155 KEILNLDKLEKAYDNLGKIRKYIKYSIEEKEKFImktENIEDLI-RTQEKSFTEVLNEIRnisSNLPRLRRELEGIKEE- 232
Cdd:PRK02224 156 DDLLQLGKLEEYRERASDARLGVERVLSDQRGSL---DQLKAQIeEKEEKDLHERLNGLE---SELAELDEEIERYEEQr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 233 ---VKTLEATFNSITELKLRLGELNgkkgRLEERIRQLESGIEEKRKKSKELEEVVKE----LPELEKKETEYRRLIEFK 305
Cdd:PRK02224 230 eqaRETRDEADEVLEEHEERREELE----TLEAEIEDLRETIAETEREREELAEEVRDlrerLEELEEERDDLLAEAGLD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 306 D----EYLVKKNELEKRLGILSNRLQEVKRKI----KDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMR----- 372
Cdd:PRK02224 306 DadaeAVEARREELEDRDEELRDRLEECRVAAqahnEEAESLREDADDLEERAEELREEAAELESELEEAREAVEdrree 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 373 ---LKAQMESLKSKLGGLEPEKINekllyLENRKKELEEEIDKITRKIGELNQ--RSKDRRLAIIELKKARGKCPVCGRE 447
Cdd:PRK02224 386 ieeLEEEIEELRERFGDAPVDLGN-----AEDFLEELREERDELREREAELEAtlRTARERVEEAEALLEAGKCPECGQP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 448 LTEEHKADLLRKYSLELSSIEKEIQEakalerqLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKIN--LEDLKRDKE 525
Cdd:PRK02224 461 VEGSPHVETIEEDRERVEELEAELED-------LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEelIAERRETIE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 526 EYELLKSESNKLKGEVESlkkevnELNDYKNESTKLEIEIDKAKKELSEIEDRLlrlgfktiDELSGRIRELEKFHNKYI 605
Cdd:PRK02224 534 EKRERAEELRERAAELEA------EAEEKREAAAEAEEEAEEAREEVAELNSKL--------AELKERIESLERIRTLLA 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 606 EAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEkvtsqlnELQRKFDQKKYEEKREKMMKLSMEIKGLETKLEEL 685
Cdd:PRK02224 600 AIADAEDEIERLREKREALAELNDERRERLAEKRERKR-------ELEAEFDEARIEEAREDKERAEEYLEQVEEKLDEL 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 686 ERRRDEIKSTIEKLKEERKERESAKMELEKLNIAIKRIEELRGKIKEY-------KALIKEEALNKIGEIASEIFS-EFT 757
Cdd:PRK02224 673 REERDDLQAEIGAVENELEELEELRERREALENRVEALEALYDEAEELesmygdlRAELRQRNVETLERMLNETFDlVYQ 752
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 758 DGKYSGIAIRAEDNkvklFVIYDGVERPL--TFLSGGERIALGLAFRLAMSMYLIGKVD------LLILDEPTPFLDE-- 827
Cdd:PRK02224 753 NDAYSHIELDGEYE----LTVYQKDGEPLepEQLSGGERALFNLSLRCAIYRLLAEGIEgdaplpPLILDEPTVFLDSgh 828
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 18202079 828 -ERRRKLIEIMERHlrKISQVIIVSHDEELKDAADHVIRIR 867
Cdd:PRK02224 829 vSQLVDLVESMRRL--GVEQIVVVSHDDELVGAADDLVRVE 867
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
782-874 |
6.91e-30 |
|
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: 117.71 E-value: 6.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 782 VERPLTFLSGGERIALGLAFRLAMSMYLIGKVDLLILDEPTPFLDEERRR-KLIEIMERHLR-KISQVIIVSHDEELKDA 859
Cdd:cd03240 109 LLDMRGRCSGGEKVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSqKNFQLIVITHDEELVDA 188
|
90
....*....|....*.
gi 18202079 860 ADHVIRIRLEG-GASK 874
Cdd:cd03240 189 ADHIYRVEKDGrQKSR 204
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
259-863 |
4.05e-27 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 117.56 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 259 RLEERIRQLESGIEEKRKK-SKELEEVVKELPELEKKETEYRRLIEFKDEYLVKKNELEKRLGILSNRLQEVkRKIKDAE 337
Cdd:COG4717 50 RLEKEADELFKPQGRKPELnLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 338 SKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRlkaQMESLKSKLGGLEPEKINEKLLYLENRKKELEEEIDKITRKI 417
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEELRELEE---ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 418 GELNQRSKDRRLAIIELKKARGKCPVCGRELTEEHKADLLRKYSLEL-------------SSIEKEIQEAKALERQLRAE 484
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLliaaallallglgGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 485 FRKVENELSRLSSLKTIADQIIEIRERLSKINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDYKNESTKlEIE 564
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-ELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 565 IDKAKKELSEIedrLLRLGFKTIDELSGRIRELEKFHNKYIEAKNAEKELRDILESLKDEREELDKAfeelaKIETDIEK 644
Cdd:COG4717 365 LEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEELEE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 645 VTSQLNELQrkfdqKKYEEKREKMMKLSMEIKGLETKlEELERRRDEIKSTIEKLKEERKERESAKMELEKLNIAIKRIE 724
Cdd:COG4717 437 LEEELEELE-----EELEELREELAELEAELEQLEED-GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 725 ELRgkikeykalikeeaLNKIGEIASEIFSEFTDGKYSGIAIrAEDNKVKLfVIYDGVERPLTFLSGGERIALGLAFRLA 804
Cdd:COG4717 511 EER--------------LPPVLERASEYFSRLTDGRYRLIRI-DEDLSLKV-DTEDGRTRPVEELSRGTREQLYLALRLA 574
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 18202079 805 MSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERhLRKISQVIIVSHDEELKDAADHV 863
Cdd:COG4717 575 LAELLAGEPLPLILDDAFVNFDDERLRAALELLAE-LAKGRQVIYFTCHEELVELFQEE 632
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-145 |
1.08e-25 |
|
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: 105.38 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 3 IERVIVQNFRS-HKNSEIEFKPGINLIIGQNGAGKSSLLDAILVGLYWSKRMRLRGLKKD-EFTRTGTRGAIIEITFEED 80
Cdd:cd03240 1 IDKLSIRNIRSfHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDpKLIREGEVRAQVKLAFENA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18202079 81 -GTKYKVLRDFarnvsylkrldgrewrhvtetsmesvssfidriipyNVFLNAIYVRQGQIDAILE 145
Cdd:cd03240 81 nGKKYTITRSL------------------------------------AILENVIFCHQGESNWPLL 110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-739 |
3.53e-21 |
|
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: 99.76 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 3 IERVIVQNFRSH-KNSEIEFKPGINLIIGQNGAGKSSLLDAIL--VGLYWSKRMRLRGLKKDEFTRTGTRG---AIIEIT 76
Cdd:TIGR02169 2 IERIELENFKSFgKKKVIPFSKGFTVISGPNGSGKSNIGDAILfaLGLSSSKAMRAERLSDLISNGKNGQSgneAYVTVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 77 FEEDGTKYKVLRDFARNV--------SYLKrLDGREWR-----------HVTE-----------TSMESVSSF-----ID 121
Cdd:TIGR02169 82 FKNDDGKFPDELEVVRRLkvtddgkySYYY-LNGQRVRlseihdflaaaGIYPegynvvlqgdvTDFISMSPVerrkiID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 122 RIIPYNVFLNAIYVRQGQIDAILESDETRDKIVKEILN-LDKLEKA------YDNLGKIRKYIKYSIEEKEKFIMKT--E 192
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQqLERLRRErekaerYQALLKEKREYEGYELLKEKEALERqkE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 193 NIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLeaTFNSITELKLRLGELNGKKGRLEERI----RQLE 268
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL--GEEEQLRVKEKIGELEAEIASLERSIaekeRELE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 269 SGIEEKRKKSKELEEVVKELPELEKKETEYR--------RLIEFKDEYLVKKNELE---KRLGILSNRLQEVKRKIKDAE 337
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERkrrdklteEYAELKEELEDLRAELEevdKEFAETRDELKDYREKLEKLK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 338 SK-----------VARIRWIEERLKEIQEKIMKLEPRVREFEDAMRLKA--------QMESLKSKLGGLEPE--KINEKL 396
Cdd:TIGR02169 399 REinelkreldrlQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAleikkqewKLEQLAADLSKYEQElyDLKEEY 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 397 LYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGKCPVCGREL---TEEHKADLLRKYSLELSSI--EKEI 471
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLgsvGERYATAIEVAAGNRLNNVvvEDDA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 472 QEAKALE-----RQLRAEF---RKVENELSRLSSLKT-----IADQIIEIRERLSKI------------NLEDLKRDKEE 526
Cdd:TIGR02169 559 VAKEAIEllkrrKAGRATFlplNKMRDERRDLSILSEdgvigFAVDLVEFDPKYEPAfkyvfgdtlvveDIEAARRLMGK 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 527 YELLKSE-------------SNKLKGEVESLKKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRL------LRLGFKTI 587
Cdd:TIGR02169 639 YRMVTLEgelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLdelsqeLSDASRKI 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 588 DELSGRIRELEKFHNKYIE-AKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYEEKRE 666
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKErLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQA 798
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18202079 667 KMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEKLNIAI-KRIEELRGKIKEYKALIKE 739
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIeKEIENLNGKKEELEEELEE 872
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-186 |
6.99e-20 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 88.91 E-value: 6.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 2 KIERVIVQNFRSHKNSE-IEFKPGINLIIGQNGAGKSSLLDAILVGLYWSKRMRLRglKKDEFTRTGTRGAIIEITFEED 80
Cdd:COG0419 1 KLLRLRLENFRSYRDTEtIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSK--LRSDLINVGSEEASVELEFEHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 81 GTKYKVLRdfarnvsylkrldgrewrhvtetsmesvssfidriipynvflnaiyvRQGQIDAILESD-ETRDKIVKEILN 159
Cdd:COG0419 79 GKRYRIER-----------------------------------------------RQGEFAEFLEAKpSERKEALKRLLG 111
|
170 180
....*....|....*....|....*..
gi 18202079 160 LDKLEKAYDNLGKIRKYIKYSIEEKEK 186
Cdd:COG0419 112 LEIYEELKERLKELEEALESALEELAE 138
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-875 |
2.40e-19 |
|
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: 93.88 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 1 MKIERVIVQNFRSHKNSEIEF---KPGINLIIGQNGAGKSSLLDAILVGLYWSKRMRLRGLK-KDEFTRTGTRGAIIEIT 76
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDftaLGPIFLICGKTGAGKTTLLDAITYALYGKLPRRSEVIRsLNSLYAAPSEAAFAELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 77 FEEDGTKYKVLRDFARNVSYLK------RLDGREWRHVTETS--MESVSSFIDRI--IPYNVFLNAIYVRQGQIDAILES 146
Cdd:TIGR00618 81 FSLGTKIYRVHRTLRCTRSHRKteqpeqLYLEQKKGRGRILAakKSETEEVIHDLlkLDYKTFTRVVLLPQGEFAQFLKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 147 DETRDKIVkeILNLDKLEKaYDNLGKIRKYIKYSIEEK-EKFIMKTENIEDLIRTQEKSFTEVL----NEIRNISSNLPR 221
Cdd:TIGR00618 161 KSKEKKEL--LMNLFPLDQ-YTQLALMEFAKKKSLHGKaELLTLRSQLLTLCTPCMPDTYHERKqvleKELKHLREALQQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 222 LRRELEGIKEEVKTLEATFNSITELKLRLGELNgKKGRLEERIRQLESGIEEKRKK------SKELEEVVKELPEL--EK 293
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRAQEAVLEETQERINRARKAaplaahIKAVTQIEQQAQRIhtEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 294 KETEYRRLIEFKDEYLVKKNELE-KRLGILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMR 372
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSiEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 373 -LKAQMESLKSKLGGLEPEKINEKLLYLENRKKELEEEIDKITRKIGEL--NQRSKDRRLAIIELKKARGKCPvcGRELT 449
Cdd:TIGR00618 397 sLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAaiTCTAQCEKLEKIHLQESAQSLK--EREQQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 450 EEHKADLLRKYSLELSSIEKEIQEAKALERQLRAEFRKVENELSRL---------------------SSLKTIADQIIEI 508
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltrrmqrgeqtyaqleTSEEDVYHQLTSE 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 509 RERLsKINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDY---------------KNESTKLEIEIDKAK---- 569
Cdd:TIGR00618 555 RKQR-ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLteklseaedmlaceqHALLRKLQPEQDLQDvrlh 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 570 ---------KELSEIEDRLLRLGFKTIDELSGRIRELEKfhNKYIEAKNAEKELRDILESLKDEREELDKAFEELAKIET 640
Cdd:TIGR00618 634 lqqcsqelaLKLTALHALQLTLTQERVREHALSIRVLPK--ELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELET 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 641 DIEKVTSQLNELQRKFD----------------QKKYEEKREKMMKLSME----------------------IKGLETKL 682
Cdd:TIGR00618 712 HIEEYDREFNEIENASSslgsdlaaredalnqsLKELMHQARTVLKARTEahfnnneevtaalqtgaelshlAAEIQFFN 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 683 EELERRRDEIKSTIEKLKEERKERESAKM---------------------------------------ELEKLNIAIKRI 723
Cdd:TIGR00618 792 RLREEDTHLLKTLEAEIGQEIPSDEDILNlqcetlvqeeeqflsrleeksatlgeithqllkyeecskQLAQLTQEQAKI 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 724 EELRGKIKEYKALIKEEALNKIGEIASEI------------FSEFTdGKYSGIAIRAEDNKVKLFV---IYDGVERPLTF 788
Cdd:TIGR00618 872 IQLSDKLNGINQIKIQFDGDALIKFLHEItlyanvrlanqsEGRFH-GRYADSHVNARKYQGLALLvadAYTGSVRPSAT 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGERIALGLAFRLAMSMYLIGK----VDLLILDEPTPFLDEERRRKLIEIMERhLRKISQVI-IVSHDEELKDAADHV 863
Cdd:TIGR00618 951 LSGGETFLASLSLALALADLLSTSggtvLDSLFIDEGFGSLDEDSLDRAIGILDA-IREGSKMIgIISHVPEFRERIPHR 1029
|
1050
....*....|..
gi 18202079 864 IRIRLEGGASKV 875
Cdd:TIGR00618 1030 ILVKKTNAGSHV 1041
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
18-758 |
1.77e-18 |
|
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: 90.89 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 18 EIEFKPGINLIIGQNGAGKSSLLDAILVGLYWSKRMRLRGLKKDE--FTRTGTRGAI----IEITFEED-----GTKY-- 84
Cdd:TIGR02168 18 TINFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDviFNGSETRKPLslaeVELVFDNSdgllpGADYse 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 85 -KVLRDFARNVSYLKRLDGREWR--HVTETSMES---VSSFidriipynvflnAIyVRQGQIDAILES-DETRDKIvkei 157
Cdd:TIGR02168 98 iSITRRLYRDGESEYFINGQPCRlkDIQDLFLDTglgKRSY------------SI-IEQGKISEIIEAkPEERRAI---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 158 lnldkLEKAydnlGKIRKYiKYSIEEKEKFIMKTEniEDLIRTQEksfteVLNEIRnisSNLPRLRRELEG------IKE 231
Cdd:TIGR02168 161 -----FEEA----AGISKY-KERRKETERKLERTR--ENLDRLED-----ILNELE---RQLKSLERQAEKaerykeLKA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 232 EVKTLEATF--NSITELKLRLGELNGKKGRLEERIRQLESGIEEKrkkSKELEEVVKELPELEKKETEYR---------- 299
Cdd:TIGR02168 221 ELRELELALlvLRLEELREELEELQEELKEAEEELEELTAELQEL---EEKLEELRLEVSELEEEIEELQkelyalanei 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 300 -RLIEFKDEYLVKKNELEKRLGILSNRLQEVKRKIKDAESKVARIRWIEERLKE----IQEKIMKLEPRVREFEDAMR-L 373
Cdd:TIGR02168 298 sRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEelesLEAELEELEAELEELESRLEeL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 374 KAQMESLKSKLGGLEPE--KINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGKCPVCGRELTEE 451
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQiaSLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 452 HKADLLRKYSLELSSIEKEIQEAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKIN--LEDLKRDKEEYE- 528
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvLSELISVDEGYEa 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 529 ------------LLKSESNKLKGEVESLKK---------EVNELNDYKNESTKLEI------------EIDKAKKELSE- 574
Cdd:TIGR02168 538 aieaalggrlqaVVVENLNAAKKAIAFLKQnelgrvtflPLDSIKGTEIQGNDREIlkniegflgvakDLVKFDPKLRKa 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 575 IEDRLLRL----GFKTIDELSGRIREL--------EKFHNKYIEAKNAEKELRDILE---SLKDEREELDKAFEELAKIE 639
Cdd:TIGR02168 618 LSYLLGGVlvvdDLDNALELAKKLRPGyrivtldgDLVRPGGVITGGSAKTNSSILErrrEIEELEEKIEELEEKIAELE 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 640 TDIEKVTSQLNELQRKFDQ--KKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMEL-EKL 716
Cdd:TIGR02168 698 KALAELRKELEELEEELEQlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAeEEL 777
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 18202079 717 NIAIKRIEELRGKIKEYKalikeEALNKIGEIASEIFSEFTD 758
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLK-----EELKALREALDELRAELTL 814
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
168-725 |
6.49e-17 |
|
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: 85.88 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 168 DNLGKIRKYIKYSIEEKEKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEATFNS-ITEL 246
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 247 KLRLGELNGKKGRLEERIRQLEsgiEEKRKKSKELEEVVKELPELEKKETEYR--RLIEFKDEYLVKKNELEKRLGILSN 324
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLE---DRRERLQQEIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELRE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 325 RLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRLKAQMESLKSKLGGLEPEKINEKLLYLENRKK 404
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQ 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 405 ELEEEIDKITRKIGELNQRSKDRRLAIIELKKARG-KCPVCGRELTEEHK------------------------------ 453
Cdd:TIGR02168 549 AVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGtEIQGNDREILKNIEgflgvakdlvkfdpklrkalsyllggvlvv 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 454 ------ADLLRKYSL----------------------------------ELSSIEKEIQEAKALERQLRAEFRKVENELS 493
Cdd:TIGR02168 629 ddldnaLELAKKLRPgyrivtldgdlvrpggvitggsaktnssilerrrEIEELEEKIEELEEKIAELEKALAELRKELE 708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 494 RLSSLKTIADQIIEIRERLSKINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDYKNESTKLEIEIDKAKKELS 573
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 574 E-IEDRLLRLGF--KTIDELSGRIREL-EKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQL 649
Cdd:TIGR02168 789 AqIEQLKEELKAlrEALDELRAELTLLnEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18202079 650 NELQRKFD--QKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKstiEKLKEERKERESAKMELEKLNIAIKRIEE 725
Cdd:TIGR02168 869 EELESELEalLNERASLEEALALLRSELEELSEELRELESKRSELR---RELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
241-597 |
1.34e-15 |
|
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: 81.64 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 241 NSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELpeLEKKETEYRRLIEFKDEYLVKKNELEKRLG 320
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL--RKELEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 321 ILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDamrlkaQMESLKSKLGGLEPEK--INEKLLY 398
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE------ELKALREALDELRAELtlLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 399 LENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGKCPVCGRELTEEHKA----------------DLLRKYSL 462
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasleealallrSELEELSE 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 463 ELSSIEKEIQEAKALERQLRAEFRKVENELSRLSSlktiadQIIEIRERLS---KINLEDLkrdKEEYELLKSESNKLKG 539
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEV------RIDNLQERLSeeySLTLEEA---EALENKIEDDEEEARR 972
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18202079 540 EVESLKKEVNEL--------NDYKNESTKLEiEIDKAKKELSEIEDRLLrlgfKTIDELSGRIREL 597
Cdd:TIGR02168 973 RLKRLENKIKELgpvnlaaiEEYEELKERYD-FLTAQKEDLTEAKETLE----EAIEEIDREARER 1033
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
155-761 |
2.64e-15 |
|
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: 80.45 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 155 KEILNLDKLEKAYDNLGKIRKYIKYSIEEKEKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVK 234
Cdd:TIGR04523 90 KLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 235 TLEATFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEevvKELPELEKKETEYRRLIEFKDEYLVKK-- 312
Cdd:TIGR04523 170 ELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLE---SQISELKKQNNQLKDNIEKKQQEINEKtt 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 313 --NELEKRLGILSNRLQEVKRKIKDAESKvarirwieerLKEIQEKIMKLEPRVREfedamrLKAQMESLKSKLGGLEPE 390
Cdd:TIGR04523 247 eiSNTQTQLNQLKDEQNKIKKQLSEKQKE----------LEQNNKKIKELEKQLNQ------LKSEISDLNNQKEQDWNK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 391 KINEKLLYLENRKKELEEEIDKITRKIGELNQRskdrrlaIIELKKARGkcpvcGRELTEEHKADLLRKYSLELSSIEKE 470
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ-------ISQLKKELT-----NSESENSEKQRELEEKQNEIEKLKKE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 471 IQEAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNE 550
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 551 LNDYKnesTKLEIEIDKAKKELSEIEDRLLrlgfKTIDELSGRIRELEKFHNKYIEAKNAEKELRDILESLKDEREELDK 630
Cdd:TIGR04523 459 LDNTR---ESLETQLKVLSRSINKIKQNLE----QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 631 afeELAKIETDIEKVTSQLNELQRKFDQKKYE----EKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEE---- 702
Cdd:TIGR04523 532 ---EKKEKESKISDLEDELNKDDFELKKENLEkeidEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEieek 608
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18202079 703 -------RKERESAKMELEKLNIAIKRIEELRGKIKEYKALIKEEaLNKIGEIASEIFSEFTDGKY 761
Cdd:TIGR04523 609 ekkisslEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET-IKEIRNKWPEIIKKIKESKT 673
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-715 |
4.28e-15 |
|
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: 79.68 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 168 DNLGKIRKYIKYSIEEKEKfimKTENIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEAtfnSITELK 247
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEK---ELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS---DLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 248 LRLGELNGKKGRLEERIRQLESGIEE-KRKKSKELEEVVKELPELEKKETEYRRLIEFKDEYLVKKNELEKRLGILSNRL 326
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKEnKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 327 QEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREfedamrLKAQMESLKSKLGGLEpEKINEKLLYLENRKKEL 406
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQ------LKDNIEKKQQEINEKT-TEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 407 EEEIDKITRKIGELNQRSKdrrlAIIELKKARGKCPVCGRELTEEHKADLLRKYSLELSSIEKEIqeakaleRQLRAEFR 486
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNK----KIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL-------EEIQNQIS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 487 KVENELSRLSslktiaDQIIEIRERLSKINLEDLKRDKE------EYELLKSESNKLKGEVESLKKEVNELN----DYKN 556
Cdd:TIGR04523 332 QNNKIISQLN------EQISQLKKELTNSESENSEKQREleekqnEIEKLKKENQSYKQEIKNLESQINDLEskiqNQEK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 557 ESTKLEIEIDKAKKELSEIEDRLLRLGfKTIDELSGRIRELEKfhnkyieaKNAEKELrdILESLKDEREELDKafeELA 636
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLK-ETIIKNNSEIKDLTN--------QDSVKEL--IIKNLDNTRESLET---QLK 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18202079 637 KIETDIEKVTSQLNELQRKFDQKKYEEKrekmmKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEK 715
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELK-----KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
369-875 |
8.12e-15 |
|
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: 78.96 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 369 DAMRLKAQMESLKSKLGGLEPEK--INEKLLYLENRKKELEEEIDKITRKIGEL----NQRSKDRRLAIIELKKARGKCP 442
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELssLQSELRRIENRLDELSQELSDASRKIGEIekeiEQLEQEEEKLKERLEELEEDLS 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 443 VCGRELTE-----EHKADLLRKYSLELSSIEKEIQEAKALE-----RQLRAEFRKVENELSRLSSlktiadQIIEIRERL 512
Cdd:TIGR02169 748 SLEQEIENvkselKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEA------RLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 513 SKINLEDLKRDKEEYELlKSESNKLKGEVESLKKEVNELNDYKNEstkLEIEIDKAKKELSEIEDRLLRLGfKTIDELSG 592
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQEL-QEQRIDLKEQIKSIEKEIENLNGKKEE---LEEELEELEAALRDLESRLGDLK-KERDELEA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 593 RIRELEkfhNKYIEAKNAEKELRDILESLKDEREELdkaFEELAKIETDI-EKVTSQLNELQRKFDQKKYEEKREKMMKL 671
Cdd:TIGR02169 897 QLRELE---RKIEELEAQIEKKRKRLSELKAKLEAL---EEELSEIEDPKgEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 672 SMEIKGLETKLEELERRRDEIKSTIEKLKEERKEresakmeleklniAIKRIEELRGKIKEykalIKEEALNKIGEIASE 751
Cdd:TIGR02169 971 EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA-------------ILERIEEYEKKKRE----VFMEAFEAINENFNE 1033
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 752 IFSEFTDGKYSGIAIRAED---NKVKLFVIYDGVE-RPLTFLSGGERIALGLAFRLAMSMYLigKVDLLILDEPTPFLDE 827
Cdd:TIGR02169 1034 IFAELSGGTGELILENPDDpfaGGLELSAKPKGKPvQRLEAMSGGEKSLTALSFIFAIQRYK--PSPFYAFDEVDMFLDG 1111
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 18202079 828 ERRRKLIEiMERHLRKISQVIIVSHDEELKDAADHVIRIRL-EGGASKV 875
Cdd:TIGR02169 1112 VNVERVAK-LIREKAGEAQFIVVSLRSPMIEYADRAIGVTMrRNGESQV 1159
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1-735 |
1.78e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.03 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 1 MKIERVIVQN---FrsHKNSEIEFKPGINLIIGQNGAGKSSLLDAILVGLYWSKRMRL----RGLKKDEFT-RTGTRGAI 72
Cdd:COG4913 1 FRLQRLQLINwgtF--DGVHTIDFDGRGTLLTGDNGSGKSTLLDAIQTLLVPAKRPRFnkaaNDAGKSDRTlLSYVRGKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 73 IEITfEEDGTKYKVLRDFArNVSYL-----KRLDGRE-------WRHVTETSMESVSSFidRIIPynvflnaiyvRQGQI 140
Cdd:COG4913 79 GSER-DEAGTRPVYLRPGD-TWSAIaatfaNDGSGQTvtlaqvfWLKGDASSLGDVKRF--FVIA----------DGPLD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 141 DAILESDETRdkivkeiLNLDKLEKAYDNLG--KIRKYIKYSIEEKEKFIMKTE----------------NIEDLIRTQ- 201
Cdd:COG4913 145 LEDFEEFAHG-------FDIRALKARLKKQGveFFDSFSAYLARLRRRLGIGSEkalrllhktqsfkpigDLDDFVREYm 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 202 -EKsfTEVLNEIRNISSN---LPRLRRELEGIKEEVKTLEAtfnsITELKLRLGELNGKKGRLEERIRQLEsgIEEKRKK 277
Cdd:COG4913 218 lEE--PDTFEAADALVEHfddLERAHEALEDAREQIELLEP----IRELAERYAAARERLAELEYLRAALR--LWFAQRR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 278 SKELEEVVKEL-PELEKKETEYRRLIEFKDEYLVKKNELEKRL-GILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQE 355
Cdd:COG4913 290 LELLEAELEELrAELARLEAELERLEARLDALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 356 KI-MKLEPRVREFEDAMR-LKAQMESLKSKLGGLEPE--KINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAI 431
Cdd:COG4913 370 ALgLPLPASAEEFAALRAeAAALLEALEEELEALEEAlaEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 432 IE-LKKARGKCPVCGrEL---------------------------TEEHKADLLRKY-------------------SLEL 464
Cdd:COG4913 450 AEaLGLDEAELPFVG-ELievrpeeerwrgaiervlggfaltllvPPEHYAAALRWVnrlhlrgrlvyervrtglpDPER 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 465 SSIEK-------EIQEAKA---LERQLRAEF--RKVEN--ELSRLSSLKTIADQIIEIRERLSKinlEDLKRDKEEYELl 530
Cdd:COG4913 529 PRLDPdslagklDFKPHPFrawLEAELGRRFdyVCVDSpeELRRHPRAITRAGQVKGNGTRHEK---DDRRRIRSRYVL- 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 531 kSESNKLKgeVESLKKEVNELNDyknestkleiEIDKAKKELSEIEDRLlrlgfKTIDELSGRIRELEKFHNKYIEAKNA 610
Cdd:COG4913 605 -GFDNRAK--LAALEAELAELEE----------ELAEAEERLEALEAEL-----DALQERREALQRLAEYSWDEIDVASA 666
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 611 EKELRDilesLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDqkkyeEKREKMMKLSMEIKGLETKLEELERRRD 690
Cdd:COG4913 667 EREIAE----LEAELERLDASSDDLAALEEQLEELEAELEELEEELD-----ELKGEIGRLEKELEQAEEELDELQDRLE 737
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18202079 691 EIKSTI---------EKLKEERKERESAKM------ELEKLNIAIKRIE-ELRGKIKEYKA 735
Cdd:COG4913 738 AAEDLArlelralleERFAAALGDAVERELrenleeRIDALRARLNRAEeELERAMRAFNR 798
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
767-874 |
5.63e-14 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 70.47 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 767 RAEDNKVKLFVIYDGVERPLTF--LSGGERIALGLAFRLAMSmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKI 844
Cdd:cd03227 54 RRSGVKAGCIVAAVSAELIFTRlqLSGGEKELSALALILALA--SLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKG 131
|
90 100 110
....*....|....*....|....*....|.
gi 18202079 845 SQVIIVSHDEELKDAADHVIRI-RLEGGASK 874
Cdd:cd03227 132 AQVIVITHLPELAELADKLIHIkKVITGVYK 162
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
789-867 |
7.51e-14 |
|
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: 69.97 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGERialglaFRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHD-EELKDAADHVIRIR 867
Cdd:cd00267 81 LSGGQR------QRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVLK 154
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-732 |
7.52e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 7.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 198 IRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEAtfnSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKK 277
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRL---ELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 278 SKELEEVVKEL-PELEKKETEYRRLIEFKDEYLVKKNELEKRLGILSNRLQEVKRKIKDAESkvARIRWIEERLKEIQEK 356
Cdd:COG1196 311 RRELEERLEELeEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA--ELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 357 IMKLEPRVREFEDAMRLKAQMESLKSKLGGLEPEK--INEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIEL 434
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELeeLEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 435 KKARGKCPVCGRELTEEHKADLLRKYSLELSSIEKEIQEAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRE--RL 512
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaAL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 513 SKINLEDLKRDKEEYELLKSE---------SNKLKGEVESLKKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLG 583
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 584 FKTIDELSGRIREL-EKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYE 662
Cdd:COG1196 629 AARLEAALRRAVTLaGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 663 EKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEKLNIAIKRIEELRGKIKE 732
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
261-745 |
8.63e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.95 E-value: 8.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 261 EERIRQLESGIEEKRKKSKELEEVVKELPELEKKETEYRRLIEFKDEYLVKKNELEKRLGILSN----------RLQEVK 330
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeekkkadeaKKAEEK 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 331 RKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRlKAQMESLKSKLGGLEPEKINEKLLYLENRKKELEEEI 410
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK-AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 411 DKI------TRKIGELNQRSKDRRLAIIELKKA---RGKCPVCGRELTEEHKADLLRKYSLELSSIEKEIQEA----KAL 477
Cdd:PTZ00121 1381 DAAkkkaeeKKKADEAKKKAEEDKKKADELKKAaaaKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAeeakKAE 1460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 478 ERQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKiNLEDLKRDKEEY----ELLKSESNKLKGEVESLKKEVNELND 553
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKK-KADEAKKAAEAKkkadEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 554 YKNESTKLEIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIRELEKFhnKYIEAKNAEKELRDILESLKDEREELDKAFE 633
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA--KKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 634 ELAKIETdiekvTSQLNELQRKFDQ--KKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKM 711
Cdd:PTZ00121 1618 AKIKAEE-----LKKAEEEKKKVEQlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
490 500 510
....*....|....*....|....*....|....*...
gi 18202079 712 ELEKLNIAIKRIEELRGKIKEYK----ALIKEEALNKI 745
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKkkaeELKKAEEENKI 1730
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
192-755 |
1.20e-13 |
|
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: 75.15 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 192 ENIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEATFNSitelklRLGELNGKKGRLEERIRqlesgi 271
Cdd:pfam15921 267 DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR------QLSDLESTVSQLRSELR------ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 272 EEKRKKSKELEEVVKELPELEKKETEYR-RLIEFKDEYLVKKNELEKRLGILSNRLQEVKrkikdAESKVARIRWIEERL 350
Cdd:pfam15921 335 EAKRMYEDKIEELEKQLVLANSELTEARtERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLWDRDTG 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 351 KEIQEKIMKLEPRVREFEdAMRLKAQMESLKSKLGGlepeKINEKLLYLENRKKELEeeidKITRKIGELNQRSKDRRLA 430
Cdd:pfam15921 410 NSITIDHLRRELDDRNME-VQRLEALLKAMKSECQG----QMERQMAAIQGKNESLE----KVSSLTAQLESTKEMLRKV 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 431 IIELKkargkcpvcGRELTEEHKADLLRKYSLELSSIEKEIQEAKALERQLRAefrKVENELSRLSSLKTIADQIIEIRE 510
Cdd:pfam15921 481 VEELT---------AKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRS---RVDLKLQELQHLKNEGDHLRNVQT 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 511 RLSKINLEDLKRDKEeYELLKSEsnklkgeVESLKKEVNElndykNESTKLEIEIDKAKKElSEIEDRLLRLG-FKTI-D 588
Cdd:pfam15921 549 ECEALKLQMAEKDKV-IEILRQQ-------IENMTQLVGQ-----HGRTAGAMQVEKAQLE-KEINDRRLELQeFKILkD 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 589 ELSGRIRELE-KFHNKYIEAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKyEEKREK 667
Cdd:pfam15921 615 KKDAKIRELEaRVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS-EEMETT 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 668 MMKLSMEIKGLETkleELERRRDEIKS-------TIEKLKEERKERESAKMELEKLNIAIKRIEELRGKIKEYKALIKEE 740
Cdd:pfam15921 694 TNKLKMQLKSAQS---ELEQTRNTLKSmegsdghAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEE 770
|
570
....*....|....*
gi 18202079 741 AlNKIGEIASEIFSE 755
Cdd:pfam15921 771 K-NKLSQELSTVATE 784
|
|
| YydB |
COG5293 |
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown]; |
18-435 |
1.33e-13 |
|
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown];
Pssm-ID: 444096 [Multi-domain] Cd Length: 572 Bit Score: 74.60 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 18 EIEFKPGINLIIGQ-----------NGAGKSSLLDAILVGLyWSKRMRLRGLKKDEFTRTGTrgaiIEITFEEDGTKYKV 86
Cdd:COG5293 15 PIEFNPGLNVILGEisspendkdstNGVGKSTLLELIDFCL-GADKDKKRFLKHEDELGDHT----FFLEFELDGKDLTI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 87 LRDFARNVSYLKRLDGREWRHVtETSMESVSSFIDRIIPYNVFLNAIYVRQ----------GQIDAILESDETRDKIVKE 156
Cdd:COG5293 90 RRSVSDPKKISLCGDGYEWDHE-KVSLEEAKALLEELLFGLPALKGPSFRSllgyflrrqgDDFKDPLQLFSTAQKDADW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 157 ILNLDKLEKAYDNLGKIRKYIKYSIEEKEKFIMKTEniEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIkEEVKTL 236
Cdd:COG5293 169 KLYLAYLLGLDWDLAAEKYELKEEIKELKKLRKALK--DELIGSVVKSISELRAEILELEEEIEKLEKDLEKF-DVAENY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 237 EATFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKS-----KELEEVVKELPELEKKETE-----YRRLIEFKD 306
Cdd:COG5293 246 EELEKELDELKREINELRNERYSLERRLKKIERSLEEEIDIDpdeleKLYEEAGVFFPDQVKKRFEeveafHKSIVENRR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 307 EYLVK-KNELEKRLGILSNRLQEVKRKIKDAESKVARIRWIEErLKEIQEKIMKLEPRVREFEDAMRLKAQMESLKSKLG 385
Cdd:COG5293 326 EYLEEeIAELEAELEELEAELAELGKERAELLSLLDSKGALDK-YKELQEELAELEAELEELESRLEKLQELEDEIRELK 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 18202079 386 GLEPEKINEKLLYLENRKkeleEEIDKITRKIGELNQRSKDRRLAIIELK 435
Cdd:COG5293 405 EERAELKEEIESDIEERK----ELLDEINKLFSEIVEELYGNRKASLSIE 450
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
217-732 |
1.87e-13 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 74.87 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 217 SNLPRLRRELEGIKEEVKTLEATFNSITElklrlgELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPE--LEKK 294
Cdd:pfam12128 347 EQLPSWQSELENLEERLKALTGKHQDVTA------KYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEddLQAL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 295 ETEYRrliefkDEYLVKKNELEKRLGILSNRLQEVKRKIKDA---ESKVARIRWIEERLKEIQEKimkLEPRVREFEDAM 371
Cdd:pfam12128 421 ESELR------EQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREE---QEAANAEVERLQ 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 372 RLKAQMESLKSKlgglEPEKINEKLLYLENRKKELEEEIDKITRKIGEL----NQRSKDRRLAIIEL--KKARGKCPVcG 445
Cdd:pfam12128 492 SELRQARKRRDQ----ASEALRQASRRLEERQSALDELELQLFPQAGTLlhflRKEAPDWEQSIGKVisPELLHRTDL-D 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 446 RELTEEHKADLLRKYSLELSSIEKEIQEAKALERQLRAEFRKVENEL-SRLSSLKTIADQIIEIRERLSKINLEdLKRDK 524
Cdd:pfam12128 567 PEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALqSAREKQAAAEEQLVQANGELEKASRE-ETFAR 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 525 EEYELLKSESNKLKGEVESLKKEVNElndyknestKLEIEIDKAKKELSEIEDRLLRLGFKTIDELsgrirelEKFHNKY 604
Cdd:pfam12128 646 TALKNARLDLRRLFDEKQSEKDKKNK---------ALAERKDSANERLNSLEAQLKQLDKKHQAWL-------EEQKEQK 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 605 IEAKNAEKELRDILESLKDEREELDKAfeELAKIETDIEKVTSQLNElQRKFDQKKYEEKREKMMKLSMEIKGLETKLEE 684
Cdd:pfam12128 710 REARTEKQAYWQVVEGALDAQLALLKA--AIAARRSGAKAELKALET-WYKRDLASLGVDPDVIAKLKREIRTLERKIER 786
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 18202079 685 LERRRDEIKSTIEKLKEE-RKERESAKMELEKLNIAIKRIEELRGKIKE 732
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQETwLQRRPRLATQLSNIERAISELQQQLARLIA 835
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
256-751 |
3.90e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.02 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 256 KKGRLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKETEYRRLIEFKDEYLVKKNELEKRLGilSNRLQEVKRKIKD 335
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE--DAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 336 AesKVARIRWIEERLKEIQEKIMKLEPR----VREFEDAMRL----KAQMESLKSKLGGLEPEKINEKLLYLENRKKELE 407
Cdd:PTZ00121 1163 A--RKAEEARKAEDAKKAEAARKAEEVRkaeeLRKAEDARKAeaarKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 408 E-------EIDKITRKIGELNQRSKDRRLAIIELKKARGKCPVcgRELTEEHKADLLRKYS--LELSSIEKEIQEAKALE 478
Cdd:PTZ00121 1241 EakkaeeeRNNEEIRKFEEARMAHFARRQAAIKAEEARKADEL--KKAEEKKKADEAKKAEekKKADEAKKKAEEAKKAD 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 479 --RQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKINLEDLKRDKEEYELLKSESNKL----------KGEVESLKK 546
Cdd:PTZ00121 1319 eaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKadaakkkaeeKKKADEAKK 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 547 EVNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIRELEKFHNKYIEAKNAEK--ELRDILESLKDE 624
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKkaEEAKKADEAKKK 1478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 625 REELDKAfEELAKIETDIEKVTSQLN---ELQRKFDQ-KKYEEKR--EKMMKLSMEIKGLETKLEELERRRDEIKSTIE- 697
Cdd:PTZ00121 1479 AEEAKKA-DEAKKKAEEAKKKADEAKkaaEAKKKADEaKKAEEAKkaDEAKKAEEAKKADEAKKAEEKKKADELKKAEEl 1557
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 18202079 698 KLKEERKERESAKMELEKLNIAIKRIEELR----GKIKEYKALIKEEALNKIGEIASE 751
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaeeARIEEVMKLYEEEKKMKAEEAKKA 1615
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
225-715 |
4.74e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.64 E-value: 4.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 225 ELEGIKEEVKTLEATFNSITELKLRLGELngkKGRLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKETEYRRlief 304
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAA---KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK---- 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 305 KDEYLVKKNELEKRLGILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQE--KIMKLEPRVREFEDAMRLKAQMESLK- 381
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEAKKADEAKKKAEEAKk 1458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 382 ---SKLGGLEPEKINEKLLYLENRKK--ELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGKCPVCGRELTEEHKADL 456
Cdd:PTZ00121 1459 aeeAKKKAEEAKKADEAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 457 LRKYSLELSSIE-KEIQEAKALERQLRAEFRKVENELSRLSSLKT-IADQIIEIRERLSKINLEDLKRDKEEyELLKSES 534
Cdd:PTZ00121 1539 AKKAEEKKKADElKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAeEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEE 1617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 535 NKLKGE----VESLKKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIRELEKFHNKYIEAKNA 610
Cdd:PTZ00121 1618 AKIKAEelkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 611 EKELRDILESLKDEREELDKAfEELAKIEtdiEKVTSQLNELQRKFDQKKyeEKREKMMKLSMEIKGLETKLEELERRRD 690
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKA-EELKKAE---EENKIKAEEAKKEAEEDK--KKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
490 500
....*....|....*....|....*..
gi 18202079 691 EIKSTIEKLKEE--RKERESAKMELEK 715
Cdd:PTZ00121 1772 EIRKEKEAVIEEelDEEDEKRRMEVDK 1798
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
223-784 |
5.91e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 223 RRELEGIKEEVKTLEATFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELE--EVVKELPELEKKETEYRR 300
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKkaEEKKKADEAKKKAEEAKK 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 301 LIEFKDeylvKKNELEKRLGILSNRLQEVKRKI----KDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRLKAQ 376
Cdd:PTZ00121 1317 ADEAKK----KAEEAKKKADAAKKKAEEAKKAAeaakAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 377 MESLKSKlgGLEPEKINEKLLYLENRKKELEEEIDKI--TRKIGELNQRSKDRRLAIIELKKA--RGKCPVCGRELTEEH 452
Cdd:PTZ00121 1393 ADEAKKK--AEEDKKKADELKKAAAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAeeAKKAEEAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 453 KADLLRKYSLELSSIEKEIQEAKalerqlraEFRKVENELSRLSSLKTIADQIIEIRERLSKINLEDLKRDKEEYELLKS 532
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAE--------EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 533 ESNKLKGEV---ESLKK--EVNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIRELEKFHNKYIEA 607
Cdd:PTZ00121 1543 EEKKKADELkkaEELKKaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 608 KNAEK--ELRDILESLKDEREELDKAFEELAKIEtdiekvtsQLNELQRKFDQKKYEEKREKMMKLSMEIKGLETKLEEL 685
Cdd:PTZ00121 1623 EELKKaeEEKKKVEQLKKKEAEEKKKAEELKKAE--------EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 686 ERRRDEIKSTIEKLKEERKERESAKMELEKLNIAIKRIEELRGKIKEYK-----ALIKEEALNKIGEIASEIFSEFTDGK 760
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKkkaeeAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
570 580
....*....|....*....|....
gi 18202079 761 YSGIAIRAEDNKVKLFVIYDGVER 784
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
399-862 |
6.98e-13 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 72.46 E-value: 6.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 399 LENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGK------CPVCGRELTEEHKADLLRKYSLELSSIEKEIQ 472
Cdd:COG4694 104 LEEEIEELEKEIEDLKKELDKLEKELKEAKKALEKLLEDLAKsikddlKKLFASSGRNYRKANLEKKLSALKSSSEDELK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 473 EAKaleRQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKIN-LEDLKRDKEEY----------ELLKSESNK----- 536
Cdd:COG4694 184 EKL---KLLKEEEPEPIAPITPLPDLKALLSEAETLLEKSAVSSaIEELAALIQNPgnsdwveqglAYHKEEEDDtcpfc 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 537 LKGEVESLKKEVNEL--NDYKNESTKLEI---EIDKAKKELSEIEDRLLRLGFKTI-DELSGRIRELEKFHNKYIEAknA 610
Cdd:COG4694 261 QQELAAERIEALEAYfdDEYEKLLAALKDlleELESAINALSALLLEILRTLLPSAkEDLKAALEALNALLETLLAA--L 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 611 EKELRDILESLKDEREELdkaFEELAKIETDIEKVTSQLNELQRKFDQKKyEEKREKMMKLsmeikgletKLEELERRRD 690
Cdd:COG4694 339 EEKIANPSTSIDLDDQEL---LDELNDLIAALNALIEEHNAKIANLKAEK-EEARKKLEAH---------ELAELKEDLS 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 691 EIKSTIEKLKEERKERESAKMELEKLNIAIKRIEELRGKIKEYKALIKEEaLNKIGeiaseifseftdgkYSGIAIRAED 770
Cdd:COG4694 406 RYKAEVEELIEELKTIKALKKALEDLKTEISELEAELSSVDEAADEINEE-LKALG--------------FDEFSLEAVE 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 771 NKVKLFVIY---DGVERPLTFLSGGERIALGLAFRLAMsmyLIGKVD-----LLILDEPTPFLDEERRRKLIEIMERHLR 842
Cdd:COG4694 471 DGRSSYRLKrngENDAKPAKTLSEGEKTAIALAYFLAE---LEGDENdlkkkIVVIDDPVSSLDSNHRFAVASLLKELSK 547
|
490 500
....*....|....*....|....
gi 18202079 843 KISQVIIVSHDE----ELKDAADH 862
Cdd:COG4694 548 KAKQVIVLTHNLyflkELRDLADE 571
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-195 |
8.57e-13 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 69.64 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 1 MKIERVIVQNFRSHKNSEIEF--KPGINLIIGQNGAGKSSLLDAILVGLYWSkrmrLRGLKKDEFTRtgtrgaiIEITFE 78
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEIDFdnPPRLTVLVGENGSGKTTLLEAIALALSGL----LSRLDDVKFRK-------LLIRNG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 79 EDGTKYKVLRDF--ARNVSYLKRLDGREWRHVTETSMESVSSFIDRIIPYNVFLNaiYVRQGQIDAILESDETRDKIVKE 156
Cdd:COG3950 70 EFGDSAKLILYYgtSRLLLDGPLKKLERLKEEYFSRLDGYDSLLDEDSNLREFLE--WLREYLEDLENKLSDELDEKLEA 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 18202079 157 ILNLdkLEKAYDNLgkirKYIKYSIEEKEKFIMKTENIE 195
Cdd:COG3950 148 VREA--LNKLLPDF----KDIRIDRDPGRLVILDKNGEE 180
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-86 |
1.05e-12 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 70.57 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 2 KIERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAIlvglYWSKRMR-LRGLKKDEFTRTGTRGAIIEITFEED 80
Cdd:COG1195 1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAI----YLLATGRsFRTARDAELIRFGADGFRVRAEVERD 76
|
....*.
gi 18202079 81 GTKYKV 86
Cdd:COG1195 77 GREVRL 82
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
3-81 |
1.08e-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: 67.62 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 3 IERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAILVGLYWSKRMRLRG--LKKdeFTRTGTRGAIIEITFEED 80
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGssLKD--LIKDGESSAKITVTLKNQ 78
|
.
gi 18202079 81 G 81
Cdd:cd03276 79 G 79
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
323-852 |
2.37e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 323 SNRLQEVKRKIKDAESKVARIrwiEERLKEIQEKIMKLEPRVREFEDAMR-LKAQMESLKSKLGGLEpekinEKLLYLEN 401
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEEL---EEKIAELEKALAELRKELEELEEELEqLRKELEELSRQISALR-----KDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 402 RKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARgkcpvcgrELTEEHKADL---LRKYSLELSSIEKEIQEAKALE 478
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL--------AEAEAEIEELeaqIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 479 RQLRAEFRKVENELSRLssLKTIADQIIEIRErlskinledlkrdkeeyelLKSESNKLKGEVESLKKEVNELNDYKNEs 558
Cdd:TIGR02168 813 TLLNEEAANLRERLESL--ERRIAATERRLED-------------------LEEQIEELSEDIESLAAEIEELEELIEE- 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 559 tkLEIEIDKAKKELSEIEDRLLRLGFKtIDELSGRIRELEKfhnkyieaknAEKELRDILESLKDEREELDkafEELAKI 638
Cdd:TIGR02168 871 --LESELEALLNERASLEEALALLRSE-LEELSEELRELES----------KRSELRRELEELREKLAQLE---LRLEGL 934
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 639 ETDIEKVTSQLNELQR---KFDQKKYEEKREKMMKLSMEIKGLETKL--------------EELERRRDEIKSTIEKLKE 701
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSltlEEAEALENKIEDDEEEARRRLKRLENKIkelgpvnlaaieeyEELKERYDFLTAQKEDLTE 1014
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 702 ERKERESAkmeLEKLNIAIKrieelrgkiKEYKalikeEALNKIGEIASEIFSEFTDGKYSGIAIRAEDNkvklfVIYDG 781
Cdd:TIGR02168 1015 AKETLEEA---IEEIDREAR---------ERFK-----DTFDQVNENFQRVFPKLFGGGEAELRLTDPED-----LLEAG 1072
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 782 VE----------RPLTFLSGGERIALGLAfrLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMeRHLRKISQVIIVS 851
Cdd:TIGR02168 1073 IEifaqppgkknQNLSLLSGGEKALTALA--LLFAIFKVKPAPFCILDEVDAPLDDANVERFANLL-KEFSKNTQFIVIT 1149
|
.
gi 18202079 852 H 852
Cdd:TIGR02168 1150 H 1150
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
479-740 |
4.62e-12 |
|
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: 70.10 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 479 RQLRAEFRKVENELSRLSSLKTIADQIIEI--RERLSKINLEDLKRDKEEYELlKSESNKLKGEVESLKKEVNELNDYKN 556
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERlrREREKAERYQALLKEKREYEG-YELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 557 ESTKLEIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIREL-EKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEEL 635
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 636 AKIETDIEKVTSQLNELQRKFDQ--KKYEEKREKMMKLSMEIKGLETKLEELerrRDEIKSTIEKLKEERKERESAKMEL 713
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKltEEYAELKEELEDLRAELEEVDKEFAET---RDELKDYREKLEKLKREINELKREL 408
|
250 260
....*....|....*....|....*..
gi 18202079 714 EKLNIAIKRIEELRGKIKEYKALIKEE 740
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNAAIAGIEAK 435
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-186 |
5.06e-12 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 65.60 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 6 VIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAILVGLYWSKRMRLRGLKKD------EFTRTGTRGAIIEITFEE 79
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGfvkgdiRIGLEGKGKAYVEITFEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 80 DGTKYKVLRDFARNVSYLKRLDGREwRHVTETSMESVSSFIDRIIPYNVFLNAIYVRQGQIDAILESDETRDKivkeilN 159
Cdd:pfam13476 81 NDGRYTYAIERSRELSKKKGKTKKK-EILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKEKKE------R 153
|
170 180
....*....|....*....|....*..
gi 18202079 160 LDKLEKAYDNLGKIRKYIKYSIEEKEK 186
Cdd:pfam13476 154 LEELEKALEEKEDEKKLLEKLLQLKEK 180
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
146-749 |
6.79e-12 |
|
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: 69.70 E-value: 6.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 146 SDETRDKIVK--EILNLDKLEKAYDNLGKIRKyikysIEEKekfiMKTENIEDLIRTQEKSFTEVLN----EIRNISSNL 219
Cdd:TIGR01612 1057 IDEIEKEIGKniELLNKEILEEAEINITNFNE-----IKEK----LKHYNFDDFGKEENIKYADEINkikdDIKNLDQKI 1127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 220 PRLRRELEGIKEEVKtleatfNSITELKLRLGEL---------NGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPE 290
Cdd:TIGR01612 1128 DHHIKALEEIKKKSE------NYIDEIKAQINDLedvadkaisNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAE 1201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 291 LEKKETEYRRLIEFKDEYlvkknelEKRLGILSnrLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEprvREFEDA 370
Cdd:TIGR01612 1202 IEKDKTSLEEVKGINLSY-------GKNLGKLF--LEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIE---NEMGIE 1269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 371 MRLKAQMESL-----KSKLGGLEPEKINEKLLYLENRKKELEEEIDKITrkigELNQRSKDRRLAIIELKKARGKCPVCG 445
Cdd:TIGR01612 1270 MDIKAEMETFnishdDDKDHHIISKKHDENISDIREKSLKIIEDFSEES----DINDIKKELQKNLLDAQKHNSDINLYL 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 446 RELTEEHKAdllrkysLELSSIEKEIQEAKALERQLRAEFRKVENELSRLSSL-KTIADQIiEIRERLSKI--------- 515
Cdd:TIGR01612 1346 NEIANIYNI-------LKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLiKKIKDDI-NLEECKSKIestlddkdi 1417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 516 -----NLEDLK--------------RDKEEY-----------ELLKSES-----NKLKGEVESLKKEVNELNDYKNESTK 560
Cdd:TIGR01612 1418 decikKIKELKnhilseesnidtyfKNADENnenvlllfkniEMADNKSqhilkIKKDNATNDHDFNINELKEHIDKSKG 1497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 561 LEIEIDKA--------------KKELSEIEDRLLRLGFK-----TIDELSGRIRELEKFHNKYI-EAKNAEKELRDILE- 619
Cdd:TIGR01612 1498 CKDEADKNakaieknkelfeqyKKDVTELLNKYSALAIKnkfakTKKDSEIIIKEIKDAHKKFIlEAEKSEQKIKEIKKe 1577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 620 --SLKDEREELDKAFEELAKIETDIEKVTSQL----NELQRKFDQKKYEEKREKMMKlSMEIKGLETKLEELERRRDEIK 693
Cdd:TIGR01612 1578 kfRIEDDAAKNDKSNKAAIDIQLSLENFENKFlkisDIKKKINDCLKETESIEKKIS-SFSIDSQDTELKENGDNLNSLQ 1656
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 18202079 694 STIEKLKEERKERESAKMELEKLNIAIKRIE-ELRGKIKEYKALIKEealnKIGEIA 749
Cdd:TIGR01612 1657 EFLESLKDQKKNIEDKKKELDELDSEIEKIEiDVDQHKKNYEIGIIE----KIKEIA 1709
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-79 |
8.00e-12 |
|
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: 67.72 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 1 MKIERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAILVGLywsKRMRLRGLKKDEFTRTGTRGAI---IEITF 77
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEALRLLL---GPSSSRKFDEEDFYLGDDPDLPeieIELTF 77
|
..
gi 18202079 78 EE 79
Cdd:COG3593 78 GS 79
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
137-714 |
1.91e-11 |
|
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: 68.22 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 137 QGQIDAILEsdETRDKIVKEILNLDKLEKAYDNLG----KIRKYIKYSIEEKEKFIMKTENIEDLIRTQEKSFTE----V 208
Cdd:pfam15921 298 QSQLEIIQE--QARNQNSMYMRQLSDLESTVSQLRselrEAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 209 LNEIRNISSNLPRLRRELEGIKEEVKTL--EATFNSIT--ELKLRLGELNGKKGRLEERIR--------QLESGIEEKRK 276
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLwdRDTGNSITidHLRRELDDRNMEVQRLEALLKamksecqgQMERQMAAIQG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 277 KSKELEEVVKELPELEKKETEYRRLIEfkdEYLVKKNELE---KRLGILSNRLQEVKRKIKDAESKVARIR-WIEERLKE 352
Cdd:pfam15921 456 KNESLEKVSSLTAQLESTKEMLRKVVE---ELTAKKMTLEsseRTVSDLTASLQEKERAIEATNAEITKLRsRVDLKLQE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 353 IQEkimkleprVREFEDAMRlKAQMESLKSKLGGLEPEKINEKLlylenrkkelEEEIDKITRKIGE------------- 419
Cdd:pfam15921 533 LQH--------LKNEGDHLR-NVQTECEALKLQMAEKDKVIEIL----------RQQIENMTQLVGQhgrtagamqveka 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 420 -LNQRSKDRRLAIIELKKARGKCPVCGRELtEEHKADL-LRKYSLELSSIEK--EIQEAKALERQLRAEFRKVENELSRL 495
Cdd:pfam15921 594 qLEKEINDRRLELQEFKILKDKKDAKIREL-EARVSDLeLEKVKLVNAGSERlrAVKDIKQERDQLLNEVKTSRNELNSL 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 496 SSlktiadqiieirerlskiNLEDLKRD-KEEYELLKSESNKLKGEvesLKKEVNELNDYKNESTKLEIEIDKAKKELSE 574
Cdd:pfam15921 673 SE------------------DYEVLKRNfRNKSEEMETTTNKLKMQ---LKSAQSELEQTRNTLKSMEGSDGHAMKVAMG 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 575 IEDRLL-RLGfkTIDELSGRIRELEKfhnkyiEAKNAEKELRDIleslkdeREELDKAFEELAKIETDIEKVTSQLNELq 653
Cdd:pfam15921 732 MQKQITaKRG--QIDALQSKIQFLEE------AMTNANKEKHFL-------KEEKNKLSQELSTVATEKNKMAGELEVL- 795
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18202079 654 rkfdqkkyeekREKMMKLSMEIKGLETKLEELERRRDEIKSTIeklkeERKERESAKMELE 714
Cdd:pfam15921 796 -----------RSQERRLKEKVANMEVALDKASLQFAECQDII-----QRQEQESVRLKLQ 840
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-475 |
3.56e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 1 MKIERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAILVGLywskRMRLRGLKKDEFTRTGTRGAIIEITFEED 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTIEFSPGLNVIYGPNEAGKSTLLAFIRAML----LERLEKEADELFKPQGRKPELNLKELKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 81 GTKYKVLRD----FARNVSYLKRLdgREWRHVTETSMESVSSFIDRIIPYnVFLNAIYVRQGQIDAILESDETR-DKIVK 155
Cdd:COG4717 77 EEELKEAEEkeeeYAELQEELEEL--EEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAELPERlEELEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 156 EILNLDKLEKAYDNLGKIRKYIKYSIEEKEKFImkTENIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKT 235
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQL--SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 236 LEAT------FNSITELKLRLG------ELNGKKGRLEERIRQLE------------SGIEEKRKKSKELEEVVKELPEL 291
Cdd:COG4717 232 LENEleaaalEERLKEARLLLLiaaallALLGLGGSLLSLILTIAgvlflvlgllalLFLLLAREKASLGKEAEELQALP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 292 EKKETEYRRLIEFKDEYLVKKNELEKRLGILSNRLQEVKRKIKDAESKVARIRwIEERLKEIQEKIMK--------LEPR 363
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEagvedeeeLRAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 364 VREFEDAMRLKAQMESLKSKLGGLEP-----------EKINEKLLYLENRKKELEEEIDKITRKIGELNQR----SKDRR 428
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGeleellealdeEELEEELEELEEELEELEEELEELREELAELEAEleqlEEDGE 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 18202079 429 LAIIELKKARGKcpvcgRELTEEHKADLLRKYSLELssIEKEIQEAK 475
Cdd:COG4717 471 LAELLQELEELK-----AELRELAEEWAALKLALEL--LEEAREEYR 510
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
470-740 |
4.75e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 470 EIQEAKALE-RQLRAEFRKVENELsRLSSLKTIADQIIEIRERLSKINLEdLKRDKEEYELLKSESNKLKGEVESLKKEV 548
Cdd:COG1196 206 ERQAEKAERyRELKEELKELEAEL-LLLKLRELEAELEELEAELEELEAE-LEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 549 NELNdykNESTKLEIEIDKAKKELSEIEDRLLRLGfKTIDELSGRIRELEKfhnKYIEAKNAEKELRDILESLKDEREEL 628
Cdd:COG1196 284 EEAQ---AEEYELLAELARLEQDIARLEERRRELE-ERLEELEEELAELEE---ELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 629 DKAFEELAKIETDIEKVTSQLNELQRKFDQKKYEEKREKMMKLSmEIKGLETKLEELERRRDEIKSTIEKLKEERKERES 708
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270
....*....|....*....|....*....|...
gi 18202079 709 AKMELEK-LNIAIKRIEELRGKIKEYKALIKEE 740
Cdd:COG1196 436 EEEEEEEaLEEAAEEEAELEEEEEALLELLAEL 468
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-81 |
5.07e-11 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 65.18 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 1 MKIERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAI-LVGLywskrmrLRGLKK---DEFTRTGTRGAIIEIT 76
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAIyLLAP-------GRSHRTardKELIRFGAEAAVIHGR 73
|
....*
gi 18202079 77 FEEDG 81
Cdd:PRK00064 74 VEKGG 78
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
454-709 |
5.27e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.56 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 454 ADLLRKYSLELSSIEKEIQEAKALERQLRAEFRKVENELsrlsslKTIADQIIEIRERLSKINledlkrdkeeyellkSE 533
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL------AALERRIAALARRIRALE---------------QE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 534 SNKLKGEVESLKKEVNELndyknestklEIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIRELEKFHNKYIEAKNAEKE 613
Cdd:COG4942 78 LAALEAELAELEKEIAEL----------RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 614 LRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKyEEKREKMMKLSMEIKGLETKLEELERRRDEIK 693
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK-AERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*.
gi 18202079 694 STIEKLKEERKERESA 709
Cdd:COG4942 227 ALIARLEAEAAAAAER 242
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
3-76 |
5.59e-11 |
|
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: 63.00 E-value: 5.59e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18202079 3 IERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAILVGLYWSKRMRLRGLKKDEFTRTGTRGAIIEIT 76
Cdd:cd03277 3 IVRIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIE 76
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
783-867 |
6.68e-11 |
|
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: 62.87 E-value: 6.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 783 ERPLTFLSGGE--RIALGLAfrLAMsmyligKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHD-EELKDA 859
Cdd:cd03225 129 DRSPFTLSGGQkqRVAIAGV--LAM------DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDlDLLLEL 200
|
....*...
gi 18202079 860 ADHVIRIR 867
Cdd:cd03225 201 ADRVIVLE 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
783-875 |
6.85e-11 |
|
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: 63.12 E-value: 6.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 783 ERPLTFLSGGE--RIALglAFRLAMsmyligKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHD-EELKDA 859
Cdd:COG1122 129 DRPPHELSGGQkqRVAI--AGVLAM------EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAEL 200
|
90 100
....*....|....*....|.
gi 18202079 860 ADHVI-----RIRLEGGASKV 875
Cdd:COG1122 201 ADRVIvlddgRIVADGTPREV 221
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2-391 |
1.50e-10 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 64.65 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 2 KIERVIVQNFRSHKN--SEIEF-KPGINLIIGQNGAGKSSLLDAILVGLYWSKrmrLRGLKKDEF-TRTGTRGAIIEITF 77
Cdd:PHA02562 3 KFKKIRYKNILSVGNqpIEIQLdKVKKTLITGKNGAGKSTMLEALTFALFGKP---FRDIKKGQLiNSINKKDLLVELWF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 78 EEDGTKYKVLRDFARNVSYLKRlDGREWRHvtETSMESVSSFIDRIIPYN--------VFLNAIYVRQGQIDAilesdET 149
Cdd:PHA02562 80 EYGEKEYYIKRGIKPNVFEIYC-NGKLLDE--SASSKDFQKYFEQMLGMNyksfkqivVLGTAGYVPFMQLSA-----PA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 150 RDKIVKEILNL------DKLEKAY--------DNLGKIRKYIKYSIEEKEKFI--MKTENIEDLIRTQEKsFTEVLNEIR 213
Cdd:PHA02562 152 RRKLVEDLLDIsvlsemDKLNKDKirelnqqiQTLDMKIDHIQQQIKTYNKNIeeQRKKNGENIARKQNK-YDELVEEAK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 214 NISSNLPRLRRElegIKEEVKTLEATFNSITELKLRLGELNGKKGRLEERIRQLESG---------IEEKRKKSKELEEV 284
Cdd:PHA02562 231 TIKAEIEELTDE---LLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGgvcptctqqISEGPDRITKIKDK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 285 VKELpelekkETEYRRLIEFKDEYLVKKNELEKrlgiLSNRLQEVKRKIkdaESKVARIRWIEERLKEIQEKIMKLEP-R 363
Cdd:PHA02562 308 LKEL------QHSLEKLDTAIDELEEIMDEFNE----QSKKLLELKNKI---STNKQSLITLVDKAKKVKAAIEELQAeF 374
|
410 420
....*....|....*....|....*...
gi 18202079 364 VREFEDAMRLKAQMESLKSKLGGLEPEK 391
Cdd:PHA02562 375 VDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
174-558 |
1.75e-10 |
|
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: 65.09 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 174 RKYIKYSIEEKEKFIMKTENIEDLirtqEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEatfNSITELKLRLGEL 253
Cdd:TIGR02169 663 RGGILFSRSEPAELQRLRERLEGL----KRELSSLQSELRRIENRLDELSQELSDASRKIGEIE---KEIEQLEQEEEKL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 254 NGKKGRLEERIRQLESGIEEKRKkskELEEVVKELPELEKKETEYRRLIefkdeylvkkNELEKRLGilSNRLQEVKRKI 333
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKS---ELKELEARIEELEEDLHKLEEAL----------NDLEARLS--HSRIPEIQAEL 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 334 KDAESKVARirwIEERLKEIQEKIMKLEPRVREFEDAMrlkaqmeslksklgglepEKINEKLLYLENRKKELEEEIDKI 413
Cdd:TIGR02169 801 SKLEEEVSR---IEARLREIEQKLNRLTLEKEYLEKEI------------------QELQEQRIDLKEQIKSIEKEIENL 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 414 TRKIGELNQRSKDRRLAIIELKKARGKCpvcgRELTEEHKADlLRKYSLELSSIEKEIQEAKALERQLRAEFRKVENELS 493
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDL----KKERDELEAQ-LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS 934
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 494 RLS--------------SLKTIADQIIEIRERLSK---INL---EDLKRDKEEYELLKSESNKLKGEVESLKKEVNELND 553
Cdd:TIGR02169 935 EIEdpkgedeeipeeelSLEDVQAELQRVEEEIRAlepVNMlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
....*
gi 18202079 554 YKNES 558
Cdd:TIGR02169 1015 KKREV 1019
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
784-866 |
2.27e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 60.71 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 784 RPLTFLSGGER----IALGLAFRlamsmyligkVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEELKDA 859
Cdd:NF040873 115 RQLGELSGGQRqralLAQGLAQE----------ADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR 184
|
....*..
gi 18202079 860 ADHVIRI 866
Cdd:NF040873 185 ADPCVLL 191
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
789-867 |
2.29e-10 |
|
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: 59.38 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEimerHLRKISQ-VIIVSHDEELKDA-ADHVIRI 866
Cdd:cd03221 71 LSGGEKM------RLALAKLLLENPNLLLLDEPTNHLDLESIEALEE----ALKEYPGtVILVSHDRYFLDQvATKIIEL 140
|
.
gi 18202079 867 R 867
Cdd:cd03221 141 E 141
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
159-856 |
1.20e-09 |
|
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: 62.37 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 159 NLDKLEKAYDNLGKIRKYIKYSIEEKEKFIMKTENIEDLIRTQEKSFTEVLNEI----------RNISSNLPRLRRELEG 228
Cdd:TIGR00606 571 NKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYedklfdvcgsQDEESDLERLKEEIEK 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 229 IKEEVKTLEATFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSK--------ELEEVVKELPELEKKETEYRR 300
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQsklrlapdKLKSTESELKKKEKRRDEMLG 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 301 LIEFKDEYLVKK----NELEKRLGILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRLKAQ 376
Cdd:TIGR00606 731 LAPGRQSIIDLKekeiPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQ 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 377 MES-LKSKLGGLEPEKINEKllylenrKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKArgkcpvcgrelteehkad 455
Cdd:TIGR00606 811 QAAkLQGSDLDRTVQQVNQE-------KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK------------------ 865
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 456 lLRKYSLELSSIEKEIQEAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKINLEDLKRDKEEYELLKSESN 535
Cdd:TIGR00606 866 -TNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVN 944
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 536 KLKGEVESLKKEVNELNDYKNES-----TKLEIEIDKAKKELSEIEDRLLR----LGFKTIDELSGRIRElekfhnKYIE 606
Cdd:TIGR00606 945 DIKEKVKNIHGYMKDIENKIQDGkddylKQKETELNTVNAQLEECEKHQEKinedMRLMRQDIDTQKIQE------RWLQ 1018
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 607 AKNAEKELRDILESLKDEREELDKAFEELakietDIEKVTSQLNELQRKFDQKKYEEKR--EKMMKLSMEIKGLETKLEE 684
Cdd:TIGR00606 1019 DNLTLRKRENELKEVEEELKQHLKEMGQM-----QVLQMKQEHQKLEENIDLIKRNHVLalGRQKGYEKEIKHFKKELRE 1093
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 685 LERRRDEikstiEKLKEERKERESAKMELEKLNIAIKRIEELRGKIKEykalIKEEALNKIGEIASEIFSEFTDGKYSGI 764
Cdd:TIGR00606 1094 PQFRDAE-----EKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHS----MKMEEINKIIRDLWRSTYRGQDIEYIEI 1164
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 765 AIRAEDNKVKLFVIYDGVERPLTF-----------LSGGERIALGLAFRLAMSMYLIGKVDLLILDEPTPFLDEERRRKL 833
Cdd:TIGR00606 1165 RSDADENVSASDKRRNYNYRVVMLkgdtaldmrgrCSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIESL 1244
|
730 740
....*....|....*....|....*...
gi 18202079 834 IE-----IMERHLRKISQVIIVSHDEEL 856
Cdd:TIGR00606 1245 AHalveiIKSRSQQRNFQLLVITHDEDF 1272
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
783-866 |
1.48e-09 |
|
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: 58.64 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 783 ERPLTFLSGGE--RIALGLAfrlamsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDeELKDAA 860
Cdd:COG4133 126 DLPVRQLSAGQkrRVALARL--------LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ-PLELAA 196
|
....*.
gi 18202079 861 DHVIRI 866
Cdd:COG4133 197 ARVLDL 202
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
145-715 |
1.74e-09 |
|
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: 61.57 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 145 ESDETRDKIVKEILNLDKLEKAYDNLGKIRKYIKYSIEEKEKFIM----KTENIEDLIRTQEKSFTEVLNEIRNISSNLP 220
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEklnnKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 221 RLRRELEGIKEEVKTLEATFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKEteyrr 300
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI----- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 301 liefKDEYLVKKNELE---KRLGILSNRLQEVKRKIKDAESKVAR--IRWIEERLKEIQEKIMKLEPRVREFEDAM-RLK 374
Cdd:TIGR04523 266 ----KKQLSEKQKELEqnnKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIIsQLN 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 375 AQMESLKSKLGGLEPE--KINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKargkcpvcgrelTEEH 452
Cdd:TIGR04523 342 EQISQLKKELTNSESEnsEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK------------LNQQ 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 453 KADLLRKYSLELSSIEKEIQEAKALERQLRAEFRKVENELS-------RLSSLKTIADQIIEIRERLSKINLEDLKRDKE 525
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSvkeliikNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 526 EYELLKSESNKLKGEVESLKKEVNELNDYKNEST----KLEIEIDKAKKELSEIEDRLLRLGF-KTIDELSGRIR----E 596
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKekieKLESEKKEKESKISDLEDELNKDDFeLKKENLEKEIDeknkE 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 597 LEKFHNKYIEAKNAEKELRDILESLKDER------------------EELDKAFEELAKIETDIEKVTSQLNELQR--KF 656
Cdd:TIGR04523 570 IEELKQTQKSLKKKQEEKQELIDQKEKEKkdlikeieekekkissleKELEKAKKENEKLSSIIKNIKSKKNKLKQevKQ 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 657 DQKKYEEKREKMMKLSMEIKGLETK-------------------------------LEELERRRDEIKSTIEKLKEERKE 705
Cdd:TIGR04523 650 IKETIKEIRNKWPEIIKKIKESKTKiddiielmkdwlkelslhykkyitrmirikdLPKLEEKYKEIEKELKKLDEFSKE 729
|
650
....*....|
gi 18202079 706 RESAKMELEK 715
Cdd:TIGR04523 730 LENIIKNFNK 739
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
256-676 |
1.95e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 256 KKGRLEERIRQLESGIEEKRKKS---KELEEVVKELPELEKKETEYRRLIEfkdeylVKKNELEKRLGILSNRLQEVKRK 332
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADeakKKAEEDKKKADELKKAAAAKKKADE------AKKKAEEKKKADEAKKKAEEAKK 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 333 IKDAESKVARIRWIEERLKEIQE--KIMKLEPRVREFEDAMRLKAQMESLKSKLGGL----EPEKINEKLLYLENRKKEL 406
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEakKADEAKKKAEEAKKADEAKKKAEEAKKKADEAkkaaEAKKKADEAKKAEEAKKAD 1525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 407 EEEIDKITRKIGELNQRSKDRRLAII----ELKKARGKCPVCGRELTEEHKADLLRKYSLELSSIEKEIQEAKAL---ER 479
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeeEK 1605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 480 QLRAE-FRKVENELSRLSSLKTiADQIIEIRERLSKINLEDLKRDKE---EYELLKSESNKLKGEVESLKKEVNELNDYK 555
Cdd:PTZ00121 1606 KMKAEeAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEKKKAEElkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 556 NESTKLEIEIDKAKKELSEIEDrLLRLGFKTIDELSGRIRELEKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEEL 635
Cdd:PTZ00121 1685 EDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 18202079 636 AKIETDIEKVTSQLNELQRKFDQKKYEEKREKMMKLSMEIK 676
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
478-752 |
1.96e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 478 ERQLRAefrkVENELSRLSslktiaDQIIEIRERLSKinLEDLKRDKEEYELLKSESNKLKGEV---------ESLKKEV 548
Cdd:COG1196 178 ERKLEA----TEENLERLE------DILGELERQLEP--LERQAEKAERYRELKEELKELEAELlllklreleAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 549 NELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLGfKTIDELSGRIRELEKfhnkyiEAKNAEKELRDILESLKDEREEL 628
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELE-LELEEAQAEEYELLA------ELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 629 DKAFEELAKIETDIEKVTSQLNELqrkfdQKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERES 708
Cdd:COG1196 319 EELEEELAELEEELEELEEELEEL-----EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 18202079 709 AKMELE-KLNIAIKRIEELRGKIKEYKALIKEEALNKIGEIASEI 752
Cdd:COG1196 394 AAAELAaQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
441-866 |
2.42e-09 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision 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: 273184 [Multi-domain] Cd Length: 925 Bit Score: 61.18 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 441 CPVCGRELTEEHKADLLRKYsLELSSIEKEIQEAKALERQlRAEFRKVENELSRLSSLKTIAD-QIIEIRERLS------ 513
Cdd:TIGR00630 118 CPTCGRPISRQTPSQIVDQI-LALPEGTRVILLAPIVRGR-KGEFRKLLEKLRKQGFARVRVDgEVYPLEDPPKleknkk 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 514 ----------KINLEDLKRDKEEYELLKSESNklkGEVESLKKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRLLR-- 581
Cdd:TIGR00630 196 htidvvidrlTVKNENRSRLAESVETALRLGD---GLLEVEFDDDEEVAESKEELFSEKFACPECGFSLPELEPRLFSfn 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 582 -----------LGFK-TIDELSGRIRELEKFHNKYIEA--KNAEKELRDILESLKDERE-ELDKAFEELAKIETDIekvt 646
Cdd:TIGR00630 273 spygacpecsgLGIKqEFDPELIIPDPLLSLNGGAIVPfkKSTTSYYRQMFASLAEHLGfDLDTPWKDLPEEAQKA---- 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 647 sQLNELQRKFDQKKYEEKREKMMKLSMEIKGLetkLEELERRRDEIKST-----IEKLKEER--KERESAKMELEKLNIA 719
Cdd:TIGR00630 349 -ILYGSGEEVIVVKYRNGGGETFRYHKPFEGV---IPELERRYLETESEsmreyLEKFMSERpcPSCGGTRLKPEALAVT 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 720 I--KRIEELRGK-IKEYKALIKEEALNKIGE-IASEIFSEFTDgkysgiairaednkvKLFVIYD------GVERPLTFL 789
Cdd:TIGR00630 425 VggKSIADVSELsIREAHEFFNQLTLTPEEKkIAEEVLKEIRE---------------RLGFLIDvgldylSLSRAAGTL 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 790 SGGE----RIALGLAFRLAMSMYligkvdllILDEPTPFLDEERRRKLIEIMeRHLRKI-SQVIIVSHDEELKDAADHVI 864
Cdd:TIGR00630 490 SGGEaqriRLATQIGSGLTGVLY--------VLDEPSIGLHQRDNRRLINTL-KRLRDLgNTLIVVEHDEDTIRAADYVI 560
|
..
gi 18202079 865 RI 866
Cdd:TIGR00630 561 DI 562
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
789-867 |
2.91e-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: 57.88 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGE--RIALGLAfrlamsmyLIGKVDLLILDEPTPFLDEERRRKLIEImerhLRKISQ-----VIIVSHDEELKDAAD 861
Cdd:cd03255 141 LSGGQqqRVAIARA--------LANDPKIILADEPTGNLDSETGKEVMEL----LRELNKeagttIVVVTHDPELAEYAD 208
|
....*.
gi 18202079 862 HVIRIR 867
Cdd:cd03255 209 RIIELR 214
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-316 |
3.25e-09 |
|
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: 59.92 E-value: 3.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 1 MKIERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAIlvglYWSKRMRLRGLKKDEFTRTGTRGAIIEITFEED 80
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEAL----DIFLNNKEKFFEDDFLVLYLKDVIKIDKEDLNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 81 GTKYKVLRDFARNVSYLKRLDGREWRHVTETSMESVSSFIDriipYNVFLNAIYVRQGQIDAILESDETRDKIVKEILNL 160
Cdd:pfam13175 77 FENISFSIDIEIDVEFLLILFGYLEIKKKYLCLASKGKAKE----YEKTLHPKGANKADLLLELKISDLKKYLKQFKIYI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 161 DKLEKAYDNLGKIRKYIKYSI-------EEKEKFIMKT--ENIEDLIRTQEKSFTEVLNEIRN--ISSNLPRLRRELEGI 229
Cdd:pfam13175 153 YNNYYLDEKKNVFDKKSKYELpslkeefLNSEKEEIKVdkEDLKKLINELEKSINYHENVLENlqIKKLLISADRNASDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 230 KEEVK--TLEATFNSITElklrlgELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKETEYRRLIEFKDE 307
Cdd:pfam13175 233 DSEKInsLLGALKQRIFE------EALQEELELTEKLKETQNKLKEIDKTLAEELKNILFKKIDKLKDFGYPPFLNPEIE 306
|
....*....
gi 18202079 308 YLVKKNELE 316
Cdd:pfam13175 307 IKKDDEDLP 315
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-145 |
3.28e-09 |
|
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: 57.66 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 1 MKIERVIVQNFRS-HKNSEIEF----KPGINLIIGQNGAGKSSLLDAILVGLYWSKRMRLRGLKKDEFTRTGTRGAIIEI 75
Cdd:cd03279 1 MKPLKLELKNFGPfREEQVIDFtgldNNGLFLICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDTAEVSF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 76 TFEEDGTKYKVLRDFARNvsylkrldgrewrhvtetsmesvssfidriipYNVFLNAIYVRQGQIDAILE 145
Cdd:cd03279 81 TFQLGGKKYRVERSRGLD--------------------------------YDQFTRIVLLPQGEFDRFLA 118
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
518-741 |
4.18e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 518 EDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDyknESTKLEIEIDKAKKELSEIEDRLLRLgfktIDELSGRIREL 597
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQA---ELEALQAEIDKLQAEIAEAEAEIEER----REELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 598 EK--FHNKYIEAknaekelrdILESlkderEELDKAFEELAKIETDIEKVTSQLNELQRkfDQKKYEEKREKMMKLSMEI 675
Cdd:COG3883 96 YRsgGSVSYLDV---------LLGS-----ESFSDFLDRLSALSKIADADADLLEELKA--DKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 676 KG----LETKLEELERRRDEIKSTIEKLKEERKERESAKMELEKLNIAIKRIEELRGKIKEYKALIKEEA 741
Cdd:COG3883 160 EAlkaeLEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
583-858 |
4.73e-09 |
|
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: 58.56 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 583 GFKTIDELSGRIRELEKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYE 662
Cdd:pfam13304 38 RNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 663 EKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEKLNIAIKRIEELRGKIKEYKALIKEEAL 742
Cdd:pfam13304 118 LRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 743 NKIGEIASEIFSEFTDGKYSGIAIRAEDNKvklfviyDGVERPLTFLSGGERIALGLAFRLamsMYLIGKVDLLILDEPT 822
Cdd:pfam13304 198 NLSDLGEGIEKSLLVDDRLRERGLILLENG-------GGGELPAFELSDGTKRLLALLAAL---LSALPKGGLLLIDEPE 267
|
250 260 270
....*....|....*....|....*....|....*.
gi 18202079 823 PFLDEERRRKLIEIMERHLRKISQVIIVSHDEELKD 858
Cdd:pfam13304 268 SGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
779-878 |
5.41e-09 |
|
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: 56.56 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 779 YDGVERPLTFLSGGERIALglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEELKD 858
Cdd:cd03238 78 YLTLGQKLSTLSGGELQRV----KLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLS 153
|
90 100
....*....|....*....|
gi 18202079 859 AADHVIRIRLEGGASKVEVV 878
Cdd:cd03238 154 SADWIIDFGPGSGKSGGKVV 173
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
789-867 |
7.13e-09 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 59.39 E-value: 7.13e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18202079 789 LSGGERIALGLAfRLamsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISqVIIVSHDEELKDAADHVIRIR 867
Cdd:COG4987 472 LSGGERRRLALA-RA-----LLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRT-VLLITHRLAGLERMDRILVLE 543
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
2-43 |
7.87e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 58.40 E-value: 7.87e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 18202079 2 KIERVIVQNFRSHKNSEIEFKPgINLIIGQNGAGKSSLLDAI 43
Cdd:COG4637 1 MITRIRIKNFKSLRDLELPLGP-LTVLIGANGSGKSNLLDAL 41
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-79 |
9.38e-09 |
|
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: 55.78 E-value: 9.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 3 IERVIVQNFRSHKNSEIEFKP-GINLIIGQNGAGKSSLLDAILVGLYWSKRMRLRGLKKD---EFTRTGTRGAIIEITFE 78
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSnSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFlagGGVKAGINSASVEITFD 80
|
.
gi 18202079 79 E 79
Cdd:cd03239 81 K 81
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
789-866 |
1.22e-08 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 58.45 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGE--RIALGLAF-RLAmsmyligkvDLLILDEPTPFLDEERRRKLIEIMERhLRKISQVIIVSHDEELKDAADHVIR 865
Cdd:TIGR02857 459 LSGGQaqRLALARAFlRDA---------PLLLLDEPTAHLDAETEAEVLEALRA-LAQGRTVLLVTHRLALAALADRIVV 528
|
.
gi 18202079 866 I 866
Cdd:TIGR02857 529 L 529
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
199-510 |
1.30e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 58.60 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 199 RTQEKSFTEVLNE-IRNISSNLPRLRRELEGIKEEVKTLEATFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKK 277
Cdd:pfam17380 287 RQQQEKFEKMEQErLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 278 SKELEEVVKELPELEKKETEYRRliefKDEYLVKKNELEKRLGILSnrlQEVKRKIKDAESKVARIRWIEERLKEIQEKI 357
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQ----KNERVRQELEAARKVKILE---EERQRKIQQQKVEMEQIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 358 MKlEPRVREFE----DAMRLKAQMESLKSKlgglEPEKINEKLlyLENRKKELEEEIDKITRKIgeLNQRSKDRRLAIIE 433
Cdd:pfam17380 440 LE-EERAREMErvrlEEQERQQQVERLRQQ----EEERKRKKL--ELEKEKRDRKRAEEQRRKI--LEKELEERKQAMIE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 434 LKKARgkcPVCGRELTEEHKA---DLLRKYSLELSSIEKEIQEAKALERQLraefRKVENELSRLSSLKTIADQIIEIRE 510
Cdd:pfam17380 511 EERKR---KLLEKEMEERQKAiyeEERRREAEEERRKQQEMEERRRIQEQM----RKATEERSRLEAMEREREMMRQIVE 583
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
789-871 |
1.84e-08 |
|
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: 54.70 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGE--RIALGLAfrlamsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISqVIIVSHDEELKDAADHVirI 866
Cdd:cd03228 97 LSGGQrqRIAIARA--------LLRDPPILILDEATSALDPETEALILEALRALAKGKT-VIVIAHRLSTIRDADRI--I 165
|
....*
gi 18202079 867 RLEGG 871
Cdd:cd03228 166 VLDDG 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
789-871 |
1.85e-08 |
|
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: 58.31 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGERIALGLAfRLamsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISqVIIVSHDEELKDAADHVirIRL 868
Cdd:COG2274 612 LSGGQRQRLAIA-RA-----LLRNPRILILDEATSALDAETEAIILENLRRLLKGRT-VIIIAHRLSTIRLADRI--IVL 682
|
...
gi 18202079 869 EGG 871
Cdd:COG2274 683 DKG 685
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
789-867 |
1.86e-08 |
|
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: 54.71 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHD-EELKDAADHVIRIR 867
Cdd:cd03230 96 LSGGMKQ------RLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHIlEEAERLCDRVAILN 169
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
316-659 |
1.95e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 316 EKRLGILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRLKAQMESLKSKLGGLEP-----E 390
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssddlA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 391 KINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGKCPVCGRELTEEHKADLLRKYSLE--LSSIE 468
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDavERELR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 469 KEIQEA-KALERQLRAEFRKVENELSR--------LSSLKTIADQIIEIRERLSKINLEDLKRDKEEY-ELLKSESN--- 535
Cdd:COG4913 769 ENLEERiDALRARLNRAEEELERAMRAfnrewpaeTADLDADLESLPEYLALLDRLEEDGLPEYEERFkELLNENSIefv 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 536 -----KLKGEVESLKKEVNELNDyknestkleieidkakkELSEIE---DRLLRLGFKtiDELSGRIRELekfhnkyiea 607
Cdd:COG4913 849 adllsKLRRAIREIKERIDPLND-----------------SLKRIPfgpGRYLRLEAR--PRPDPEVREF---------- 899
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 18202079 608 knaEKELRDILE-SLKDEREELDKAFEELAKIetdIEKVTSQLNELQRKFDQK 659
Cdd:COG4913 900 ---RQELRAVTSgASLFDEELSEARFAALKRL---IERLRSEEEESDRRWRAR 946
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
139-747 |
1.96e-08 |
|
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: 58.44 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 139 QIDAILESDETRDKIVKEILNLDKLEKAYDNLGKIRKYIKYSIEEKEkFIMKTENIEDLIRTQEKSFTEVLNEIRNISSN 218
Cdd:pfam02463 188 LIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL-NEERIDLLQELLRDEQEEIESSKQEIEKEEEK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 219 LPRLRRELEGIKEEVKTLEATFN-SITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKETE 297
Cdd:pfam02463 267 LAQVLKENKEEEKEKKLQEEELKlLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 298 YRRLIEFKDEYLVKKNELEKRLGILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRLKAQM 377
Cdd:pfam02463 347 LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 378 ESLKsklgglEPEKINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGKcpVCGRELTEEHKADLL 457
Cdd:pfam02463 427 EELE------ILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ--EQLELLLSRQKLEER 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 458 RKYSLELSSIEKEIQEAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKINLEDLKRDKEEYELLKSESNKL 537
Cdd:pfam02463 499 SQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGAR 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 538 KGEVESLKKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIRELEK--------FHNKYIEAKN 609
Cdd:pfam02463 579 KLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESakakesglRKGVSLEEGL 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 610 AEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYEEKREKMMKLSMEIKGLETKL----EEL 685
Cdd:pfam02463 659 AEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQdkinEEL 738
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18202079 686 ERRRDEIKSTIEKLKEERKERESAKMELEKLNIAIKRIEELRGKIKEYKALIKEEALNKIGE 747
Cdd:pfam02463 739 KLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQE 800
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-86 |
3.49e-08 |
|
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: 54.39 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 3 IERVIVQNFRSH-KNSEIEFKPGINLIIGQNGAGKSSLLDAILVGLYWSKRMRLRGLKKDE--FTRTGTRGAI----IEI 75
Cdd:cd03278 1 LKKLELKGFKSFaDKTTIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDviFAGSETRKPAnfaeVTL 80
|
90
....*....|.
gi 18202079 76 TFEEDGTKYKV 86
Cdd:cd03278 81 TFDNSDGRYSI 91
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
789-870 |
4.93e-08 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 54.68 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGERIALGLAfrLAmsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHD-EELKDAADHVI--- 864
Cdd:COG1131 132 LSGGMKQRLGLA--LA----LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYlEEAERLCDRVAiid 205
|
....*...
gi 18202079 865 --RIRLEG 870
Cdd:COG1131 206 kgRIVADG 213
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
784-872 |
5.13e-08 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.93 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 784 RPLTFLSGGERIALGLAFRLamSMYLIGKVdLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEELKDAADHV 863
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKEL--SKRSTGKT-LYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWI 241
|
....*....
gi 18202079 864 IRIRLEGGA 872
Cdd:cd03271 242 IDLGPEGGD 250
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
449-726 |
7.58e-08 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 56.09 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 449 TEEHKADLLRK-YSLELSSIEkEIQEAKALE--RQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKINLEDLKRDKE 525
Cdd:PRK05771 14 LKSYKDEVLEAlHELGVVHIE-DLKEELSNErlRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 526 EyellksESNKLKGEVESLKKEVNELndyKNESTKLEIEIDKAKKELS-EIEDRLLRlGFKTIDELSGRIRELEKFHNKY 604
Cdd:PRK05771 93 E------ELEKIEKEIKELEEEISEL---ENEIKELEQEIERLEPWGNfDLDLSLLL-GFKYVSVFVGTVPEDKLEELKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 605 IEAKNAEKELRDILES----LKDEREELDKAFEELAKIEtdiekvtsqlnelqrkFDQKKYEEKRekmmKLSMEIKGLET 680
Cdd:PRK05771 163 ESDVENVEYISTDKGYvyvvVVVLKELSDEVEEELKKLG----------------FERLELEEEG----TPSELIREIKE 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 18202079 681 KLEELERRRDEIKSTIEKLKEERKERESAkmELEKLNIAIKRIEEL 726
Cdd:PRK05771 223 ELEEIEKERESLLEELKELAKKYLEELLA--LYEYLEIELERAEAL 266
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-81 |
8.25e-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: 54.61 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 3 IERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAIlvglYWSKRMR-LRGLKKDEFTRTGTRGAIIEITFEEDG 81
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAI----SLLATGKsHRTSRDKELIRWGAEEAKISAVLERQG 76
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
783-874 |
8.38e-08 |
|
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: 53.81 E-value: 8.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 783 ERPLTFLSGGERIALGLAFRLAMSMYLI----GKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEELKD 858
Cdd:cd03279 118 ARPVSTLSGGETFLASLSLALALSEVLQnrggARLEALFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKE 197
|
90
....*....|....*.
gi 18202079 859 AADHVIRIRLEGGASK 874
Cdd:cd03279 198 RIPQRLEVIKTPGGSR 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
783-875 |
8.43e-08 |
|
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: 54.28 E-value: 8.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 783 ERPLTFLSGGER----IALGLAfrlamsmyliGKVDLLILDEPTPFLDEERRrklIEIMErHLRKISQ-----VIIVSHD 853
Cdd:COG1120 132 DRPVDELSGGERqrvlIARALA----------QEPPLLLLDEPTSHLDLAHQ---LEVLE-LLRRLARergrtVVMVLHD 197
|
90 100 110
....*....|....*....|....*....|
gi 18202079 854 eeLKDAA---DHVI-----RIRLEGGASKV 875
Cdd:COG1120 198 --LNLAAryaDRLVllkdgRIVAQGPPEEV 225
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
584-739 |
9.14e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 584 FKTIDELSGRIRELEKFHNKYIEAKnaekELRDILESLKDEREELDKAFEELAKIETDIEKvtsqlneLQRKFDQKKYEE 663
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAR----EQIELLEPIRELAERYAAARERLAELEYLRAA-------LRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 664 KREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEER-----KERESAKMELEKLNiaiKRIEELRGKIKEYKALIK 738
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggDRLEQLEREIERLE---RELEERERRRARLEALLA 369
|
.
gi 18202079 739 E 739
Cdd:COG4913 370 A 370
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2-744 |
9.21e-08 |
|
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: 56.21 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 2 KIERVIVQNFRS-----HKNSEIEFKPGINLIIGQNGAGKSSLLDAILvglYWSKRMRLRGLKKDEF-----------TR 65
Cdd:TIGR00606 2 KFLKMSILGVRSfgiedKDKQIIDFFSPLTILVGPNGAGKTTIIECLK---YICTGDFPPGTKGNTFvhdpkvaqetdVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 66 TGTRGAIIEITFEEDGTKYKVLRDFARNVSYLKRLDG--REWRHVTETSMESVSSFIDRI------IPYNVFLNAIYVRQ 137
Cdd:TIGR00606 79 AQIRLQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGviTRYKHGEKVSLSSKCAEIDREmishlgVSKAVLNNVIFCHQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 138 GQIDAILESDETRDKIVKEILNLDKLEKAYDNLGKIRKYIKYSIEEKE-------KFIMKTENIEDLIRTQEKSFTEVLN 210
Cdd:TIGR00606 159 EDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQmelkylkQYKEKACEIRDQITSKEAQLESSRE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 211 EIRNISSNLPRLRRELEGIKEEVKTLEATFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKEL--------- 281
Cdd:TIGR00606 239 IVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNhqrtvreke 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 282 EEVVKELPELEKKETEYRRLIEFKDEYLVKKNELE------------KRLGILSNRLQ----------EVKRKIKDAESK 339
Cdd:TIGR00606 319 RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlqadrhqehiraRDSLIQSLATRleldgfergpFSERQIKNFHTL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 340 VAR-----IRWIEERLKEIQEKIMKLEPRVREFEDAMRLKAQMESLKSKLGGLEPEKINEKLLYLEN------RKKELEE 408
Cdd:TIGR00606 399 VIErqedeAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegssdRILELDQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 409 EIDKITRKIGELNQRSKDRRLAIIELKKARGKCPVCGRELTEEHKADLLRKYSLELSSIEKEIQEAKALERQLRAEFRKV 488
Cdd:TIGR00606 479 ELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRH 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 489 ENELSRLSSL---KTIADQIIEIRERLSKINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDYKNE---STKLE 562
Cdd:TIGR00606 559 SDELTSLLGYfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcgSQDEE 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 563 IEIDKAKKELSEIEDRLLRLGFKT----------IDELSGRIRELEKFHNKYIEAKNAEKELRDILESLKDEREELDKAF 632
Cdd:TIGR00606 639 SDLERLKEEIEKSSKQRAMLAGATavysqfitqlTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESEL 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 633 EELAK-IETDIEKVTSQLNELQRKfdQKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKM 711
Cdd:TIGR00606 719 KKKEKrRDEMLGLAPGRQSIIDLK--EKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMER 796
|
810 820 830
....*....|....*....|....*....|...
gi 18202079 712 ELEKLNIAIKRIEELRGKIKEYKALIKEEALNK 744
Cdd:TIGR00606 797 FQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQ 829
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
783-856 |
9.49e-08 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 53.20 E-value: 9.49e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18202079 783 ERPLTFLSGGERIALGLAFRLAMsmyligKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEEL 856
Cdd:TIGR01166 122 ERPTHCLSGGEKKRVAIAGAVAM------RPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDL 189
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
481-715 |
9.84e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.79 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 481 LRAEFRKVENELSRLSSLKTIADQIIEIR----ERLSKINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVnelndykn 556
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIKTYnkniEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDEL-------- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 557 esTKLEIEIDKAKKELSEIEDRLLRLGFKtIDELSGrireLEKFHNKYIEA---KNAEKELRDILESLKDEREELDKAFE 633
Cdd:PHA02562 244 --LNLVMDIEDPSAALNKLNTAAAKIKSK-IEQFQK----VIKMYEKGGVCptcTQQISEGPDRITKIKDKLKELQHSLE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 634 ELAKIETDIEKVTSQLNELQRKFD--QKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKM 711
Cdd:PHA02562 317 KLDTAIDELEEIMDEFNEQSKKLLelKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
....
gi 18202079 712 ELEK 715
Cdd:PHA02562 397 ELVK 400
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
346-768 |
1.13e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 346 IEERLKEIQEKIMKLEPRVREFEDAMRLKAQMESLKSKLGGLEPEKINEKLLYLENRKKELEEEIDKITRKIGELNQRSK 425
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 426 DRRLAIIELKKAR---------------------------------GKCPVCGRELTEEHK---------ADLLRKYSLE 463
Cdd:COG4913 320 ALREELDELEAQIrgnggdrleqlereierlereleererrrarleALLAALGLPLPASAEefaalraeaAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 464 LSSIEKEIQEAKALERQLRAEFRKVENELSRLSSLK-TIADQIIEIRERLS---KINLEDLK--------RDKEE----- 526
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKsNIPARLLALRDALAealGLDEAELPfvgelievRPEEErwrga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 527 ------------------YELLKS--ESNKLKGEVESLKKEVNELNDYKNE------STKLEIEIDKAKKEL-SEIEDRL 579
Cdd:COG4913 480 iervlggfaltllvppehYAAALRwvNRLHLRGRLVYERVRTGLPDPERPRldpdslAGKLDFKPHPFRAWLeAELGRRF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 580 LRLGFKTIDEL---------SGRIRELEKFHNK----------YIEAKNAEKelrdiLESLKDEREELDkafEELAKIET 640
Cdd:COG4913 560 DYVCVDSPEELrrhpraitrAGQVKGNGTRHEKddrrrirsryVLGFDNRAK-----LAALEAELAELE---EELAEAEE 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 641 DIEKVTSQLNELQRKFDQ----KKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEKL 716
Cdd:COG4913 632 RLEALEAELDALQERREAlqrlAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDEL 711
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 18202079 717 NiaiKRIEELRGKIKEYKALIKE--EALNKIGEIASEIFSEFTDGKYSGIAIRA 768
Cdd:COG4913 712 K---GEIGRLEKELEQAEEELDElqDRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| Rad50_zn_hook |
pfam04423 |
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal ... |
420-471 |
1.28e-07 |
|
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal maintenance and functions in homologous recombination, telomere maintenance and sister chromatid association. The Rad50 coiled-coil region contains a dimer interface at the apex of the coiled coils in which pairs of conserved Cys-X-X-Cys motifs form interlocking hooks that bind one Zn ion. This alignment includes the zinc hook motif and a short stretch of coiled-coil on either side.
Pssm-ID: 427940 [Multi-domain] Cd Length: 52 Bit Score: 48.73 E-value: 1.28e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 18202079 420 LNQRSKDRRLAIIELKKARGKCPVCGRELTEEHKADLLRKYSLELSSIEKEI 471
Cdd:pfam04423 1 LHQETLELNKKIEELKEAEGCCPLCGRPLDEEHRSELIKELQSKLERLPEEL 52
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
789-877 |
1.45e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 55.20 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGE--RIALGlafRLamsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISqVIIVSHDEELKDAADHVIRI 866
Cdd:COG4178 486 LSLGEqqRLAFA---RL-----LLHKPDWLFLDEATSALDEENEAALYQLLREELPGTT-VISVGHRSTLAAFHDRVLEL 556
|
90
....*....|.
gi 18202079 867 RLEGGASKVEV 877
Cdd:COG4178 557 TGDGSWQLLPA 567
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
139-414 |
1.50e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 55.32 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 139 QIDAILESDETrDKIVKEILNLDKLEKAYDNLGKIRKYIKysIEEKEKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSN 218
Cdd:PRK05771 32 HIEDLKEELSN-ERLRKLRSLLTKLSEALDKLRSYLPKLN--PLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 219 LPRLRRELEGIKEEVKTLEatfnSITELKLRLGELNGKKgrleeRIRQLESGIEEKRKKSKELEEVVKELPELEKKETEY 298
Cdd:PRK05771 109 ISELENEIKELEQEIERLE----PWGNFDLDLSLLLGFK-----YVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 299 RRLIEFKDEYLVKKNELEKRLGILSNRLQEvKRKIKDaeskvaRIRWIEERLKEIQEKIMKLEPRVREF-----EDAMRL 373
Cdd:PRK05771 180 YVVVVVLKELSDEVEEELKKLGFERLELEE-EGTPSE------LIREIKEELEEIEKERESLLEELKELakkylEELLAL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 18202079 374 KAQMESLKSKLGGLEPEKINEKLLYLE-----NRKKELEEEIDKIT 414
Cdd:PRK05771 253 YEYLEIELERAEALSKFLKTDKTFAIEgwvpeDRVKKLKELIDKAT 298
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
464-706 |
1.87e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 54.91 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 464 LSSIEKEIQEAKALERQLRA-EFRKVE-NELSRLSSLKTIADQIIEirERLSKINLEDLKRDK----------EEYELLK 531
Cdd:PLN02939 155 LEDLEKILTEKEALQGKINIlEMRLSEtDARIKLAAQEKIHVEILE--EQLEKLRNELLIRGAteglcvhslsKELDVLK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 532 SESNKLKGEVESLKKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRL-------LRLGFKTIDELSGRIRELEKFHNKy 604
Cdd:PLN02939 233 EENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFivaqedvSKLSPLQYDCWWEKVENLQDLLDR- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 605 ieAKNAEKELRDILESLKDEREELDKAFEELAkiETDIEKVTSQLNELQrkfdQKKYEEKREKMMKLSMEIkglETKLEE 684
Cdd:PLN02939 312 --ATNQVEKAALVLDQNQDLRDKVDKLEASLK--EANVSKFSSYKVELL----QQKLKLLEERLQASDHEI---HSYIQL 380
|
250 260
....*....|....*....|..
gi 18202079 685 LERRRDEIKSTIEKLKEERKER 706
Cdd:PLN02939 381 YQESIKEFQDTLSKLKEESKKR 402
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
774-874 |
1.91e-07 |
|
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: 52.64 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 774 KLFVIYDGVER-PLTfLSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSH 852
Cdd:cd03226 112 KDLDLYALKERhPLS-LSGGQKQ------RLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITH 184
|
90 100
....*....|....*....|...
gi 18202079 853 DEE-LKDAADHVirIRLEGGASK 874
Cdd:cd03226 185 DYEfLAKVCDRV--LLLANGAIV 205
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
779-879 |
2.03e-07 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 52.65 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 779 YDGVERPLTFLSGGE--RIalglafRLA--MSMYLIGKvdLLILDEPTPFLDEERRRKLIEIMeRHLRKI-SQVIIVSHD 853
Cdd:cd03270 128 YLTLSRSAPTLSGGEaqRI------RLAtqIGSGLTGV--LYVLDEPSIGLHPRDNDRLIETL-KRLRDLgNTVLVVEHD 198
|
90 100
....*....|....*....|....*.
gi 18202079 854 EELKDAADHVIRIRLEGGASKVEVVS 879
Cdd:cd03270 199 EDTIRAADHVIDIGPGAGVHGGEIVA 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
532-739 |
3.73e-07 |
|
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: 53.23 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 532 SESNKLKGEVESLKKEVNELNDyknESTKLEIEIDKAKKELSEIEDRLLRLGfKTIDELSGRIRELEKFHNkyiEAKNAE 611
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEK---ELAALKKEEKALLKQLAALERRIAALA-RRIRALEQELAALEAELA---ELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 612 KELRDILESLKDEREELDKAFEELAKIETDIEKVTSQ-LNELQRKFDQKKY--EEKREKMMKLSMEIKGLETKLEELERR 688
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdFLDAVRRLQYLKYlaPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18202079 689 RDEIKSTIEKLKEERKERESAKMELEKLNIAI--------KRIEELRGKIKEYKALIKE 739
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLekelaelaAELAELQQEAEELEALIAR 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
561-739 |
3.84e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 561 LEIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIRELEKFHNKYIEAKNAEKELRDILESLKDEREELDkafeelakiet 640
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR----------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 641 diekvtsqlNELQRKFDQKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEK----- 715
Cdd:COG4717 116 ---------EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEElleql 186
|
170 180 190
....*....|....*....|....*....|.
gi 18202079 716 -------LNIAIKRIEELRGKIKEYKALIKE 739
Cdd:COG4717 187 slateeeLQDLAEELEELQQRLAELEEELEE 217
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-151 |
4.80e-07 |
|
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: 51.88 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 3 IERVIVQNFRSHKNSEI--EFKPGINLIIGQNGAGKSSLLDAI---LVGLYWSKRMRLRGLKKDEFTRTGTRGAIIEITF 77
Cdd:cd03272 1 IKQVIIQGFKSYKDQTViePFSPKHNVVVGRNGSGKSNFFAAIrfvLSDEYTHLREEQRQALLHEGSGPSVMSAYVEIIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 78 EEDGTKYKVLRD--FARNVSYLK----RLDGrewRHVTETSMESV--SSFIDRIIPYNVflnaiyVRQGQIDAI--LESD 147
Cdd:cd03272 81 DNSDNRFPIDKEevRLRRTIGLKkdeyFLDK---KNVTKNDVMNLleSAGFSRSNPYYI------VPQGKINSLtnMKQD 151
|
....
gi 18202079 148 ETRD 151
Cdd:cd03272 152 EQQE 155
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
462-637 |
5.22e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 462 LELSSIEKEIQEAKALERQLRAEFRKVENELsrlsslKTIADQIIEIRERLSKInledlkrdKEEYELLKSESNKLKGEV 541
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDEL------AALEARLEAAKTELEDL--------EKEIKRLELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 542 ESLKKEVNELNDYKnESTKLEIEIDKAKKELSEIEDRLLRLgFKTIDELSGRIRELEKFHNKYIEAKNAEK-ELRDILES 620
Cdd:COG1579 76 KKYEEQLGNVRNNK-EYEALQKEIESLKRRISDLEDEILEL-MERIEELEEELAELEAELAELEAELEEKKaELDEELAE 153
|
170
....*....|....*..
gi 18202079 621 LKDEREELDKAFEELAK 637
Cdd:COG1579 154 LEAELEELEAEREELAA 170
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
144-719 |
5.51e-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: 53.90 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 144 LESDETrDKIVKEILNLDKlekayDNLGKIRKYIKYSIEEKEKfimkteniedlIRTQEKSFTEVLNEIRN------ISS 217
Cdd:TIGR01612 825 IKEDEI-FKIINEMKFMKD-----DFLNKVDKFINFENNCKEK-----------IDSEHEQFAELTNKIKAeisddkLND 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 218 NLPRLRRELEGIKEEVKTLEATFNSITELKLRLGELNGKKGRLE--ERIRQLESGIEEKRKKSKeleEVVKELPELEKKE 295
Cdd:TIGR01612 888 YEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKEsiEKFHNKQNILKEILNKNI---DTIKESNLIEKSY 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 296 TEyrrliEFKDEYLVKKNELEKRLGILSnrlqevkrkIKDAESKvarirwieerlkeiQEKIMKLeprvrefedamrlka 375
Cdd:TIGR01612 965 KD-----KFDNTLIDKINELDKAFKDAS---------LNDYEAK--------------NNELIKY--------------- 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 376 qMESLKSKLGglepeKINEKLLYleNRKKELEEEIDKITRKIGELNQRSKDRRLAIIelkkargkcpVCGRELTEEhkad 455
Cdd:TIGR01612 1002 -FNDLKANLG-----KNKENMLY--HQFDEKEKATNDIEQKIEDANKNIPNIEIAIH----------TSIYNIIDE---- 1059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 456 llrkyslelssIEKEIqeAKALERQLRAEFRKVENELSRLSslktiadqiiEIRERLSKINLEDLKRdkeeyellksesn 535
Cdd:TIGR01612 1060 -----------IEKEI--GKNIELLNKEILEEAEINITNFN----------EIKEKLKHYNFDDFGK------------- 1103
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 536 klkgevESLKKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRllrlGFKTIDELSGRIRELEKFHNKYI---EAKNAEK 612
Cdd:TIGR01612 1104 ------EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK----SENYIDEIKAQINDLEDVADKAIsndDPEEIEK 1173
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 613 ELRDILESLKDER---EELDKAFEELAKIETD---IEKVT----SQLNELQRKFDQKKYEEKRekmmKLSMEIKGLETKL 682
Cdd:TIGR01612 1174 KIENIVTKIDKKKniyDEIKKLLNEIAEIEKDktsLEEVKginlSYGKNLGKLFLEKIDEEKK----KSEHMIKAMEAYI 1249
|
570 580 590
....*....|....*....|....*....|....*..
gi 18202079 683 EELerrrDEIKSTIEKLKEERKERESAKMELEKLNIA 719
Cdd:TIGR01612 1250 EDL----DEIKEKSPEIENEMGIEMDIKAEMETFNIS 1282
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
147-699 |
5.51e-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: 53.90 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 147 DETRDKIVKEILNLDKLEKAYDNLGKIRKYIKySIEEKEKFIMKTENIE-DLIRTQEKSFTEVLNEIRNISSN----LPR 221
Cdd:TIGR01612 1169 EEIEKKIENIVTKIDKKKNIYDEIKKLLNEIA-EIEKDKTSLEEVKGINlSYGKNLGKLFLEKIDEEKKKSEHmikaMEA 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 222 LRRELEGIKEEVKTLEATFNSITELKLRLGELNGKKGRLEERI---RQLESGIEEKRKKSKELEEVVKELP-------EL 291
Cdd:TIGR01612 1248 YIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHiisKKHDENISDIREKSLKIIEDFSEESdindikkEL 1327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 292 EKKETEYRRLIEFKDEYLvkkNELEKRLGILS-NRLQEVKRKIKDAESKvarirwIEERLKEIQEKIMKLEPRVREFEDA 370
Cdd:TIGR01612 1328 QKNLLDAQKHNSDINLYL---NEIANIYNILKlNKIKKIIDEVKEYTKE------IEENNKNIKDELDKSEKLIKKIKDD 1398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 371 MRLKAQMESLKSKLGGLEPEKINEKLLYLENRKKELEEEIDKITRKIGELNQR----------SKDRRLAIIELKKARGK 440
Cdd:TIGR01612 1399 INLEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENvlllfkniemADNKSQHILKIKKDNAT 1478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 441 CPVcGRELTE--EHKaDLLRKYSLELSSIEKEIQEAKALERQLRAEFRKVENELSRLS------SLKTIADQII-EIRER 511
Cdd:TIGR01612 1479 NDH-DFNINElkEHI-DKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAiknkfaKTKKDSEIIIkEIKDA 1556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 512 LSKINLE---------DLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRL 582
Cdd:TIGR01612 1557 HKKFILEaekseqkikEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSF 1636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 583 GFKTIDelsgrirelekfhNKYIEAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYE 662
Cdd:TIGR01612 1637 SIDSQD-------------TELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIE 1703
|
570 580 590
....*....|....*....|....*....|....*..
gi 18202079 663 EKREKMMklsmeikgleTKLEELERRRDEIKSTIEKL 699
Cdd:TIGR01612 1704 KIKEIAI----------ANKEEIESIKELIEPTIENL 1730
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
400-739 |
6.01e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.49 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 400 ENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGKCpvcgrELTEEHKADLLRKYSLELSSIEKEIQEAKALER 479
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKI-----NSEIKNDKEQKNKLEVELNKLEKQKKENKKNID 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 480 QLRAEFRKVENELSRLSSlktiadqiieirerlskiNLEDLKRDKEEYEllkSESNKLKGEVESLKKEVNELNDYKNEST 559
Cdd:TIGR04523 142 KFLTEIKKKEKELEKLNN------------------KYNDLKKQKEELE---NELNLLEKEKLNIQKNIDKIKNKLLKLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 560 KLEIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIRELEKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEELAKIE 639
Cdd:TIGR04523 201 LLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 640 TDIEKVTSQLNELQRKFDQKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEKLNIA 719
Cdd:TIGR04523 281 KKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360
|
330 340
....*....|....*....|
gi 18202079 720 IKRieELRGKIKEYKALIKE 739
Cdd:TIGR04523 361 KQR--ELEEKQNEIEKLKKE 378
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
508-717 |
6.15e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 508 IRERLSKINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLgfkti 587
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 588 delsgriRELEKFHNKYIEAKNAEKELRDILESLkderEELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYE---EK 664
Cdd:COG4717 122 -------EKLLQLLPLYQELEALEAELAELPERL----EELEERLEELRELEEELEELEAELAELQEELEELLEQlslAT 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18202079 665 REKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEKLN 717
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
783-864 |
6.35e-07 |
|
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: 50.51 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 783 ERPLTFLSGGERialglafRLAM-SMYLIGKVDLLILDEPTPFLDEERRrklIEIMERhLRKISQ-----VIIVSHDEEL 856
Cdd:cd03214 92 DRPFNELSGGER-------QRVLlARALAQEPPILLLDEPTSHLDIAHQ---IELLEL-LRRLARergktVVMVLHDLNL 160
|
90
....*....|.
gi 18202079 857 kdA---ADHVI 864
Cdd:cd03214 161 --AaryADRVI 169
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
135-434 |
6.77e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 135 VRQGQIDAILESDETRDKIVKEILNLDKLEKAYDNLGKIRKYIKYSIEEKEKFIMKTEN----IEDLIRTQEKSFTEVLN 210
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeAEAEIEELEAQIEQLKE 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 211 EIRNISSNLPRLRRELEGIKEEV----KTLEATFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVK 286
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAanlrERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 287 ELPELEKKETEYRRLIEFKDEYLVKK-NELEKRLGILSNRLQEVKRKIKDAESKVARirwIEERLKEIQEKIMKLEPRVR 365
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEElRELESKRSELRRELEELREKLAQLELRLEG---LEVRIDNLQERLSEEYSLTL 953
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 366 EF---------EDAMRLKAQMESLKSKLGGL---------EPEKINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDR 427
Cdd:TIGR02168 954 EEaealenkieDDEEEARRRLKRLENKIKELgpvnlaaieEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
....*..
gi 18202079 428 RLAIIEL 434
Cdd:TIGR02168 1034 FKDTFDQ 1040
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
783-864 |
6.83e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 52.76 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 783 ERPLTFLSGGERIALGLAfRLamsmyLIGKVDLLILDEPTPFLDEERRRKLieimERHLRKISQ-VIIVSHDEELKDA-A 860
Cdd:COG0488 147 DRPVSELSGGWRRRVALA-RA-----LLSEPDLLLLDEPTNHLDLESIEWL----EEFLKNYPGtVLVVSHDRYFLDRvA 216
|
....
gi 18202079 861 DHVI 864
Cdd:COG0488 217 TRIL 220
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
144-869 |
7.25e-07 |
|
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: 53.05 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 144 LESDETRDKIVKEILNLDKLEKAYDNLGKIRKYIKYSIEEKEKFIMKTENIEDLIRTQEKSFTEvlNEIRNISSNLPRLR 223
Cdd:pfam02463 439 IELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKE--SKARSGLKVLLALI 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 224 RELEGIKEEVKTLEATFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKETEYRRLIE 303
Cdd:pfam02463 517 KDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 304 FKDEYLVKKNELEKRlgILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRLKAQMESLKSK 383
Cdd:pfam02463 597 LEIDPILNLAQLDKA--TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKE 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 384 LGGLEPEKINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLaIIELKKARGKCPVCGRELTEEHKADLLRKYSLE 463
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE-ELLADRVQEAQDKINEELKLLKQKIDEEEEEEE 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 464 LSSIEKEIQEAKALERQLRAEFRKVENELSRLsslKTIADQIIEIRERLSKINLEDLKRDKEEYELLKSESNKLKGEVES 543
Cdd:pfam02463 754 KSRLKKEEKEEEKSELSLKEKELAEEREKTEK---LKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 544 LKKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLgfktiDELSGRIRELEKFHNKYIEAKNAEKELRDILESLKD 623
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELL-----QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEE 905
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 624 EREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIK--STIEKLKE 701
Cdd:pfam02463 906 SQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVnlMAIEEFEE 985
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 702 ERKERESAKMELEKLNIAIKRIEELRGKIKEYKALIKEEALNKIGEIASEIFSEFTDGKYSGIAIRAEDNKVKLFVIYDG 781
Cdd:pfam02463 986 KEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISA 1065
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 782 VE-----RPLTFLSGGERIALGLAFRLAMSMYliGKVDLLILDEPTPFLDEERRRKLIEiMERHLRKISQVIIVSHDEEL 856
Cdd:pfam02463 1066 RPpgkgvKNLDLLSGGEKTLVALALIFAIQKY--KPAPFYLLDEIDAALDDQNVSRVAN-LLKELSKNAQFIVISLREEM 1142
|
730
....*....|...
gi 18202079 857 KDAADHVIRIRLE 869
Cdd:pfam02463 1143 LEKADKLVGVTMV 1155
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
196-446 |
7.86e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 196 DLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEAtfnSITELKLRLGELNGKKGRLEERIRQLESGIEEKR 275
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER---RIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 276 KKSKELEEVVKE-LPELEKKETEYRRLIEFKDEYLvkkNELEKRLGILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQ 354
Cdd:COG4942 97 AELEAQKEELAElLRALYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 355 EKIMKLEPRVREfedamrLKAQMESLKSKLGGLEpEKINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDR--RLAII 432
Cdd:COG4942 174 AELEALLAELEE------ERAALEALKAERQKLL-ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAaeRTPAA 246
|
250
....*....|....*.
gi 18202079 433 ELKKARGK--CPVCGR 446
Cdd:COG4942 247 GFAALKGKlpWPVSGR 262
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
311-498 |
7.98e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 311 KKNELEKRLGILSNRLQEVKRKIKDAESKVARIR------WIEERLKEIQEKIMKLEPRVREFE-DAMRLKAQMESLKSK 383
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglvDLSEEAKLLLQQLSELESQLAEARaELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 384 LGGLE---PEKINEKLLylenrkKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARgkcpvcgreltEEHKADLLRKY 460
Cdd:COG3206 249 LGSGPdalPELLQSPVI------QQLRAQLAELEAELAELSARYTPNHPDVIALRAQI-----------AALRAQLQQEA 311
|
170 180 190
....*....|....*....|....*....|....*...
gi 18202079 461 SLELSSIEKEIQEAKALERQLRAEFRKVENELSRLSSL 498
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPEL 349
|
|
| YydB |
COG5293 |
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown]; |
222-516 |
8.34e-07 |
|
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown];
Pssm-ID: 444096 [Multi-domain] Cd Length: 572 Bit Score: 52.64 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 222 LRRELEGIKEEVKTLEaTFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEE-----VVKELPELEK--- 293
Cdd:COG5293 145 LRRQGDDFKDPLQLFS-TAQKDADWKLYLAYLLGLDWDLAAEKYELKEEIKELKKLRKALKDeligsVVKSISELRAeil 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 294 -KETEYRRLIEFKDEYLVKKN--ELEKRLGILSNRLQEVKRKIKDAESKVARIrwieERLKEIQEKImkleprvrefeDA 370
Cdd:COG5293 224 eLEEEIEKLEKDLEKFDVAENyeELEKELDELKREINELRNERYSLERRLKKI----ERSLEEEIDI-----------DP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 371 MRLKAQMESLKSKLGGL------EPEKINEKLLylENRKKELEEEIDKITRKIGELNQRSK---DRRLAIIELKKARG-- 439
Cdd:COG5293 289 DELEKLYEEAGVFFPDQvkkrfeEVEAFHKSIV--ENRREYLEEEIAELEAELEELEAELAelgKERAELLSLLDSKGal 366
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18202079 440 -KCpvcgRELTEEHKAdlLRKYSLELSSIEKEIQEAKALERQLRAEFRKVENELsrLSSLKTIADQIIEIRERLSKIN 516
Cdd:COG5293 367 dKY----KELQEELAE--LEAELEELESRLEKLQELEDEIRELKEERAELKEEI--ESDIEERKELLDEINKLFSEIV 436
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
788-874 |
1.01e-06 |
|
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: 50.00 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 788 FLSGGERIALGLAfrLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEELKDAADHVIRIR 867
Cdd:cd03239 94 ILSGGEKSLSALA--LIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLIGVL 171
|
....*..
gi 18202079 868 LEGGASK 874
Cdd:cd03239 172 FVHGVST 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
783-864 |
1.20e-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: 50.22 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 783 ERPLTFLSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEImerhLRKISQ----VIIVSHD-EELK 857
Cdd:cd03235 127 DRQIGELSGGQQQ------RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYEL----LRELRRegmtILVVTHDlGLVL 196
|
....*..
gi 18202079 858 DAADHVI 864
Cdd:cd03235 197 EYFDRVL 203
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
221-516 |
1.29e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 221 RLRRELEGIKEEVKTLEAtfnsitelklRLGELNGKKGRLEERIRQLEsGIEEKRKKSKELEEVVKELPELEKketEYRR 300
Cdd:COG4913 614 ALEAELAELEEELAEAEE----------RLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREIAELEA---ELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 301 LIEFKDEylVKknELEKRLGILSNRLQEVKRKIKDAESKVARirwIEERLKEIQEKIMKLEPRVREFEDAMRLkAQMESL 380
Cdd:COG4913 680 LDASSDD--LA--ALEEQLEELEAELEELEEELDELKGEIGR---LEKELEQAEEELDELQDRLEAAEDLARL-ELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 381 KSKLGGLEPEKINEKLlylenrKKELEEEIDKITRKIGELNQRskdrrlAIIELKKARGKCPVCGRELTEEhkADLLRKY 460
Cdd:COG4913 752 EERFAAALGDAVEREL------RENLEERIDALRARLNRAEEE------LERAMRAFNREWPAETADLDAD--LESLPEY 817
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 18202079 461 SLELSSIEKEI---QEAKALERQLRAEfrkvENELSRLSSlkTIADQIIEIRERLSKIN 516
Cdd:COG4913 818 LALLDRLEEDGlpeYEERFKELLNENS----IEFVADLLS--KLRRAIREIKERIDPLN 870
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
784-871 |
1.32e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.52 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 784 RPLTFLSGGERIALGLAFRLamsMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEELKDAADHV 863
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYEL---LAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
|
....*...
gi 18202079 864 IRIRLEGG 871
Cdd:PRK00635 882 LELGPEGG 889
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
784-875 |
1.43e-06 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 51.25 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 784 RPLTfLSGGE--RIALGLAfrlamsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERhLRK---ISqVIIVSHD-EELK 857
Cdd:COG4148 130 RPAT-LSGGErqRVAIGRA--------LLSSPRLLLMDEPLAALDLARKAEILPYLER-LRDeldIP-ILYVSHSlDEVA 198
|
90 100
....*....|....*....|...
gi 18202079 858 DAADHVI-----RIRLEGGASKV 875
Cdd:COG4148 199 RLADHVVlleqgRVVASGPLAEV 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
789-864 |
1.45e-06 |
|
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: 51.83 E-value: 1.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18202079 789 LSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQ-VIIVSHD-EELKDAADHVI 864
Cdd:COG1123 143 LSGGQRQ------RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTtVLLITHDlGVVAEIADRVV 214
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
784-878 |
2.35e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision 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: 273184 [Multi-domain] Cd Length: 925 Bit Score: 51.55 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 784 RPLTFLSGGERIALGLAFRLamSMYLIGKVdLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEELKDAADHV 863
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKEL--SKRSTGRT-LYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYI 901
|
90
....*....|....*
gi 18202079 864 IRIRLEGGASKVEVV 878
Cdd:TIGR00630 902 IDLGPEGGDGGGTVV 916
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
782-867 |
2.80e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 50.83 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 782 VERPLTFLSGGERialglaFRLAMSMYLIGKVDLLILDEPTPFLDEErrrkLIEIMERHLRKIS-QVIIVSHDEELKDA- 859
Cdd:COG0488 426 AFKPVGVLSGGEK------ARLALAKLLLSPPNVLLLDEPTNHLDIE----TLEALEEALDDFPgTVLLVSHDRYFLDRv 495
|
....*...
gi 18202079 860 ADHVIRIR 867
Cdd:COG0488 496 ATRILEFE 503
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
684-848 |
2.95e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.85 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 684 ELERRRDEIkstIEKLKEERKERESAkmeLEKLnIAIKRIEELRGKIKEYKALIKE--EALNKIGEIASEIFSEFTDgky 761
Cdd:COG0419 83 RIERRQGEF---AEFLEAKPSERKEA---LKRL-LGLEIYEELKERLKELEEALESalEELAELQKLKQEILAQLSG--- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 762 sgiairaednkvklfviYDGVERpltfLSGGERIALGLAfrlamsmyligKVDLLILDepTPFLDEERRRKLIEIMERhL 841
Cdd:COG0419 153 -----------------LDPIET----LSGGERLRLALA-----------DLLSLILD--FGSLDEERLERLLDALEE-L 197
|
....*..
gi 18202079 842 RKISQVI 848
Cdd:COG0419 198 AIITHVI 204
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
165-777 |
3.26e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 50.88 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 165 KAYDNLGKIRKYIKYSIEEKEKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEATFNSIT 244
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 245 ELKLRLGELNGKKGRLEERIRQ----LESGIEEKRKKSKELEeVVKELPELE---KKETEYRRLIEFKDEYLVKKNELEK 317
Cdd:pfam05483 162 ETCARSAEKTKKYEYEREETRQvymdLNNNIEKMILAFEELR-VQAENARLEmhfKLKEDHEKIQHLEEEYKKEINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 318 RLGILSNRLQEVKRKIKD----AESKVARIRWIEERLK----EIQEKIMKLEPRVREFEDamrLKAQMESLKSKLGGLEP 389
Cdd:pfam05483 241 QVSLLLIQITEKENKMKDltflLEESRDKANQLEEKTKlqdeNLKELIEKKDHLTKELED---IKMSLQRSMSTQKALEE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 390 E-KINEKLLYLENRKKELEEEidkitrkigELNQRSKDRRLAIIELKKARGKCPVCGRELTE--EHKADLLRKYSLELSS 466
Cdd:pfam05483 318 DlQIATKTICQLTEEKEAQME---------ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlEKNEDQLKIITMELQK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 467 IEKEIQEAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKINLE---DLKRDKEEYELLKSESNKLKGEVES 543
Cdd:pfam05483 389 KSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQElifLLQAREKEIHDLEIQLTAIKTSEEH 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 544 LKKEVNELndyknestKLEIEIDKAKK-ELSEIEDRLLRLGFKTIDELSGRIRELEKFHNKYIEAKNAEKELRDILESLK 622
Cdd:pfam05483 469 YLKEVEDL--------KTELEKEKLKNiELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 623 DEREELDKAFEELAkietdiEKVTSQLNELQRKFD--QKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLK 700
Cdd:pfam05483 541 EKEMNLRDELESVR------EEFIQKGDEVKCKLDksEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH 614
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18202079 701 EERKE-RESAKMELEKLNIAIKRIEELRGKIkeykalikEEALNKIGEIASEIFSEFTDGKYSGIAIRAEDNKVKLFV 777
Cdd:pfam05483 615 QENKAlKKKGSAENKQLNAYEIKVNKLELEL--------ASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA 684
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
159-748 |
3.85e-06 |
|
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: 51.21 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 159 NLDKLEKAYDNLGKiRKYIKYSIEEKEKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSN-LPRLRRELEGIKEEVKT-- 235
Cdd:TIGR01612 460 KLKALEKRFFEIFE-EEWGSYDIKKDIDENSKQDNTVKLILMRMKDFKDIIDFMELYKPDeVPSKNIIGFDIDQNIKAkl 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 236 -------LEATFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKETEYRRLIEFKDEY 308
Cdd:TIGR01612 539 ykeieagLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKNEY 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 309 LVKKNELEKRLGILSNRLQE--------VKRKIKDAESKVARIRwiEERLKEIQEKIMKL---------EPRVREFEDAM 371
Cdd:TIGR01612 619 IKKAIDLKKIIENNNAYIDElakispyqVPEHLKNKDKIYSTIK--SELSKIYEDDIDALynelssivkENAIDNTEDKA 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 372 R---LKAQMESLKSKLGGLEPEKINEKLLYLENRKKELEEEIDKITRKI-GELNQ---------RSKDRRLA--IIELKK 436
Cdd:TIGR01612 697 KlddLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIhGEINKdlnkiledfKNKEKELSnkINDYAK 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 437 ARGKCPVCGRELTEehkadlLRKYSLELSSIEKEIQEAKALERQLRAEFRKV----ENELSR-LSSLKTIADQIIEIRER 511
Cdd:TIGR01612 777 EKDELNKYKSKISE------IKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTisikEDEIFKiINEMKFMKDDFLNKVDK 850
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 512 LskINLEDLKRDK--EEYELLKSESNKLKGEVESlkkevNELNDYK---NESTKLEIEIDKA-KKELSEIedrllrlgfK 585
Cdd:TIGR01612 851 F--INFENNCKEKidSEHEQFAELTNKIKAEISD-----DKLNDYEkkfNDSKSLINEINKSiEEEYQNI---------N 914
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 586 TIDELSGRIR-------ELEKFHNKYI--------------EAKNAEKELRDILE-SLKDEREELDKAFEELAkietdIE 643
Cdd:TIGR01612 915 TLKKVDEYIKicentkeSIEKFHNKQNilkeilnknidtikESNLIEKSYKDKFDnTLIDKINELDKAFKDAS-----LN 989
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 644 KVTSQLNELQRKFDQKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKL----------------KEERKERE 707
Cdd:TIGR01612 990 DYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIeiaihtsiyniideieKEIGKNIE 1069
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 18202079 708 SAKME-LEKLNIAIKRIEELRGKIKEYK--ALIKEEALNKIGEI 748
Cdd:TIGR01612 1070 LLNKEiLEEAEINITNFNEIKEKLKHYNfdDFGKEENIKYADEI 1113
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
789-871 |
4.39e-06 |
|
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: 47.53 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGERIALGLAfRLamsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLrkiSQVIIVSHDEELKDAADHVIRIRL 868
Cdd:cd03223 92 LSGGEQQRLAFA-RL-----LLHKPKFVFLDEATSALDEESEDRLYQLLKELG---ITVISVGHRPSLWKFHDRVLDLDG 162
|
...
gi 18202079 869 EGG 871
Cdd:cd03223 163 EGG 165
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
789-867 |
5.29e-06 |
|
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: 47.42 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGER----IALGLAFrlamsmyligKVDLLILDEPTPFLDEERRRKLIEIMERhLRK--ISqVIIVSHD-EELKDAAD 861
Cdd:cd03216 83 LSVGERqmveIARALAR----------NARLLILDEPTAALTPAEVERLFKVIRR-LRAqgVA-VIFISHRlDEVFEIAD 150
|
....*.
gi 18202079 862 HVIRIR 867
Cdd:cd03216 151 RVTVLR 156
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
532-749 |
5.59e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.01 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 532 SESNKLkgevesLKKEVNELNDyknESTKLEIEIDKAKKELSEIEDRLLRLGFKTIDELsgrirelEKFHNKYIEAKNAE 611
Cdd:PHA02562 166 SEMDKL------NKDKIRELNQ---QIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENI-------ARKQNKYDELVEEA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 612 KELRDILESLKDEREELDKAFEE----LAKIETDIEKVTSQLNELQR--KFDQK---------KYEEKREKMMKLSMEIK 676
Cdd:PHA02562 230 KTIKAEIEELTDELLNLVMDIEDpsaaLNKLNTAAAKIKSKIEQFQKviKMYEKggvcptctqQISEGPDRITKIKDKLK 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18202079 677 GLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEKLNIAIKRieeLRGKIKEYKALIKE---EALNKIGEIA 749
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLIT---LVDKAKKVKAAIEElqaEFVDNAEELA 382
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
789-867 |
6.46e-06 |
|
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: 47.57 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGERIALGLAFRLAMsmyligKVDLLILDEPTPFLDEERRRKLIEIMERhLRKISQ--VIIVSHD-EELKDAADHVIR 865
Cdd:cd03229 101 LSGGQQQRVALARALAM------DPDVLLLDEPTSALDPITRREVRALLKS-LQAQLGitVVLVTHDlDEAARLADRVVV 173
|
..
gi 18202079 866 IR 867
Cdd:cd03229 174 LR 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
587-744 |
6.70e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 587 IDELSGRIRELEKfhnkyiEAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRK----FDQKKYE 662
Cdd:COG1579 19 LDRLEHRLKELPA------ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvRNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 663 EKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERE----SAKMELEKLNIAI-KRIEELRGKIKEYKALI 737
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEaeleEKKAELDEELAELeAELEELEAEREELAAKI 172
|
....*..
gi 18202079 738 KEEALNK 744
Cdd:COG1579 173 PPELLAL 179
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
446-732 |
7.27e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 446 RELTEEHKADLLRKYSLELSSIEKEiQEAKALER--QLRAEFRKVENELSRLSSLKTIADQIIEIRER-LSKINLEDLKR 522
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKE-EKAREVERrrKLEEAEKARQAEMDRQAAIYAEQERMAMEREReLERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 523 DKEEY--ELLKSESNKLKgEVESLKKEVNElndyKNESTKLEIEIDKAKKELSEIEDRllrlgfktidELSGRIRELEKF 600
Cdd:pfam17380 361 ELERIrqEEIAMEISRMR-ELERLQMERQQ----KNERVRQELEAARKVKILEEERQR----------KIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 601 HNKYIEAKNAEkelrdiLESLKDERE-ELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKyEEKREKMMKLSMEIKGLE 679
Cdd:pfam17380 426 RAEQEEARQRE------VRRLEEERArEMERVRLEEQERQQQVERLRQQEEERKRKKLELE-KEKRDRKRAEEQRRKILE 498
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 18202079 680 TKLEELERRRDEIKSTIEKLKEERKERESAKMELEKLNIAikriEELRGKIKE 732
Cdd:pfam17380 499 KELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA----EEERRKQQE 547
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
788-864 |
7.72e-06 |
|
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: 47.97 E-value: 7.72e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18202079 788 FLSGGERIALGLAfRLamsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISqVIIVSHDEELKDAADHVI 864
Cdd:cd03245 140 GLSGGQRQAVALA-RA-----LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKT-LIIITHRPSLLDLVDRII 209
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
244-738 |
7.79e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.08 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 244 TELKLRLGELNGKKGRL-----EERIRQLESGIEEKRKKSKELEEVVKELPEL-EKKETEYRRLIEFKDEYlvkKNELEK 317
Cdd:COG5022 845 EVLIQKFGRSLKAKKRFsllkkETIYLQSAQRVELAERQLQELKIDVKSISSLkLVNLELESEIIELKKSL---SSDLIE 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 318 RLGILSNRLQEVKRKIKDAESKVARIRWIEE--RLKEIQEKIMKLEPRVREFEDAM--------RLKAQMESLKSKLGgl 387
Cdd:COG5022 922 NLEFKTELIARLKKLLNNIDLEEGPSIEYVKlpELNKLHEVESKLKETSEEYEDLLkkstilvrEGNKANSELKNFKK-- 999
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 388 EPEKINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDR--RLAIIELKKARGKCPVCGRELTEEHKADLLRKYSLELS 465
Cdd:COG5022 1000 ELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESteLSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLD 1079
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 466 SIEKEIQEA-KALERQLRAEFRKVENELSRLSSLKTIAdqiieIRERLSKINLEDlkrdkEEYELLKSESNKLKGEVESL 544
Cdd:COG5022 1080 DKQLYQLEStENLLKTINVKDLEVTNRNLVKPANVLQF-----IVAQMIKLNLLQ-----EISKFLSQLVNTLEPVFQKL 1149
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 545 KK---EVNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLGFKT----IDELSGRIRELEKFH----NKYIEAKNAEKE 613
Cdd:COG5022 1150 SVlqlELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLssseVNDLKNELIALFSKIfsgwPRGDKLKKLISE 1229
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 614 LRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYE-EKREKMMKLSMEIKG------LETKLEELE 686
Cdd:COG5022 1230 GWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEeEVLPATINSLLQYINvglfnaLRTKASSLR 1309
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 18202079 687 RRRDEIK---STIEKLKEERKERESAKMELEKLNIAIKRIEELRGKIKEYKALIK 738
Cdd:COG5022 1310 WKSATEVnynSEELDDWCREFEISDVDEELEELIQAVKVLQLLKDDLNKLDELLD 1364
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
789-872 |
7.85e-06 |
|
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: 47.21 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGERIALGLAfRlamSMYliGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEELKDAADHVirIRL 868
Cdd:cd03246 97 LSGGQRQRLGLA-R---ALY--GNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRI--LVL 168
|
....
gi 18202079 869 EGGA 872
Cdd:cd03246 169 EDGR 172
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
785-864 |
8.36e-06 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 47.77 E-value: 8.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 785 PLTFlSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEELKDA-ADHV 863
Cdd:TIGR02324 147 PATF-SGGEQQ------RVNIARGFIADYPILLLDEPTASLDAANRQVVVELIAEAKARGAALIGIFHDEEVRELvADRV 219
|
.
gi 18202079 864 I 864
Cdd:TIGR02324 220 M 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
741-866 |
1.00e-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: 47.50 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 741 ALN---KIGEIASEIFseftdgKYSGIAIRAEDNKVKLFVIYDGVERPLTF-------LSGGE--RIALGLAfrlamsmy 808
Cdd:cd03257 94 SLNprmTIGEQIAEPL------RIHGKLSKKEARKEAVLLLLVGVGLPEEVlnrypheLSGGQrqRVAIARA-------- 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18202079 809 LIGKVDLLILDEPTPFLDEERRRKLIEIMeRHLRKISQ--VIIVSHDEEL-KDAADHVIRI 866
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLL-KKLQEELGltLLFITHDLGVvAKIADRVAVM 219
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
177-715 |
1.04e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 49.33 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 177 IKYSIEEKEKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEATFN-SITELKLRLGELN- 254
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfVVTEFEATTCSLEe 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 255 ---GKKGRLEERIRQLESGIEEKRKKSKELEEVVK-------ELPELEKKETEYRRLIEFKDEYLVKKNELEKRLGILSN 324
Cdd:pfam05483 364 llrTEQQRLEKNEDQLKIITMELQKKSSELEEMTKfknnkevELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIF 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 325 RLQEVKRKIKDAESKVARIRWIEER-LKEIQEKIMKLEprvrefedamrlkaqmeslksklgglepekiNEKLlylenRK 403
Cdd:pfam05483 444 LLQAREKEIHDLEIQLTAIKTSEEHyLKEVEDLKTELE-------------------------------KEKL-----KN 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 404 KELEEEIDKITRKIGELNQRSKDrrlAIIELKKargkcpvcgrelteeHKADLLRKYSLElSSIEKEIQEAKALERQLRA 483
Cdd:pfam05483 488 IELTAHCDKLLLENKELTQEASD---MTLELKK---------------HQEDIINCKKQE-ERMLKQIENLEEKEMNLRD 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 484 EFRKVENELSRLSSlkTIADQIIEIRERLSKINLEDLKRDKeEYELLKSESNKLKGEVESLKKEVNE------------- 550
Cdd:pfam05483 549 ELESVREEFIQKGD--EVKCKLDKSEENARSIEYEVLKKEK-QMKILENKCNNLKKQIENKNKNIEElhqenkalkkkgs 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 551 -----LNDYKNESTKLEIEIDKAKKELSEIEDRLLR-LGFKTIDElSGRIRELEKFHNKYIEAKNAEKELrdileslkDE 624
Cdd:pfam05483 626 aenkqLNAYEIKVNKLELELASAKQKFEEIIDNYQKeIEDKKISE-EKLLEEVEKAKAIADEAVKLQKEI--------DK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 625 REElDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYEEKREKMMKLSMEIkgletkleELERRRDEIKSTIEKLKEERK 704
Cdd:pfam05483 697 RCQ-HKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEI--------ELSNIKAELLSLKKQLEIEKE 767
|
570
....*....|.
gi 18202079 705 ERESAKMELEK 715
Cdd:pfam05483 768 EKEKLKMEAKE 778
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
782-864 |
1.24e-05 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 47.70 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 782 VERPLTFLSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDeeLKDA-- 859
Cdd:PRK11231 132 ADRRLTDLSGGQRQ------RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD--LNQAsr 203
|
....*.
gi 18202079 860 -ADHVI 864
Cdd:PRK11231 204 yCDHLV 209
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-174 |
1.28e-05 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 48.12 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 3 IERVIVQNFRSHKNS-EIEFKPG------INLIIGQNGAGKSSLLDAI--LVGLYWSKRMRLRGLKKD--EFTRTGTRGA 71
Cdd:COG1106 2 LISFSIENFRSFKDElTLSMVASglrllrVNLIYGANASGKSNLLEALyfLRNLVLNSSQPGDKLVEPflLDSESKNEPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 72 IIEITFEEDGTKYKVlrdfarNVSYLKRLDGREWRHVTETSMESVSSFIDRIipYNVFLNAIYVRQGQIDAILESDETRD 151
Cdd:COG1106 82 EFEILFLLDGVRYEY------GFELDKERIISEWLYFLSTAAQLNVPLLSPL--YDWFDNNISLDTSSDGLTLLLKEDES 153
|
170 180
....*....|....*....|...
gi 18202079 152 kIVKEILNLdkLEKAYDNLGKIR 174
Cdd:COG1106 154 -LKEELLEL--LKIADPGIEDIE 173
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
329-579 |
1.54e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 329 VKRKIKDAESkvaRIRWIEERLKEIQEKIMKLEPRVREFedamrlkaqmeslksklgglepeKINEKLLYLENRKKELEE 408
Cdd:COG3206 166 LELRREEARK---ALEFLEEQLPELRKELEEAEAALEEF-----------------------RQKNGLVDLSEEAKLLLQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 409 EIDKITRKIGELNQRSKDRRLAIIELKKARGKCPVCGRELTEehkadllrkySLELSSIEKEIQEAKALERQLRAEFRkv 488
Cdd:COG3206 220 QLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ----------SPVIQQLRAQLAELEAELAELSARYT-- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 489 enelSRLSSLKTIADQIIEIRERLSKINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDYKNESTKLEIEIDKA 568
Cdd:COG3206 288 ----PNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
|
250
....*....|.
gi 18202079 569 KKELSEIEDRL 579
Cdd:COG3206 364 RELYESLLQRL 374
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
337-650 |
1.68e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.39 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 337 ESKVARIRWIEERLKEIQEKIMKLEpRVREFEdamrlkaqmESLKSKLGGLEPEKINEKLLYLENRKKELEEEIDKITRK 416
Cdd:PRK05771 39 ELSNERLRKLRSLLTKLSEALDKLR-SYLPKL---------NPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 417 IGELNQRSKDRRLAIIELKKARGkcpvcgreLTEEHKADLLRKY-SLELSSIEKEIQEAKALERQLRAEFRKVENELSRL 495
Cdd:PRK05771 109 ISELENEIKELEQEIERLEPWGN--------FDLDLSLLLGFKYvSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 496 SSLKTIADQIIEIRERL-----SKINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDyknestKLEIEIDKAKK 570
Cdd:PRK05771 181 VVVVVLKELSDEVEEELkklgfERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAK------KYLEELLALYE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 571 ELSEIEDRLlrlgfktidELSGRIRELEKFHnkYIEAKNAEKELRDILESLKDEREelDKAFEELAKIETDIEKVTSQLN 650
Cdd:PRK05771 255 YLEIELERA---------EALSKFLKTDKTF--AIEGWVPEDRVKKLKELIDKATG--GSAYVEFVEPDEEEEEVPTKLK 321
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
457-751 |
1.73e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 457 LRKYSLELSSIEKEIQEAKALERQLRAEFRKVENELSRL-SSLKTIADQIIEIRERLSKINlEDLKRDKEEYELLKSESN 535
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELnAQVKELREEAQELREKRDELN-EKVKELKEERDELNEKLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 536 KLKGEVESLKKEVNELNdyknestKLEIEIDKAKKELSEIEDRLLR--LGFKTIDELSGRIRELEKFHNKYIEAKNAEKE 613
Cdd:COG1340 89 ELREELDELRKELAELN-------KAGGSIDKLRKEIERLEWRQQTevLSPEEEKELVEKIKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 614 LRDILESLKDEREELDKAFEELakietdiekvtsqlnelqrkfdqkkyEEKREKMMKLSMEIKGLETKLEELERRRDEIK 693
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKI--------------------------KELAEEAQELHEEMIELYKEADELRKEADELH 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 18202079 694 STIEKLKEErkeresAKMELEKLNIAIKRIEELRGKIKEYKALIKEEALNKIGEIASE 751
Cdd:COG1340 216 KEIVEAQEK------ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEE 267
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
587-739 |
1.87e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 587 IDELSGRIRELEKfhnkyiEAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELqrkfdQKKYEEKRE 666
Cdd:COG3883 18 IQAKQKELSELQA------ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-----EAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 667 KMMKL--SMEIKGLET-----------------KLEELERRRDEIKSTIEKLKEERKERESAKMELE-KLNIAIKRIEEL 726
Cdd:COG3883 87 ELGERarALYRSGGSVsyldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEaKLAELEALKAEL 166
|
170
....*....|...
gi 18202079 727 RGKIKEYKALIKE 739
Cdd:COG3883 167 EAAKAELEAQQAE 179
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
194-434 |
1.88e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.39 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 194 IEDLirtQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEATFNSITELKL---------RLGELNGKKGRLEERI 264
Cdd:PRK05771 33 IEDL---KEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLeelikdveeELEKIEKEIKELEEEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 265 RQLESGIEEKRKKSKELEeVVKELPELEKKETEYRRLIEFKdeYLVKKNELEKRLGILSNRLQEVkrkIKDAESKVARIR 344
Cdd:PRK05771 110 SELENEIKELEQEIERLE-PWGNFDLDLSLLLGFKYVSVFV--GTVPEDKLEELKLESDVENVEY---ISTDKGYVYVVV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 345 WIEERLKEIQEKIMKlEPRVREFEDamrlkaqmeslksklggLEPEKINEKLLYLENRKKELEEEIDKITRKIGELNQRS 424
Cdd:PRK05771 184 VVLKELSDEVEEELK-KLGFERLEL-----------------EEEGTPSELIREIKEELEEIEKERESLLEELKELAKKY 245
|
250
....*....|
gi 18202079 425 KDRRLAIIEL 434
Cdd:PRK05771 246 LEELLALYEY 255
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-103 |
1.92e-05 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 47.18 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 3 IERVIVQNFRSHK-NSEIEFKPGINLIIGQNGAGKSSLLDAI--LVGLYwSKRMRLRGLK----KDEFTRTGTRGAIIEI 75
Cdd:cd03275 1 LKRLELENFKSYKgRHVIGPFDRFTCIIGPNGSGKSNLMDAIsfVLGEK-SSHLRSKNLKdliyRARVGKPDSNSAYVTA 79
|
90 100
....*....|....*....|....*...
gi 18202079 76 TFEEDGTKYKVLRDFARNVSYLKRLDGR 103
Cdd:cd03275 80 VYEDDDGEEKTFRRIITGGSSSYRINGK 107
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
4-54 |
1.96e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 42.97 E-value: 1.96e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 18202079 4 ERVIVQNFRSHKNSEIEFKP-GINLIIGQNGAGKSSLLDAILVGLYWSKRMR 54
Cdd:pfam13555 2 TRLQLINWGTFDGHTIPIDPrGNTLLTGPSGSGKSTLLDAIQTLLVPAKRAR 53
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
785-864 |
1.99e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.56 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 785 PLTfLSGGE--RIALGLAfrlamsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVII-VSHD-EELKDAA 860
Cdd:PRK11144 126 PGS-LSGGEkqRVAIGRA--------LLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILyVSHSlDEILRLA 196
|
....
gi 18202079 861 DHVI 864
Cdd:PRK11144 197 DRVV 200
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
789-864 |
2.01e-05 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 46.77 E-value: 2.01e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18202079 789 LSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHD-EELKDAADHVI 864
Cdd:COG4555 133 LSTGMKK------KVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHImQEVEALCDRVV 203
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
3-78 |
2.09e-05 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 47.20 E-value: 2.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18202079 3 IERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAILVglywskrmrLRGLKKD-EFTRTGTRGAIIEITFE 78
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALSL---------LLGGRASaDLIRSGAEKAVVEGVFD 68
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
290-733 |
2.12e-05 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 48.67 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 290 ELEKKETEYRRLIEFKDEYLVKKNELEKRLGILSNRLQEV---KRKIKDAESKVA-RIRWIEERLKEIQEKIMKLEPRVR 365
Cdd:PTZ00440 743 EEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFlqyKDTILNKENKISnDINILKENKKNNQDLLNSYNILIQ 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 366 EFEDAMRLKAqmESLKSKLGGLEPEKINEKLLYLENRKKELEEEIDKITRKIGELNQRSKdrrlAIIELKKARGKCPVCG 445
Cdd:PTZ00440 823 KLEAHTEKND--EELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNIN----IIKTLNIAINRSNSNK 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 446 RELTE--EHKADLLRKYSLELSSIEK----EIQEAKALERQLRAEFRKVENELS--RLSSLKTIADQIIEIRERLS---- 513
Cdd:PTZ00440 897 QLVEHllNNKIDLKNKLEQHMKIINTdniiQKNEKLNLLNNLNKEKEKIEKQLSdtKINNLKMQIEKTLEYYDKSKenin 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 514 ---KINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVN-----------ELNDYKNESTKLEIEiDKAKKELSEIEDRL 579
Cdd:PTZ00440 977 gndGTHLEKLDKEKDEWEHFKSEIDKLNVNYNILNKKIDdlikkqhddiiELIDKLIKEKGKEIE-EKVDQYISLLEKMK 1055
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 580 LRLGFKTIDElsgrirELEKFHNKYI--EAKNAEKELRDILESLKDEREELD--KAFEELAKIETDIEKVTSQLNELQRK 655
Cdd:PTZ00440 1056 TKLSSFHFNI------DIKKYKNPKIkeEIKLLEEKVEALLKKIDENKNKLIeiKNKSHEHVVNADKEKNKQTEHYNKKK 1129
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 656 FDQKKYEEKREKMMKLSMEIKGLETKLEELERRRDE-----IKSTIEKLKEERKEresAKMELEKLNIAIKRIEELRGKI 730
Cdd:PTZ00440 1130 KSLEKIYKQMEKTLKELENMNLEDITLNEVNEIEIEyerilIDHIVEQINNEAKK---SKTIMEEIESYKKDIDQVKKNM 1206
|
...
gi 18202079 731 KEY 733
Cdd:PTZ00440 1207 SKE 1209
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
266-752 |
2.15e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 266 QLESGIEEKRKKSKELEEVVKELPELEKKETEYRR--LIEFKDEYLVKKNELEKRLGI----------LSNRLQEVKRKI 333
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRqsVIDLQTKLQEMQMERDAMADIrrresqsqedLRNQLQNTVHEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 334 -----------KDAESKVARIRWI----EERLKEIQEKIMKLEPR--------------------------VREFEDAMR 372
Cdd:pfam15921 155 eaakclkedmlEDSNTQIEQLRKMmlshEGVLQEIRSILVDFEEAsgkkiyehdsmstmhfrslgsaiskiLRELDTEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 373 -LKAQMESLKSKLGGLEPEKINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRR---------LAIIElKKARGKCP 442
Cdd:pfam15921 235 yLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARsqansiqsqLEIIQ-EQARNQNS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 443 VCGRELTEEHKAdllrkysleLSSIEKEIQEAKaleRQLRAEFRKVENEL----SRLSSLKTIADQIIE----IRERLSK 514
Cdd:pfam15921 314 MYMRQLSDLEST---------VSQLRSELREAK---RMYEDKIEELEKQLvlanSELTEARTERDQFSQesgnLDDQLQK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 515 InLEDLKRDKEEYELLKSESNKL----KGEVESLKKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRllrlgfkTIDEL 590
Cdd:pfam15921 382 L-LADLHKREKELSLEKEQNKRLwdrdTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMER-------QMAAI 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 591 SGRIRELEKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEELAKI-------ETDIEKVTSQLNELQRKFDQKKYE- 662
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLtaslqekERAIEATNAEITKLRSRVDLKLQEl 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 663 ----EKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKE--ERKERESAKMELEKLNIAiKRIEELRGKIKEYKAL 736
Cdd:pfam15921 534 qhlkNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvGQHGRTAGAMQVEKAQLE-KEINDRRLELQEFKIL 612
|
570
....*....|....*.
gi 18202079 737 iKEEALNKIGEIASEI 752
Cdd:pfam15921 613 -KDKKDAKIRELEARV 627
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
789-866 |
2.22e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.48 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGE--RIalglafRLAMSmylIGK--VDLL-ILDEPTPFL---DEERrrkLIEIMeRHLRKI-SQVIIVSHDEELKDA 859
Cdd:COG0178 486 LSGGEaqRI------RLATQ---IGSglVGVLyVLDEPSIGLhqrDNDR---LIETL-KRLRDLgNTVIVVEHDEDTIRA 552
|
....*..
gi 18202079 860 ADHVIRI 866
Cdd:COG0178 553 ADYIIDI 559
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
785-853 |
2.33e-05 |
|
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: 48.01 E-value: 2.33e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 785 PLTFLSGGERialglaFRLAMSMYLIGKVDLLILDEPTPFLDEERrrklIEIMERHLRKIS-QVIIVSHD 853
Cdd:TIGR03719 158 DVTKLSGGER------RRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPgTVVAVTHD 217
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
259-732 |
2.66e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 259 RLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKETE-YRRLIEFKDEYLVKKNELEKRLGILSNRLQEVKRkikdae 337
Cdd:pfam01576 16 KVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETElCAEAEEMRARLAARKQELEEILHELESRLEEEEE------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 338 skvaRIRWIEERLKEIQEKIMKLEPRVREFEDAmRLKAQME--SLKSKLgglepEKINEKLLYLENR-------KKELEE 408
Cdd:pfam01576 90 ----RSQQLQNEKKKMQQHIQDLEEQLDEEEAA-RQKLQLEkvTTEAKI-----KKLEEDILLLEDQnsklskeRKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 409 EIDKITRKIGELNQRSK------DRRLAIIELKKARGKCPVCGRELTEEHKadllRKYSLELSSIEKEIQEAKALERQLR 482
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKslsklkNKHEAMISDLEERLKKEEKGRQELEKAK----RKLEGESTDLQEQIAELQAQIAELR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 483 AEFRKVENEL---------------SRLSSLKTIADQIIEI-----RERLSKINLEDLKRD-KEEYELLKSE-------- 533
Cdd:pfam01576 236 AQLAKKEEELqaalarleeetaqknNALKKIRELEAQISELqedleSERAARNKAEKQRRDlGEELEALKTEledtldtt 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 534 ------SNKLKGEVESLKK----------------------EVNELNDYKNESTKLEIEIDKAK----KELSEIEDRLLR 581
Cdd:pfam01576 316 aaqqelRSKREQEVTELKKaleeetrsheaqlqemrqkhtqALEELTEQLEQAKRNKANLEKAKqaleSENAELQAELRT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 582 LGFKTIDELSGRIR---ELEKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEEL----AKIETDIEKVTSQLNELQ- 653
Cdd:pfam01576 396 LQQAKQDSEHKRKKlegQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAegknIKLSKDVSSLESQLQDTQe 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 654 ----------------------RKFDQKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERK----ERE 707
Cdd:pfam01576 476 llqeetrqklnlstrlrqledeRNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKrlqrELE 555
|
570 580
....*....|....*....|....*
gi 18202079 708 SAKMELEKLNIAIKRIEELRGKIKE 732
Cdd:pfam01576 556 ALTQQLEEKAAAYDKLEKTKNRLQQ 580
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
786-876 |
3.10e-05 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 46.52 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 786 LTFLSGGERIALGLAfrLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKiSQVIIVSHDEELKDAADHVIR 865
Cdd:cd03273 164 LTELSGGQRSLVALS--LILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKG-SQFIVVSLKEGMFNNANVLFR 240
|
90
....*....|.
gi 18202079 866 IRLEGGASKVE 876
Cdd:cd03273 241 TRFVDGTSTVT 251
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
785-853 |
3.14e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 3.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 785 PLTFLSGGERialglaFRLAMSMYLIGKVDLLILDEPTPFLDEERrrklIEIMERHLRKIS-QVIIVSHD 853
Cdd:PRK11819 160 KVTKLSGGER------RRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWLEQFLHDYPgTVVAVTHD 219
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
496-733 |
3.42e-05 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 46.59 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 496 SSLKTIADQIIEIRERLSKINLEDLKRD-KEEYELLKSESNKLKGEVESLkkeVNELNDYKNESTKLEIEIDKAKKELSE 574
Cdd:cd22656 91 SYYAEILELIDDLADATDDEELEEAKKTiKALLDDLLKEAKKYQDKAAKV---VDKLTDFENQTEKDQTALETLEKALKD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 575 I-EDRLLRLGFKTIDELsgrIRELEKFHNKYI-EAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNEL 652
Cdd:cd22656 168 LlTDEGGAIARKEIKDL---QKELEKLNEEYAaKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 653 QRKFdqkkyeekrEKMMKLSMEIKgletkleelerrrDEIKSTIEKLKEERKERESAKMELEKLNIAIKRIEELRGKIKE 732
Cdd:cd22656 245 IPAL---------EKLQGAWQAIA-------------TDLDSLKDLLEDDISKIPAAILAKLELEKAIEKWNELAEKADK 302
|
.
gi 18202079 733 Y 733
Cdd:cd22656 303 F 303
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
783-878 |
3.68e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 783 ERPLTFLSGGERIALGLAFRLAMSMYLIgkvdLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEELKDAADH 862
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIGI----TYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADR 546
|
90
....*....|....*.
gi 18202079 863 VIRIRLEGGASKVEVV 878
Cdd:PRK00635 547 IIDIGPGAGIFGGEVL 562
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
533-750 |
3.71e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 533 ESNKLKGEVESLKKEVNELNDYKNESTKLEIEIDKakkeLSEIEDRllrlgFKTIDELSGRIRELEKFhNKYIEAKNAEK 612
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEL----LEPIREL-----AERYAAARERLAELEYL-RAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 613 ELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYEEKREkmmkLSMEIKGLETKLEELERRRDEI 692
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ----LEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18202079 693 KSTIEKLKEE--------RKERESAKMELEKLNIAIKRIEELRGKIKEYKALIKEEALNKIGEIAS 750
Cdd:COG4913 365 EALLAALGLPlpasaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
161-380 |
4.57e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 161 DKLEKAYDNLGKIRKYIKYSIEEKEKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEAtf 240
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 241 nSITELKLRLGEL------NGKKGRLE------------ERIRQLESGIEEKRKKSKELEEVVKELPELEKK-ETEYRRL 301
Cdd:COG4942 98 -ELEAQKEELAELlralyrLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAElEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18202079 302 IEFKDEYLVKKNELEKRLGILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRLKAQMESL 380
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
509-747 |
4.64e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.04 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 509 RERLSKINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDYKNESTKLEIEIDKA--KKELSEIEDRLLRLGFKT 586
Cdd:pfam17380 290 QEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMEREREleRIRQEERKRELERIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 587 IDELSGRIRELEKFHnkyIEAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQlNELQRKFDQKKYEEKRE 666
Cdd:pfam17380 370 IAMEISRMRELERLQ---MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE-QEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 667 KMMKlsmeikglETKLEELERRRDeikstIEKLKEERKERESAKMELEKLNIAIKRIEELRGKIKEY------KALIKEE 740
Cdd:pfam17380 446 REME--------RVRLEEQERQQQ-----VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeleerkQAMIEEE 512
|
....*..
gi 18202079 741 ALNKIGE 747
Cdd:pfam17380 513 RKRKLLE 519
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
608-736 |
4.91e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 46.16 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 608 KNAEKELRDILESLKDEREELDKafeELAKIETDIEKVTSQLNELQRKFDQKKYEEK-------------REKMMKLSME 674
Cdd:smart00787 143 EGLKEGLDENLEGLKEDYKLLMK---ELELLNSIKPKLRDRKDALEEELRQLKQLEDeledcdpteldraKEKLKKLLQE 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18202079 675 IKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEKL-----NIAIKRIEELRGKIKEYKAL 736
Cdd:smart00787 220 IMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKleqcrGFTFKEIEKLKEQLKLLQSL 286
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
419-738 |
5.96e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 419 ELNQRSKDRRLAIIELKKargKCPVCGRELTEEHkaDLLRKYSLELSSIEKEIQEA-KALERQLRAEFRKVENELSRLSS 497
Cdd:pfam05557 17 EKKQMELEHKRARIELEK---KASALKRQLDRES--DRNQELQKRIRLLEKREAEAeEALREQAELNRLKKKYLEALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 498 LKTIADQIIEIRERLSKIN--LEDLKRDKEEYELLKSESNKlkgEVESLKKEVNELNDYKNESTKLEIEIDKAKKELSEI 575
Cdd:pfam05557 92 LNEKESQLADAREVISCLKneLSELRRQIQRAELELQSTNS---ELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 576 EDRLLRLgfktidelsgrIRELEKFHNKYIEAKNAEKELRDILEsLKDEREELDKAFEELAKIETDIEKVTSQLNELQRK 655
Cdd:pfam05557 169 EQRIKEL-----------EFEIQSQEQDSEIVKNSKSELARIPE-LEKELERLREHNKHLNENIENKLLLKEEVEDLKRK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 656 FDQkkYEEKREKMMKLSMEIKGLETKL-----------------EELERRRDEIKSTIEKLKEER-------KERESAKM 711
Cdd:pfam05557 237 LER--EEKYREEAATLELEKEKLEQELqswvklaqdtglnlrspEDLSRRIEQLQQREIVLKEENssltssaRQLEKARR 314
|
330 340
....*....|....*....|....*...
gi 18202079 712 ELE-KLNIAIKRIEELRGKIKEYKALIK 738
Cdd:pfam05557 315 ELEqELAQYLKKIEDLNKKLKRHKALVR 342
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
565-723 |
6.15e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 565 IDKAKKELSEIEDRLLrlgFKTIDELSGRIRELEKfhnkyiEAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEK 644
Cdd:PRK12704 44 LEEAKKEAEAIKKEAL---LEAKEEIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 645 VTSQLNELQRKFDQKK--YEEKREKMMKLSMEIKGL---ETK---LEELERR-RDEIKSTIEKLKEERKEResAKMELEK 715
Cdd:PRK12704 115 KEKELEQKQQELEKKEeeLEELIEEQLQELERISGLtaeEAKeilLEKVEEEaRHEAAVLIKEIEEEAKEE--ADKKAKE 192
|
....*....
gi 18202079 716 LNI-AIKRI 723
Cdd:PRK12704 193 ILAqAIQRC 201
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
770-852 |
6.59e-05 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 44.61 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 770 DNKVKLF--VIYDGVERPLtflSGGERialglaFRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISqV 847
Cdd:cd03247 81 NQRPYLFdtTLRNNLGRRF---SGGER------QRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKT-L 150
|
....*
gi 18202079 848 IIVSH 852
Cdd:cd03247 151 IWITH 155
|
|
| ASY3-like |
pfam20435 |
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific ... |
597-739 |
7.25e-05 |
|
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific proteins, such as AtASY3 from Arabidopsis and PAIR3 from rice. They are coiled-coil domain proteins required for normal meiosis. PAIR3 is an axial element and part of the synaptonemal complex (SC) that forms between homologous chromosomes during meiosis. Members of this family are homologs of SCYP2 from vertebrates and fungal Red1/Rec10.
Pssm-ID: 466584 [Multi-domain] Cd Length: 793 Bit Score: 46.42 E-value: 7.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 597 LEKFHNKYIEAknAEKELRDILESLKderEELDKAFEEL-AKIETDIEKvTSQLNELQRKFDQKKYEEKREKMMKL---- 671
Cdd:pfam20435 637 LQNFERKLKSA--AEKKSSEIIASVS---EEIHLELENIkSHIITEAGK-TSNLAKTKRKHAETRLQEQEEKMRMIhekf 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 672 ----SMEIKGLETKLEELERRRDEIKSTIeklKEERKERESAKMELE-----KLNIAIKRIEEL----RGKIKEYKALIK 738
Cdd:pfam20435 711 kddvSHHLEDFKSTIEELEANQSELKGSI---KKQRTSHQKLIAHFEggietKLDDATKRIDSVnksaRGKMLQLKMIVA 787
|
.
gi 18202079 739 E 739
Cdd:pfam20435 788 E 788
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
783-867 |
7.42e-05 |
|
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: 45.08 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 783 ERPLTFLSGGER----IAlglafRlAMsmylIGKVDLLILDEPTPFLDEERRRKLIEIMER-HLRKISQVIIVSHD-EEL 856
Cdd:COG1119 137 DRPFGTLSQGEQrrvlIA-----R-AL----VKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVLVTHHvEEI 206
|
90
....*....|.
gi 18202079 857 KDAADHVIRIR 867
Cdd:COG1119 207 PPGITHVLLLK 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
774-863 |
8.12e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 774 KLFVIYDGVERPLTFLSGGE-RIALglafrlaMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMER-HLRKISQVIIVS 851
Cdd:PRK10938 121 QQFGITALLDRRFKYLSTGEtRKTL-------LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLN 193
|
90
....*....|..
gi 18202079 852 HDEELKDAADHV 863
Cdd:PRK10938 194 RFDEIPDFVQFA 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
783-856 |
8.18e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 45.38 E-value: 8.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18202079 783 ERPLTFLSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEEL 856
Cdd:PRK13638 131 HQPIQCLSHGQKK------RVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL 198
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
784-874 |
8.67e-05 |
|
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: 44.38 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 784 RPLTFLSGGER--IALGLAFrlamSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMeRHLRKISQVIIVSHDEELKDAAD 861
Cdd:cd03278 109 QRLSLLSGGEKalTALALLF----AIFRVRPSPFCVLDEVDAALDDANVERFARLL-KEFSKETQFIVITHRKGTMEAAD 183
|
90
....*....|....
gi 18202079 862 HVIRIRL-EGGASK 874
Cdd:cd03278 184 RLYGVTMqESGVSK 197
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
257-417 |
9.30e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 257 KGRLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKETEYRRLIEFKDEYLVKKNELEKRLGILSNRLQEVKRKIKDA 336
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 337 ESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRLKAQmeslksKLGGLEPEKINEKLlyLENRKKELEEEIDKITRK 416
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE------RISGLTAEEAKEIL--LEKVEEEARHEAAVLIKE 177
|
.
gi 18202079 417 I 417
Cdd:PRK12704 178 I 178
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
2-536 |
1.07e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 45.88 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 2 KIERVI-VQNFRSHKN-SEIEFKPGINLIIGQNGAGKSSLldailvglywSKRMRLRGLKKDEFTRTgtrgAIIEITFEE 79
Cdd:COG4694 1 MITKIKkLKNVGAFKDfGWLAFFKKLNLIYGENGSGKSTL----------SRILRSLELGDTSSEVI----AEFEIEAGG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 80 DGTKYKVL---RDFARnvsylkrldgrewrhvtetsmESVSSFIDriipynvFLNAIYVRQGQIDAilesDETRDKIVKE 156
Cdd:COG4694 67 SAPNPSVRvfnRDFVE---------------------ENLRSGEE-------IKGIFTLGEENIEL----EEEIEELEKE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 157 ILNLD-KLEKAYDNLGKIRKYIKYSIEEKEKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSN-LPRLRRELEGIKEEVK 234
Cdd:COG4694 115 IEDLKkELDKLEKELKEAKKALEKLLEDLAKSIKDDLKKLFASSGRNYRKANLEKKLSALKSSsEDELKEKLKLLKEEEP 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 235 TLEATFNSITELKlrlGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKETEYR-----------RLIE 303
Cdd:COG4694 195 EPIAPITPLPDLK---ALLSEAETLLEKSAVSSAIEELAALIQNPGNSDWVEQGLAYHKEEEDDTcpfcqqelaaeRIEA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 304 FkDEYLvkKNELEKRLGILSNRLQEVKRKIKDAESKVARIrwIEERLKEIQEKImkleprvreFEDAMRLKAQMESLKSK 383
Cdd:COG4694 272 L-EAYF--DDEYEKLLAALKDLLEELESAINALSALLLEI--LRTLLPSAKEDL---------KAALEALNALLETLLAA 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 384 LGGLEPEKINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGKCPVCgrELTEEhkadlLRKYSLE 463
Cdd:COG4694 338 LEEKIANPSTSIDLDDQELLDELNDLIAALNALIEEHNAKIANLKAEKEEARKKLEAHELA--ELKED-----LSRYKAE 410
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18202079 464 LSSIEKEIQEAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRERL--SKINLEDLKRDKEEYELLKSESNK 536
Cdd:COG4694 411 VEELIEELKTIKALKKALEDLKTEISELEAELSSVDEAADEINEELKALgfDEFSLEAVEDGRSSYRLKRNGEND 485
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-44 |
1.56e-04 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 44.21 E-value: 1.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 18202079 1 MKIERVIVQNFRSH-KNSEIE-FKPGINLIIGQNGAGKSSLLDAIL 44
Cdd:cd03273 1 MHIKEIILDGFKSYaTRTVISgFDPQFNAITGLNGSGKSNILDAIC 46
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
739-879 |
1.66e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.92 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 739 EEALNKIGEIASEIFSEFTDGkysgIAIRAEDNKVKLFVIYDGVERPLT--FLSGGERIALGLAFRLamsmYLIGKVDLL 816
Cdd:COG4637 211 PERFERILEALRDAFPGFEDI----EVEPDEDGRVLLEFREKGLDRPFParELSDGTLRFLALLAAL----LSPRPPPLL 282
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18202079 817 ILDEPTPFLDEERRRKLIEIMERHLRKiSQVIIVSHDEELKDA--ADHVIRI-RLEGGASKVEVVS 879
Cdd:COG4637 283 CIEEPENGLHPDLLPALAELLREASER-TQVIVTTHSPALLDAlePEEVLVLeREDDGETRIRRLS 347
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
463-658 |
1.94e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 463 ELSSIEKEIQEAkalERQLRaEFRKvENELSRLSS-LKTIADQIIEIRERLSKINLEdLKRDKEEYELLKSESNKLKGEV 541
Cdd:COG3206 183 QLPELRKELEEA---EAALE-EFRQ-KNGLVDLSEeAKLLLQQLSELESQLAEARAE-LAEAEARLAALRAQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 542 ESLKKEvNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLGfKTIDELSGRIRE-----LEKFHNKYIEAKNAEKELRD 616
Cdd:COG3206 257 PELLQS-PVIQQLRAQLAELEAELAELSARYTPNHPDVIALR-AQIAALRAQLQQeaqriLASLEAELEALQAREASLQA 334
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 18202079 617 ILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQ 658
Cdd:COG3206 335 QLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
809-863 |
2.07e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.01 E-value: 2.07e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 18202079 809 LIGKVDLLILDEPTPFLDEERRRKLIEIMERhLRK--ISqVIIVSHD-EELKDAADHV 863
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRR-LKAqgVA-IIYISHRlDEVFEIADRV 210
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-774 |
2.07e-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: 45.35 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 2 KIERVIVQNFRSHKN-SEIEFKPGINLIIGQNGAGKSSLLDAILVGLYWSKRMRLRGLKKDEFTRTGTRGAIieitfeed 80
Cdd:pfam02463 1 YLKRIEIEGFKSYAKtVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIHSKSGAFV-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 81 gtkykvlrDFARNVSYLKRLDGREWRHVTETSmesVSSFIDRIIPYNVFLNAIYVRQGQIDAILESDETRDKIVKEILNL 160
Cdd:pfam02463 73 --------NSAEVEITFDNEDHELPIDKEEVS---IRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 161 DKLEKAYDNLGKIRKYIKYSIEEKEKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGI-------KEEV 233
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALeyyqlkeKLEL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 234 KTLEATFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKETEYRRLIEFKDEYLVKKN 313
Cdd:pfam02463 222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 314 ELEKRLGILSNRLQ------EVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMRLKAQMESLKSKLGGL 387
Cdd:pfam02463 302 LLKLERRKVDDEEKlkesekEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 388 EPEKINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKargkcpvcgRELTEEHKADLLRKYSLELSSI 467
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELE---------ILEEEEESIELKQGKLTEEKEE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 468 EKEIQEAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKINLEDLKRDKEEYELLKSESNKLKGEVESLKKE 547
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 548 VNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIRELEKFHNKYIEAKNAEKELRDILESLKDEREE 627
Cdd:pfam02463 533 DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAT 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 628 LDKAFEEL-AKIETDIEKVTSQLNELQRKFDQKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKER 706
Cdd:pfam02463 613 LEADEDDKrAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKE 692
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18202079 707 ESAKMELEKLNIAIKRIEELR---GKIKEYKALIKEEALNKIGEIASEIFSEFTDGKYSGIAIRAEDNKVK 774
Cdd:pfam02463 693 EILRRQLEIKKKEQREKEELKklkLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKE 763
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
587-705 |
2.13e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 587 IDELSGRIReLEkfhnkyIEAKNAE-KELRDILESLKDEREELDK-----AFEELAKIETDIEKVTSQLNELQRKFDQKK 660
Cdd:COG0542 395 IDEAAARVR-ME------IDSKPEElDELERRLEQLEIEKEALKKeqdeaSFERLAELRDELAELEEELEALKARWEAEK 467
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 18202079 661 yeEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKE 705
Cdd:COG0542 468 --ELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLRE 510
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
789-866 |
2.23e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.06 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGE--RIalglafRLAMSmylIGK----VdLLILDEPTPFLDEERRRKLIEIMeRHLRKI-SQVIIVSHDEELKDAAD 861
Cdd:PRK00349 490 LSGGEaqRI------RLATQ---IGSgltgV-LYVLDEPSIGLHQRDNDRLIETL-KHLRDLgNTLIVVEHDEDTIRAAD 558
|
....*
gi 18202079 862 HVIRI 866
Cdd:PRK00349 559 YIVDI 563
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
446-747 |
2.23e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 446 RELTEEHKADLLRKYSLELSSIEKEIQEAKALERQLRAEFRKVENELSRLS-SLKTIADQIIEIR-ERLSKINLEDLKRD 523
Cdd:PLN02939 40 RGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKStSSDDDHNRASMQRdEAIAAIDNEQQTNS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 524 KEEYELLKSESNKLKGEVESLKKEVNELNDYK----NESTKLEIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIR---- 595
Cdd:PLN02939 120 KDGEQLSDFQLEDLVGMIQNAEKNILLLNQARlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHveil 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 596 --ELEKFHNKYIEAKNAEKE------------------LRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRK 655
Cdd:PLN02939 200 eeQLEKLRNELLIRGATEGLcvhslskeldvlkeenmlLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 656 F----------DQKKYEEKREKMMKLSMEIKGLETKLEE----LERRRDeIKSTIEKLKEERKERESAKMELEKLNIAIK 721
Cdd:PLN02939 280 FivaqedvsklSPLQYDCWWEKVENLQDLLDRATNQVEKaalvLDQNQD-LRDKVDKLEASLKEANVSKFSSYKVELLQQ 358
|
330 340 350
....*....|....*....|....*....|....*....
gi 18202079 722 RI-----------EELRGKIKEYKALIKE--EALNKIGE 747
Cdd:PLN02939 359 KLklleerlqasdHEIHSYIQLYQESIKEfqDTLSKLKE 397
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
782-853 |
2.23e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 43.89 E-value: 2.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18202079 782 VERPLTFLSGGErialglAFRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHD 853
Cdd:cd03236 133 LDRNIDQLSGGE------LQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHD 198
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
611-741 |
2.39e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 611 EKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFdqkkyEEKREKMMKLSMEIKGLETKLEELERRRD 690
Cdd:COG2433 391 PEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEL-----EEKDERIERLERELSEARSEERREIRKDR 465
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 18202079 691 EIKSTIEKLKEERKERESAKmeleklniaiKRIEELRGKIKEYKALIKEEA 741
Cdd:COG2433 466 EISRLDREIERLERELEEER----------ERIEELKRKLERLKELWKLEH 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
218-422 |
2.41e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 218 NLPRLRRELEGIKEEVKTLEATFNSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKEL------PEL 291
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELqdrleaAED 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 292 EKKETEYRRLIEFKDEYLVKKNELEKRLgILSNRLQEVKRKIKDAESKVARIRwiEERLKEIQEKIMKLEPRVREFEDAM 371
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRE-NLEERIDALRARLNRAEEELERAM--RAFNREWPAETADLDADLESLPEYL 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18202079 372 RLKAQMESlkSKLGGLEpEKINEKLLYLENRKK-----ELEEEIDKITRKIGELNQ 422
Cdd:COG4913 819 ALLDRLEE--DGLPEYE-ERFKELLNENSIEFVadllsKLRRAIREIKERIDPLND 871
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
143-361 |
2.45e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.24 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 143 ILESDETRDKIVKEILNldklekayDNLGKIRKYIKYSIEEKEKFIMKTENIEDLIRTQEKsftEVLNEIRN-ISSNL-P 220
Cdd:smart00787 79 ISEGRDLFKEIEEETLI--------NNPPLFKEYFSASPDVKLLMDKQFQLVKTFARLEAK---KMWYEWRMkLLEGLkE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 221 RLRRELEGIKEEVKTLEATFNSITELKLRLGElngKKGRLEERIRQLESGIEEKRK-KSKELEEVVKELPELEKKETEYR 299
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNSIKPKLRD---RKDALEEELRQLKQLEDELEDcDPTELDRAKEKLKKLLQEIMIKV 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18202079 300 RLIEFKDEylvKKNELEKRLGILSNRLQEVKRKIKDAESKVARIRWIEER-LKEIQEKIMKLE 361
Cdd:smart00787 225 KKLEELEE---ELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKeIEKLKEQLKLLQ 284
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
272-692 |
2.47e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 44.67 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 272 EEKRKKSKELEEVVKELPELEKKETEYRRLIEfkdeylVKKNELEKRLGILSNRLQEVKRKIKDAESKVA------RIRW 345
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANLQ------KLDKEKEKLEADFLDECWKKIKRKKNSALSEAlngfkyEANF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 346 IEERLKEIQEKIMKLEPRVREFEDAMRLKAQMESLKSKLGGLEPEKINekLLYLEnRKKELEEEIDKITRKIGELnQRSK 425
Cdd:pfam13166 163 KSRLLREIEKDNFNAGVLLSDEDRKAALATVFSDNKPEIAPLTFNVID--FDALE-KAEILIQKVIGKSSAIEEL-IKNP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 426 DRRLAI---IELKKA-RGKCPVCGRELTEEHKADLLRKYSLElssiekeiqeakalerqlraefrkVENELSRLSSLKT- 500
Cdd:pfam13166 239 DLADWVeqgLELHKAhLDTCPFCGQPLPAERKAALEAHFDDE------------------------FTEFQNRLQKLIEk 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 501 IADQIIEIRERLSKINLEDLKR--DKEEYELLKSESNKLKGEVESLKKEVNElndyKNESTKLEIEIDKAKKELSEIEDR 578
Cdd:pfam13166 295 VESAISSLLAQLPAVSDLASLLsaFELDVEDIESEAEVLNSQLDGLRRALEA----KRKDPFKSIELDSVDAKIESINDL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 579 LlrlgfKTIDELSGRirelekfHNKYI-----EAKNAEKELRdiLESLKDEREELDKAFEELAKIETDIEKVTSQLNELQ 653
Cdd:pfam13166 371 V-----ASINELIAK-------HNEITdnfeeEKNKAKKKLR--LHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLE 436
|
410 420 430
....*....|....*....|....*....|....*....
gi 18202079 654 RKfdQKKYEEkrekmmklsmEIKGLETKLEELERRRDEI 692
Cdd:pfam13166 437 AE--IKKLRE----------EIKELEAQLRDHKPGADEI 463
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
783-866 |
2.47e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 43.32 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 783 ERPLTFLSGGERIALGLAfRLamsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSH-DEELKDAad 861
Cdd:PRK13539 122 HLPFGYLSAGQKRRVALA-RL-----LVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHiPLGLPGA-- 193
|
....*
gi 18202079 862 HVIRI 866
Cdd:PRK13539 194 RELDL 198
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
450-735 |
2.48e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 450 EEHKADLLRKYSLElSSIEKEIQEAKALERQlRAEFRKVENELSRLSSLKTIADQIIEIrERLSKINlEDLKRDKEEyel 529
Cdd:COG2433 366 DEVKARVIRGLSIE-EALEELIEKELPEEEP-EAEREKEHEERELTEEEEEIRRLEEQV-ERLEAEV-EELEAELEE--- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 530 LKSESNKLKGEVESLKKEVNELNDYKNESTKLEIEIDKAKKELSEIEdrllrlgfKTIDELSGRIRELEKFHNKYIEakn 609
Cdd:COG2433 439 KDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEER--------ERIEELKRKLERLKELWKLEHS--- 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 610 AEKELRDILESLKdeREELDKAFEELAKIETDI----------EKVTSQLNELQ-------RKFDQKKYEEKREKMMKLs 672
Cdd:COG2433 508 GELVPVKVVEKFT--KEAIRRLEEEYGLKEGDVvylrdasgagRSTAELLAEAGpravivpGELSEAADEVLFEEGIPV- 584
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18202079 673 meIKGLETKLEELER----RRDEIKSTIEKLKEERKERESAkmeleklniaiKRIEELRGKIKEYKA 735
Cdd:COG2433 585 --LPAEDVTIQEVDDlavvDEEELEAAIEDWEERAEERRRE-----------KKAEMLERLISEYRA 638
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
289-510 |
2.64e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 289 PELEKKETEYRRLIEfkdeylvKKNELEKRLGILSNRLQEVKRKIKDAESKVARIrwiEERLKEIQEKIMKLEPRVREFE 368
Cdd:COG3883 16 PQIQAKQKELSELQA-------ELEAAQAELDALQAELEELNEEYNELQAELEAL---QAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 369 DAM--RLKAQMESLKSK------LGGLEPEKINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGK 440
Cdd:COG3883 86 EELgeRARALYRSGGSVsyldvlLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 441 cpvcgrelTEEHKADLlrkyslelssiEKEIQEAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRE 510
Cdd:COG3883 166 --------LEAAKAEL-----------EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
391-718 |
2.80e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 391 KINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGKcpVCGRELTEEHK----ADLLRKyslELSS 466
Cdd:PRK04778 102 KAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRE--LRKSLLANRFSfgpaLDELEK---QLEN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 467 IEKEIQEAKALERQ---LRAefRKVENELSR-LSSLKTIADQIIEIRERLSKINLEDLKRDKEEYELLKSE-----SNKL 537
Cdd:PRK04778 177 LEEEFSQFVELTESgdyVEA--REILDQLEEeLAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEgyhldHLDI 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 538 KGEVESLKKEVNElndykNESTKLEIEIDKAKKELSEIEDRllrlgfktIDELSGrIRELEKFHNKYIEAKNAE-----K 612
Cdd:PRK04778 255 EKEIQDLKEQIDE-----NLALLEELDLDEAEEKNEEIQER--------IDQLYD-ILEREVKARKYVEKNSDTlpdflE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 613 ELRDILESLKDEREELDKAFE----ELAK---IETDIEKVTSQLNELQRKFDQKK--YEEKREKMMKLSMEIKGLETK-- 681
Cdd:PRK04778 321 HAKEQNKELKEEIDRVKQSYTlnesELESvrqLEKQLESLEKQYDEITERIAEQEiaYSELQEELEEILKQLEEIEKEqe 400
|
330 340 350
....*....|....*....|....*....|....*....
gi 18202079 682 --LEELERRRDEIKSTIEKLKEERKERESAKMELEKLNI 718
Cdd:PRK04778 401 klSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEKSNL 439
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
783-853 |
3.44e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.39 E-value: 3.44e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18202079 783 ERPLTFLSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLR-KISQVIIVSHD 853
Cdd:COG1245 450 DKNVKDLSGGELQ------RVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEnRGKTAMVVDHD 515
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
391-718 |
3.44e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.07 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 391 KINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKkargkcpvcgrELTEEHKADLLrKYSLELSSIEKE 470
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELK-----------DKYRELRKTLL-ANRFSYGPAIDE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 471 IQEakalerqlraEFRKVENELSRLSSLKTIADqIIEIRERLSKIN--LEDLKRDKEEY-ELLKSESNKLKGEVESLKKE 547
Cdd:pfam06160 151 LEK----------QLAEIEEEFSQFEELTESGD-YLEAREVLEKLEeeTDALEELMEDIpPLYEELKTELPDQLEELKEG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 548 VNEL--NDYKNESTKLEIEIDKAKKELSEIEDRLLRLGFKT----IDELSGRIRELEKFHNKYIEAKNAEKELRDILES- 620
Cdd:pfam06160 220 YREMeeEGYALEHLNVDKEIQQLEEQLEENLALLENLELDEaeeaLEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDy 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 621 ----------LKDEREELDKAF-------EELAKIETDIEKVTSQLNELQRKFDQKK---------YEEKREKMMKLSME 674
Cdd:pfam06160 300 lehaeeqnkeLKEELERVQQSYtlnenelERVRGLEKQLEELEKRYDEIVERLEEKEvayselqeeLEEILEQLEEIEEE 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 18202079 675 IKGLETKLEELerRRDEIKSTiEKLKEERKERESAKMELEKLNI 718
Cdd:pfam06160 380 QEEFKESLQSL--RKDELEAR-EKLDEFKLELREIKRLVEKSNL 420
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
782-853 |
3.59e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.00 E-value: 3.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18202079 782 VERPLTFLSGGErialgLAfRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHD 853
Cdd:COG1245 206 LDRDISELSGGE-----LQ-RVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHD 271
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
783-871 |
3.60e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.78 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 783 ERPLTFLSGGE--RIAL--GLAFrlamsmylIGKVdlLILDEPTPFLDEERRRKLIEIMERHLR-KISQVIIVSHDEELK 857
Cdd:PRK10247 132 TKNIAELSGGEkqRISLirNLQF--------MPKV--LLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDKDEI 201
|
90
....*....|....
gi 18202079 858 DAADHVIRIRLEGG 871
Cdd:PRK10247 202 NHADKVITLQPHAG 215
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
321-586 |
4.07e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 321 ILSNRLQEVKRKIKDAESKvarIRWIEERLKeIQEKIMKlEPRVREFEDAMRLKAQMESLKSklgglEPEKINEKLLYLE 400
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMK---IDHIQQQIK-TYNKNIE-EQRKKNGENIARKQNKYDELVE-----EAKTIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 401 NRKKELEEEIDKITRKIGELNQ-----RSKDRRLA-IIELKKARGKCPVCGRELTEEHKAdllrkyslelssIEKEIQEA 474
Cdd:PHA02562 241 DELLNLVMDIEDPSAALNKLNTaaakiKSKIEQFQkVIKMYEKGGVCPTCTQQISEGPDR------------ITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 475 KALERQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKINlEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDY 554
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNK-QSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDE 387
|
250 260 270
....*....|....*....|....*....|..
gi 18202079 555 KNESTKLEIEIDKAKKELSEIEDRLLRLGFKT 586
Cdd:PHA02562 388 LDKIVKTKSELVKEKYHRGIVTDLLKDSGIKA 419
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
165-359 |
4.10e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 165 KAYDNlgkirkyIKYSIEEKEKFIMKTENIEDLIRT--QEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKtleatfns 242
Cdd:COG2433 343 KAYDA-------YKNKFERVEKKVPPDVDRDEVKARviRGLSIEEALEELIEKELPEEEPEAEREKEHEERE-------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 243 ITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPELEKKETEYRRLIefkdeylvkkNELEKRLGIL 322
Cdd:COG2433 408 LTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREI----------SRLDREIERL 477
|
170 180 190
....*....|....*....|....*....|....*..
gi 18202079 323 SNRLQEVKRKIKDAESKVarirwieERLKEIQEKIMK 359
Cdd:COG2433 478 ERELEEERERIEELKRKL-------ERLKELWKLEHS 507
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
789-853 |
4.13e-04 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 42.94 E-value: 4.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18202079 789 LSGGERIALGLAFRLAMsmyligKVDLLILDEPTPFLDEERRRKLIEIMERhLRKISQVIIVSHD 853
Cdd:cd03260 142 LSGGQQQRLCLARALAN------EPEVLLLDEPTSALDPISTAKIEELIAE-LKKEYTIVIVTHN 199
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
789-864 |
4.16e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 43.08 E-value: 4.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18202079 789 LSGGERIALGLAFRLAMsmyligKVDLLILDEPTPFLDEERRRKLIEIMER-HLRKISQVIIVSHD-EELKDAADHVI 864
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAM------EPEVLVLDEPTAGLDPKGRKEMMEMFYKlHKEKGLTTVLVTHSmEDAARYADQIV 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
537-727 |
4.41e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 537 LKGEVESLKKEV----NELNDYK--NESTKLEIEIDKAKKELSEIEDRLLRLGFKtIDELSGRIRELEKFHNKYIEAKNA 610
Cdd:COG3206 180 LEEQLPELRKELeeaeAALEEFRqkNGLVDLSEEAKLLLQQLSELESQLAEARAE-LAEAEARLAALRAQLGSGPDALPE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 611 EKELrDILESLKDEREELDKAFEELAKIETD----IEKVTSQLNELQRKFDQkkyeEKREKMMKLSMEIKGLETKLEELE 686
Cdd:COG3206 259 LLQS-PVIQQLRAQLAELEAELAELSARYTPnhpdVIALRAQIAALRAQLQQ----EAQRILASLEAELEALQAREASLQ 333
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18202079 687 RRRDEIKSTIEKLKEERKERESAKMELE----KLNIAIKRIEELR 727
Cdd:COG3206 334 AQLAQLEARLAELPELEAELRRLEREVEvareLYESLLQRLEEAR 378
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
751-864 |
4.61e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 42.78 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 751 EIFSEFTDGKYSGIAIRAE-DNKVKLFVIYDgveRPLTFLSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEER 829
Cdd:cd03237 80 DLLSSITKDFYTHPYFKTEiAKPLQIEQILD---REVPELSGGELQ------RVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
90 100 110
....*....|....*....|....*....|....*..
gi 18202079 830 RRKLIEIMERH-LRKISQVIIVSHDEELKD-AADHVI 864
Cdd:cd03237 151 RLMASKVIRRFaENNEKTAFVVEHDIIMIDyLADRLI 187
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
196-554 |
4.67e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 196 DLIRTQEKSFTEVLNE---IRNISSNLPRLRRELEGIKEEVKT-LEATFNSITELKLRLGELNGKKGRLEERIRQLESGI 271
Cdd:pfam07888 45 ELLQAQEAANRQREKEkerYKRDREQWERQRRELESRVAELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 272 EEKRKKSKELEEVVKELPE-LEKKETEYRRLIEFKDEYLVKKNELEKRLGILSNRLQEVKRKIKDAESKVARIR-WIEER 349
Cdd:pfam07888 125 AAHEARIRELEEDIKTLTQrVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRnSLAQR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 350 LKEIQEKIMKLEPRVREFEDAMRLKAQMESLKSKLGGLEpEKINEKLLYLENRKKELEEEIDKITRKIGELNQR-----S 424
Cdd:pfam07888 205 DTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQ-ERLNASERKVEGLGEELSSMAAQRDRTQAELHQArlqaaQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 425 KDRRLAIIELKKARGKCPVCGRELTEEHKADLLRKYSLELSSiekEIQEAKALERQLRAEFRKVENELSrlsslktiadq 504
Cdd:pfam07888 284 LTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSA---ELQRLEERLQEERMEREKLEVELG----------- 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 18202079 505 iieiRERLSkiNLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDY 554
Cdd:pfam07888 350 ----REKDC--NRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEY 393
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
780-854 |
4.96e-04 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 43.50 E-value: 4.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18202079 780 DGVERPLT----FLSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISqVIIVSHDE 854
Cdd:TIGR02868 459 DGLDTVLGeggaRLSGGERQ------RLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRT-VVLITHHL 530
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
594-763 |
5.01e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.85 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 594 IRELEKFHNKYIEAKNAEKELRDIlESLKDEREELDKAFE----ELAKIETDIEKVTSQLNELQRKFDQKKYEEKRE--- 666
Cdd:NF033838 90 NKKLSDIKTEYLYELNVLKEKSEA-ELTSKTKKELDAAFEqfkkDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNypt 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 667 ---KMMKLSMEIKGLETKLEELERRRDEIKST--IEKLKEERKERESAKMELEKLNiaikrieelrgKIKEYKALIKEEA 741
Cdd:NF033838 169 ntyKTLELEIAESDVEVKKAELELVKEEAKEPrdEEKIKQAKAKVESKKAEATRLE-----------KIKTDREKAEEEA 237
|
170 180
....*....|....*....|..
gi 18202079 742 LNKIGEIASEIFSEFTDGKYSG 763
Cdd:NF033838 238 KRRADAKLKEAVEKNVATSEQD 259
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
446-669 |
5.05e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 446 RELTEEHKADLLRKYSLE--LSSIEKEIQEAKALERQLRAEFRKVENELsrLSSLKTIADQIIEIRERLSKINLEdLKRD 523
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQqqIKTYNKNIEEQRKKNGENIARKQNKYDEL--VEEAKTIKAEIEELTDELLNLVMD-IEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 524 KEEYELLKSESNKLKGEVESLKKEVN-------------ELNDYKNESTKLEIEIDKAKKELSEIEDRllrlgfktIDEL 590
Cdd:PHA02562 254 SAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTA--------IDEL 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18202079 591 SGRIRELEKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYEEKREKMM 669
Cdd:PHA02562 326 EEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYH 404
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
770-862 |
5.55e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 42.24 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 770 DNKVKLFVIYDGVERPLTFLSGGERIALGLaFRLAMSmyligKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVII 849
Cdd:PRK13540 109 TELCRLFSLEHLIDYPCGLLSSGQKRQVAL-LRLWMS-----KAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLL 182
|
90
....*....|...
gi 18202079 850 VSHDEELKDAADH 862
Cdd:PRK13540 183 TSHQDLPLNKADY 195
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
245-714 |
6.26e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 245 ELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPE-LEKKETEYRRLIEFKDEYLVKKNELEKRLGILS 323
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEkLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 324 NRLQEVKRKIKDAE----SKVARIRWIEERLKEIQEKIMKLEPRVREFEDAMR-LKAQMESLKSKLgglepEKINEKLLY 398
Cdd:pfam01576 468 SQLQDTQELLQEETrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLStLQAQLSDMKKKL-----EEDAGTLEA 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 399 LENRKKELEEEIDkitrkigELNQRSKDRRLAIIELKKARGKCpvcgRELTEEHKADLLRKYSLeLSSIEKEIQE----- 473
Cdd:pfam01576 543 LEEGKKRLQRELE-------ALTQQLEEKAAAYDKLEKTKNRL----QQELDDLLVDLDHQRQL-VSNLEKKQKKfdqml 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 474 -------AKALERQLRAEFRKVENElSRLSSLKTIADQIIEIRERLSKINledlkrdkeeyELLKSESNKLKGEVESLKK 546
Cdd:pfam01576 611 aeekaisARYAEERDRAEAEAREKE-TRALSLARALEEALEAKEELERTN-----------KQLRAEMEDLVSSKDDVGK 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 547 EVNELNDYKNestKLEIEIDKAKKELSEIEDRL-------LRLGFKTIDELSGRIRELEKFHNKYIEAKNA-EKELRDIL 618
Cdd:pfam01576 679 NVHELERSKR---ALEQQVEEMKTQLEELEDELqatedakLRLEVNMQALKAQFERDLQARDEQGEEKRRQlVKQVRELE 755
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 619 ESLKDEREELDKAFEELAKIETDIEKVTSQLNELQrkfdqKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEK 698
Cdd:pfam01576 756 AELEDERKQRAQAVAAKKKLELDLKELEAQIDAAN-----KGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKE 830
|
490
....*....|....*.
gi 18202079 699 LKEERKERESAKMELE 714
Cdd:pfam01576 831 SEKKLKNLEAELLQLQ 846
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
1-47 |
6.74e-04 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 42.85 E-value: 6.74e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 18202079 1 MKIERVIVQNFRSHKNSEIEFKPGINLIIGQNGAGKSSLLDAILVGL 47
Cdd:PRK14079 1 MRLLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIYLAL 47
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
797-870 |
6.83e-04 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 41.82 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 797 LGLAFRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHD-EELKDAADHVI-----RIRLEG 870
Cdd:cd03268 129 LGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLlSEIQKVADRIGiinkgKLIEEG 208
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
521-746 |
7.03e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.30 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 521 KRDKEEYELLKSESNKLKGEVESLKKEVNELNDYKNESTKLEIE--IDKAKKELS-EIEDRLLRLGFKtidelsgrirel 597
Cdd:PLN03229 418 KVNMKKREAVKTPVRELEGEVEKLKEQILKAKESSSKPSELALNemIEKLKKEIDlEYTEAVIAMGLQ------------ 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 598 EKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYEEKREKMMKLSMEIkg 677
Cdd:PLN03229 486 ERLENLREEFSKANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEI-- 563
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18202079 678 lETKLEELeRRRDEIKSTIEKLKEERKERESAKMelEKLNIAIK-RIEELRGKIK-EYKALIKEEALNKIG 746
Cdd:PLN03229 564 -NKKFKEV-MDRPEIKEKMEALKAEVASSGASSG--DELDDDLKeKVEKMKKEIElELAGVLKSMGLEVIG 630
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-537 |
7.08e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 162 KLEKAYDNLGKIRKYIKYSIEEKEKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEA-TF 240
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTdSS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 241 NSITELKlRLGELNGKKGRLEERI--------RQLESGIEEKRKKSKELEEVVKEL-PELEKKETEYRRLIEFK---DEY 308
Cdd:pfam10174 433 NTDTALT-TLEEALSEKERIIERLkeqreredRERLEELESLKKENKDLKEKVSALqPELTEKESSLIDLKEHAsslASS 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 309 LVKKNELEKRLGILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPRV-REFEDAMRLKAQMESLKSKLGGL 387
Cdd:pfam10174 512 GLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVaRYKEESGKAQAEVERLLGILREV 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 388 EPEKI--NEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGKCPV-CGRELTEEHKADLLRKYSLEL 464
Cdd:pfam10174 592 ENEKNdkDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLAdNSQQLQLEELMGALEKTRQEL 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 465 -------SSIEKEIQEAKALERQLRAEFRKVENELSRLSSLKTIAdqiiEIRERLSKINLEDL-----KRDKEEYELLKS 532
Cdd:pfam10174 672 datkarlSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLA----AISEKDANIALLELssskkKKTQEEVMALKR 747
|
....*
gi 18202079 533 ESNKL 537
Cdd:pfam10174 748 EKDRL 752
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
751-863 |
7.16e-04 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 42.11 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 751 EIFSEFTdGKYSGIAIRAEDNKVKLFVIYDGVERPLTFLSGGERialglaFRLAMSMYLIGKVDLLILDEPTPFLDEERR 830
Cdd:cd03263 97 RFYARLK-GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMK------RKLSLAIALIGGPSVLLLDEPTSGLDPASR 169
|
90 100 110
....*....|....*....|....*....|....
gi 18202079 831 RKLIEIMERhLRKISQVIIVSHDEELKDA-ADHV 863
Cdd:cd03263 170 RAIWDLILE-VRKGRSIILTTHSMDEAEAlCDRI 202
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
783-853 |
8.01e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.87 E-value: 8.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18202079 783 ERPLTFLSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLR-KISQVIIVSHD 853
Cdd:PRK13409 448 DKNVKDLSGGELQ------RVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEeREATALVVDHD 513
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
261-652 |
8.17e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 261 EERIRQLESGIEEKRKKSKELEEVVKELpeLEKKETEYRRLIEFKDEYLVKKNELEKRLGILSNRLQEVKRKIKDAESKV 340
Cdd:pfam06160 99 EEDIKQILEELDELLESEEKNREEVEEL--KDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEELTESGDYLE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 341 AR--IRWIEERLKEIQEKIMKLEPRVREFEDamRLKAQMESLKSKLGGLEPEKINEKLLYLENRKKELEEEIDKITRKIG 418
Cdd:pfam06160 177 ARevLEKLEEETDALEELMEDIPPLYEELKT--ELPDQLEELKEGYREMEEEGYALEHLNVDKEIQQLEEQLEENLALLE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 419 EL--------NQRSKDRRLAIIELkkargkcpvcgreLTEEHKAdllRKYSLE-LSSIEKEIQEAKALERQLRAEFRKV- 488
Cdd:pfam06160 255 NLeldeaeeaLEEIEERIDQLYDL-------------LEKEVDA---KKYVEKnLPEIEDYLEHAEEQNKELKEELERVq 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 489 ------ENELSRLSSLKTiadQIIEIRERLSKInLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDYKNEstkLE 562
Cdd:pfam06160 319 qsytlnENELERVRGLEK---QLEELEKRYDEI-VERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQS---LR 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 563 IEIDKAKKELSEIEDRLLRLgfktidelsgrIRELEKFH-----NKYIEA-KNAEKELRDILESLKDEREELDKAFEELA 636
Cdd:pfam06160 392 KDELEAREKLDEFKLELREI-----------KRLVEKSNlpglpESYLDYfFDVSDEIEDLADELNEVPLNMDEVNRLLD 460
|
410
....*....|....*.
gi 18202079 637 KIETDIEKVTSQLNEL 652
Cdd:pfam06160 461 EAQDDVDTLYEKTEEL 476
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
441-550 |
8.20e-04 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 42.44 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 441 CPVCGRELTEEHKADLLRKySLELSSIEKEIQEAKALERQLRAEFRKVENELSRLSSLKT----IADQIIEIRERLSKIN 516
Cdd:pfam10186 13 CPTCARNRLYELRVDLARL-LSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKLRLLKSevaiSNERLNEIKDKLDQLR 91
|
90 100 110
....*....|....*....|....*....|....
gi 18202079 517 lEDLKRDKEEYELLKSESNKLKGEVESLKKEVNE 550
Cdd:pfam10186 92 -REIAEKKKKIEKLRSSLKQRRSDLESASYQLEE 124
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
784-852 |
8.26e-04 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 41.58 E-value: 8.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18202079 784 RPLTFLSGGERIALGLAfRLamsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSH 852
Cdd:TIGR01189 123 LPAAQLSAGQQRRLALA-RL-----WLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
325-684 |
8.80e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.82 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 325 RLQEVKRKIKDAESKVARIRWiEERLKEIQEKIMKLEPRVREFEDAmrlKAQMESLKSKLGGLEPEKINEKLLYLENRKK 404
Cdd:pfam09731 60 KPKTFRPLQPSVVSAVTGESK-EPKEEKKQVKIPRQSGVSSEVAEE---EKEATKDAAEAKAQLPKSEQEKEKALEEVLK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 405 ELEEEIDKITRKIGEL--------NQRSKDRRLAIIELKKARGKCPVCGRELTEEHKADLLRKYSLELSSIEK----EIQ 472
Cdd:pfam09731 136 EAISKAESATAVAKEAkddaiqavKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEaappLLD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 473 EAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKINLEDLKR-----DKEEYELLKSESNKLKGEVESLKKE 547
Cdd:pfam09731 216 AAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSifpdiIPVLKEDNLLSNDDLNSLIAHAHRE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 548 VNELNDY-----KNESTKLEIEIDKAKKELSEIEDRLLRlgfKTIDELSGRIRELEKfhnkyiEAKNAEKELRdileslK 622
Cdd:pfam09731 296 IDQLSKKlaelkKREEKHIERALEKQKEELDKLAEELSA---RLEEVRAADEAQLRL------EFEREREEIR------E 360
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18202079 623 DEREELDKAFEELAKIETDI--EKVTSQLNELQRKFDQ---KKYEEKR----EKMMKLSMEIKGLETKLEE 684
Cdd:pfam09731 361 SYEEKLRTELERQAEAHEEHlkDVLVEQEIELQREFLQdikEKVEEERagrlLKLNELLANLKGLEKATSS 431
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
25-269 |
9.26e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.38 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 25 INLIIGQNGAGKSSLLDAILVglywskrmrLRGLKKDEFTRTGTRGAIIEITFEEDGTKYKVLRDFARNVSYLKRLDGRE 104
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRF---------LADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 105 WRhvtetsmesvssfidriIPYNVFLNAIYVRQGQIDAILESDETRDKIVkEILNLDKLEKAYDNLGKIRKYIKYSIEEK 184
Cdd:pfam13304 72 YR-----------------YGLDLEREDVEEKLSSKPTLLEKRLLLREDS-EEREPKFPPEAEELRLGLDVEERIELSLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 185 EKFIMKTENIEDLIRTQEKSFTEVLNEIRNISSNLPRLRRELEGIKEEVKTLEATFNSITELKLRLGELNGKKGRLEERI 264
Cdd:pfam13304 134 ELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVD 213
|
....*
gi 18202079 265 RQLES 269
Cdd:pfam13304 214 DRLRE 218
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
588-749 |
1.06e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 42.74 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 588 DELSGRIRELEKFHNKYIEAKNAEKELrdiLESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYEEKREK 667
Cdd:pfam13166 279 DEFTEFQNRLQKLIEKVESAISSLLAQ---LPAVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEAKRKDPFKSI 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 668 MMK----LSMEIKGLETKLEELERRRDEIKSTIEKLKE------ERKERESAKMELEKLNIAIKRIEELRGKIKEYKALI 737
Cdd:pfam13166 356 ELDsvdaKIESINDLVASINELIAKHNEITDNFEEEKNkakkklRLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNL 435
|
170
....*....|..
gi 18202079 738 KEEALNKIGEIA 749
Cdd:pfam13166 436 EAEIKKLREEIK 447
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
767-867 |
1.07e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 42.03 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 767 RAEDnKVKLFVIYDGVERPLTFLSGGERIALGLAFRLAMsmyligKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQ 846
Cdd:PRK13647 118 RVEE-ALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM------DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKT 190
|
90 100
....*....|....*....|..
gi 18202079 847 VIIVSHDEELK-DAADHVIRIR 867
Cdd:PRK13647 191 VIVATHDVDLAaEWADQVIVLK 212
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
137-551 |
1.14e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 137 QGQIDAILESDETRDKIVKEILNLDKLEKAYDNLgkirkyIKYSIEEKEKfimKTENIEDLIRTQEKSFTEVLNEIRNIS 216
Cdd:pfam05557 54 QKRIRLLEKREAEAEEALREQAELNRLKKKYLEA------LNKKLNEKES---QLADAREVISCLKNELSELRRQIQRAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 217 SNLPRLRRELEGIKEEVKTLEATFNSITELKLRL-------GELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELP 289
Cdd:pfam05557 125 LELQSTNSELEELQERLDLLKAKASEAEQLRQNLekqqsslAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 290 ELEKKETEYRRLIEFKDEYLV---KKNELEKRLGilsnRLQEVKRKIKDAESKVARIrwiEERLKEIQEKIMKLEPRVRE 366
Cdd:pfam05557 205 ELERLREHNKHLNENIENKLLlkeEVEDLKRKLE----REEKYREEAATLELEKEKL---EQELQSWVKLAQDTGLNLRS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 367 FEDamrLKAQMESLKSKLGGLEPEK--INEKLLYLENRKKELEEEIDKITRKIGELNQRSKD-----RRLA--IIELKKA 437
Cdd:pfam05557 278 PED---LSRRIEQLQQREIVLKEENssLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRhkalvRRLQrrVLLLTKE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 438 RGKCpvcgRELTEEHKADL-LRKYSLELS----SIEKEIQEAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRERl 512
Cdd:pfam05557 355 RDGY----RAILESYDKELtMSNYSPQLLerieEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQ- 429
|
410 420 430
....*....|....*....|....*....|....*....
gi 18202079 513 sKINLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNEL 551
Cdd:pfam05557 430 -QESLADPSYSKEEVDSLRRKLETLELERQRLREQKNEL 467
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
779-864 |
1.16e-03 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. 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: 213231 [Multi-domain] Cd Length: 211 Bit Score: 41.41 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 779 YDGVERPLTFLSGGERIALGLAfrlamsMYLIGKVDLLILDEPTPFLD-EERRRklieiMERHLRKISQ---VIIVSHD- 853
Cdd:cd03264 121 GDRAKKKIGSLSGGMRRRVGIA------QALVGDPSILIVDEPTAGLDpEERIR-----FRNLLSELGEdriVILSTHIv 189
|
90
....*....|.
gi 18202079 854 EELKDAADHVI 864
Cdd:cd03264 190 EDVESLCNQVA 200
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
789-873 |
1.18e-03 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). 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.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 41.27 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGERIALglafrlAMSMYLIGKVDLLILDEPT----PfldeerrrKLIEIMERHLRKISQ----VIIVSHD-EELKDA 859
Cdd:cd03224 133 LSGGEQQML------AIARALMSRPKLLLLDEPSeglaP--------KIVEEIFEAIRELRDegvtILLVEQNaRFALEI 198
|
90
....*....|....*....
gi 18202079 860 ADHVI-----RIRLEGGAS 873
Cdd:cd03224 199 ADRAYvlergRVVLEGTAA 217
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
627-740 |
1.24e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 627 ELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYEEKREkmmkLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKER 706
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAE----LRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|....
gi 18202079 707 ESAKMELEKLNiaiKRIEELRGKIKEYKALIKEE 740
Cdd:COG0542 481 EQRYGKIPELE---KELAELEEELAELAPLLREE 511
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
266-636 |
1.28e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 266 QLESGIEEKRKKSKELEEVVKELPELEKK----ETEYRRLIEFKDEYLVKKNELEKRLGILSNRLQEVKRKIKDAESKVA 341
Cdd:PLN02939 115 QQTNSKDGEQLSDFQLEDLVGMIQNAEKNilllNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 342 RIRWIEERLKEIQEKIMKLEPRVREFEDAMrlkaqmeslksklgGLEPEKINEKLLYLENRKKELEEEIDKITRkigeln 421
Cdd:PLN02939 195 HVEILEEQLEKLRNELLIRGATEGLCVHSL--------------SKELDVLKEENMLLKDDIQFLKAELIEVAE------ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 422 qrskdrrlaiielkkargkcpvcgrelTEEHKADLLRKYSLELSSIekeiqeakaleRQLRAEFRKVENELSRLSSLKTi 501
Cdd:PLN02939 255 ---------------------------TEERVFKLEKERSLLDASL-----------RELESKFIVAQEDVSKLSPLQY- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 502 aDQIIEIRERLSKInLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNELNDYKNESTKLEIeidkAKKELSEIEDRLLR 581
Cdd:PLN02939 296 -DCWWEKVENLQDL-LDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVEL----LQQKLKLLEERLQA 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 18202079 582 LGFKTidelsgrirelekfhNKYIEA-KNAEKELRDILESLKDEREEldKAFEELA 636
Cdd:PLN02939 370 SDHEI---------------HSYIQLyQESIKEFQDTLSKLKEESKK--RSLEHPA 408
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
787-867 |
1.46e-03 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 42.40 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 787 TFLSGGERIalglafRLAMSMYLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKisqVIIVSHDEELKDAADHVIRI 866
Cdd:TIGR00958 616 SQLSGGQKQ------RIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRT---VLLIAHRLSTVERADQILVL 686
|
.
gi 18202079 867 R 867
Cdd:TIGR00958 687 K 687
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
148-752 |
1.49e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 148 ETRDKIVKEILNLDKLE---KAYDNLGKIRKY----IKYSIEEKEKFIM--------KTENIEDLIRTQEKSFTEVLNEI 212
Cdd:PTZ00440 1039 EIEEKVDQYISLLEKMKtklSSFHFNIDIKKYknpkIKEEIKLLEEKVEallkkideNKNKLIEIKNKSHEHVVNADKEK 1118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 213 RNISSNLPRLRRELEGIKEEVKTLEATFNSITELKLRLGELNGKKGRLEE-RIRQLESGIEEKRKKSK----ELEEVVKE 287
Cdd:PTZ00440 1119 NKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEVNEIEIEYERiLIDHIVEQINNEAKKSKtimeEIESYKKD 1198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 288 LPELEKKETEYRRLIEFKDEYlvkkNELEKRLGILSNRLQEVKRKIKDAESKVARIRWIEErLKEIQEKIMK-LEPRVRE 366
Cdd:PTZ00440 1199 IDQVKKNMSKERNDHLTTFEY----NAYYDKATASYENIEELTTEAKGLKGEANRSTNVDE-LKEIKLQVFSyLQQVIKE 1273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 367 FEDAMRLKAQMESLKSKLGGLEPEKINEKLLYLENRKKELEEEIDKITRKIGELNQRskdrrlaiIELKKargkcpvcgr 446
Cdd:PTZ00440 1274 NNKMENALHEIKNMYEFLISIDSEKILKEILNSTKKAEEFSNDAKKELEKTDNLIKQ--------VEAKI---------- 1335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 447 ELTEEHKADLLRkySLELSSIEKEIQEAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRER-LSKINLEDLKRDKE 525
Cdd:PTZ00440 1336 EQAKEHKNKIYG--SLEDKQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNASRgKDKIDFLNKHEAIE 1413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 526 EYELLKSESNKLKGEVESLKKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLGFKT-----IDELSGRIRELEKF 600
Cdd:PTZ00440 1414 PSNSKEVNIIKITDNINKCKQYSNEAMETENKADENNDSIIKYEKEITNILNNSSILGKKTklekkKKEATNIMDDINGE 1493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 601 H-NKYIEAKNAEKELRDILE--SLKDEREELDKAFEELAK--IETDIEKVTSQLNELQRKfdQKKYEEKREKMMKLSMEI 675
Cdd:PTZ00440 1494 HsIIKTKLTKSSEKLNQLNEqpNIKREGDVLNNDKSTIAYetIQYNLGRVKHNLLNILNI--KDEIETILNKAQDLMRDI 1571
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18202079 676 KGLETKLEE--LERRRDEIKSTIEKLKEERKERESAKMELEKLNIAIKRIEELRGKIKEYKALIKEEALNKIGEIASEI 752
Cdd:PTZ00440 1572 SKISKIVENknLENLNDKEADYVKYLDNILKEKQLMEAEYKKLNEIYSDVDNIEKELKKHKKNYEIGLLEKVIEINKNI 1650
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
812-867 |
1.50e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 1.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 18202079 812 KVDLLILDEPTPFLDEERRRKLIEIMeRHLRK--ISQVIIvSHD-EELKDAADHVIRIR 867
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLL-LELKAqgITSIII-SHKlNEIRRVADSITVLR 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
789-852 |
1.62e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 42.12 E-value: 1.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18202079 789 LSGGERIALGLAfRLamsmyLIGKVDLLILDEPTPFLDEERRRkliEIMERhLRKISQ---VIIVSH 852
Cdd:PRK11160 476 LSGGEQRRLGIA-RA-----LLHDAPLLLLDEPTEGLDAETER---QILEL-LAEHAQnktVLMITH 532
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
211-544 |
1.69e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 211 EIRNISSNLPRLRRELEGIKEEVKTLEATFNSITE-LKLRLGELngkkgRLEERIRQLESGIEEKRKKSKELEEVVKELP 289
Cdd:PRK04863 301 QLAAEQYRLVEMARELAELNEAESDLEQDYQAASDhLNLVQTAL-----RQQEKIERYQADLEELEERLEEQNEVVEEAD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 290 ElEKKETEyRRLIEFKDEYLVKKNEL---EKRLGILSNR----------LQEVKRKIKDAESKVARIR-WIEE---RLKE 352
Cdd:PRK04863 376 E-QQEENE-ARAEAAEEEVDELKSQLadyQQALDVQQTRaiqyqqavqaLERAKQLCGLPDLTADNAEdWLEEfqaKEQE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 353 IQEKIMKLEPRVREFEDAMRLKAQ-MESLKSKLGGLEPE----KINEKLLYLENrKKELEEEIDKITRKIGELNQRSKDR 427
Cdd:PRK04863 454 ATEELLSLEQKLSVAQAAHSQFEQaYQLVRKIAGEVSRSeawdVARELLRRLRE-QRHLAEQLQQLRMRLSELEQRLRQQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 428 RLAIIELKKArgkcpvCGRELTEEHKADLLRKYSLELSSIEKEIQEAKALERQLRAEFRKVENEL-SRLSSLKTIADQII 506
Cdd:PRK04863 533 QRAERLLAEF------CKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLqARIQRLAARAPAWL 606
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 18202079 507 EIRERLSKIN--------------------LEDLKRDKEEYELLKSESNKLKGEVESL 544
Cdd:PRK04863 607 AAQDALARLReqsgeefedsqdvteymqqlLERERELTVERDELAARKQALDEEIERL 664
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
789-870 |
1.73e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 41.13 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGERIALGLAFRLAMSmyligkVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEELKDAADHVI---- 864
Cdd:PRK13644 137 LSGGQGQCVALAGILTME------PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIvmdr 210
|
....*..
gi 18202079 865 -RIRLEG 870
Cdd:PRK13644 211 gKIVLEG 217
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
516-650 |
1.75e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 41.64 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 516 NLEDLKRDKEEYELLKSESNKLKGEVESLKKEVNE----LNDYKNESTKLEIEIDKAKKELSEIEDrllrlgfktidels 591
Cdd:TIGR04320 238 IADGNKFDKTPIPNPPNSLAALQAKLATAQADLAAaqtaLNTAQAALTSAQTAYAAAQAALATAQK-------------- 303
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 18202079 592 grirELEKFHNKyiEAKNAEKELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLN 650
Cdd:TIGR04320 304 ----ELANAQAQ--ALQTAQNNLATAQAALANAEARLAKAKEALANLNADLAKKQAALD 356
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-44 |
1.86e-03 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 40.53 E-value: 1.86e-03
10 20 30
....*....|....*....|....*....|.
gi 18202079 15 KNSEIEFKPG-INLIIGQNGAGKSSLLDAIL 44
Cdd:cd03250 22 KDINLEVPKGeLVAIVGPVGSGKSSLLSALL 52
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
782-856 |
1.95e-03 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 41.37 E-value: 1.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18202079 782 VERPLTFLSGGERIALGLAFRLAMSmyligkVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEEL 856
Cdd:PRK09536 133 ADRPVTSLSGGERQRVLLARALAQA------TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDL 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
781-868 |
2.04e-03 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 40.55 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 781 GVE-RPLTFLSGGERIALGLAfRLamsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHdEELKDA 859
Cdd:cd03231 117 GFEdRPVAQLSAGQQRRVALA-RL-----LLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH-QDLGLS 189
|
....*....
gi 18202079 860 ADHVIRIRL 868
Cdd:cd03231 190 EAGARELDL 198
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-47 |
2.18e-03 |
|
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: 39.65 E-value: 2.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 18202079 5 RVIVQNFRSHK-NSEIEF-KPGINLIIGQNGAGKSSLLDAILVGL 47
Cdd:cd03227 1 KIVLGRFPSYFvPNDVTFgEGSLTIITGPNGSGKSTILDAIGLAL 45
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
241-528 |
2.47e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 241 NSITELKLRLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKELPE-LEKKETEYRRLIEFKDEYLVKKNELEKRL 319
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAqVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 320 GILSNRLQEVKRKIKDAESKVARIRWIEERLKEIQEKIMKLEPR----VREFEDAMRLKAQMESLKSKLGGLEPE-KINE 394
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRqqteVLSPEEEKELVEKIKELEKELEKAKKAlEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 395 KLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKargkcpvcgrelteehKADLLRKyslELSSIEKEIQEA 474
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYK----------------EADELRK---EADELHKEIVEA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 18202079 475 KALERQLRAEFRKVENELSRLSslKTIADQIIEIRERLSKINLEDLKRDKEEYE 528
Cdd:COG1340 222 QEKADELHEEIIELQKELRELR--KELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| PrfA |
COG0216 |
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein ... |
614-731 |
2.49e-03 |
|
Protein chain release factor RF1 [Translation, ribosomal structure and biogenesis]; Protein chain release factor RF1 is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 439986 [Multi-domain] Cd Length: 356 Bit Score: 41.14 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 614 LRDILESLKDEREELDkafEELAKIEtdiekVTSqlnelqrkfDQKKYeekrekmMKLSMEIKGLE---TKLEELERRRD 690
Cdd:COG0216 2 MLDKLEALEERYEELE---ALLSDPE-----VIS---------DQKRF-------RKLSKEYAELEpivEAYREYKKLLE 57
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 18202079 691 EIKSTIEKLKEERKE--RESAKMELEKLNiaiKRIEELRGKIK 731
Cdd:COG0216 58 DIEEAKELLEEESDPemREMAKEELEELE---ARLEELEEELK 97
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
432-760 |
2.67e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 432 IELKKARGKCPVCGRElteeHKADLLRKYSLELSSIEKEIQEAKALERQLRAEFRK-VENELSRLSSLKTIADQIIEIRE 510
Cdd:pfam15921 59 VELDSPRKIIAYPGKE----HIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQsVIDLQTKLQEMQMERDAMADIRR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 511 RLSKiNLEDLKrdkeeyellksesNKLKGEVESLKKEVNELNDYKNESTKleiEIDKAKKELSEIEDRLlrlgfktiDEL 590
Cdd:pfam15921 135 RESQ-SQEDLR-------------NQLQNTVHELEAAKCLKEDMLEDSNT---QIEQLRKMMLSHEGVL--------QEI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 591 SGRIRELEKFHNKYIEAKNAEKEL--RDILESLKDEREELDKafeELAKIETDIEKVTSQLNELQRKFDQK------KYE 662
Cdd:pfam15921 190 RSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELDT---EISYLKGRIFPVEDQLEALKSESQNKielllqQHQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 663 EKREKMM-KLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESakMELEKLNIAIKRIEELRGKIKEYKALIKEea 741
Cdd:pfam15921 267 DRIEQLIsEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNS--MYMRQLSDLESTVSQLRSELREAKRMYED-- 342
|
330 340
....*....|....*....|..
gi 18202079 742 lnKIGEIASEIF---SEFTDGK 760
Cdd:pfam15921 343 --KIEELEKQLVlanSELTEAR 362
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
809-867 |
2.68e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.17 E-value: 2.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18202079 809 LIGKVDLLILDEPTPFLDEERRRKLIEIMeRHLRK--ISqVIIVSHD-EELKDAADHVIRIR 867
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEIL-RRLAAegKS-IIFITHKlREVMAIADRVTVLR 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
789-864 |
2.80e-03 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 40.11 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 789 LSGGERIALGLAfrlamsMYLIGKVDLLILDEPTPFLDEERRRKLIEImerhLRKISQ----VIIVSHDEEL-KDAADHV 863
Cdd:cd03219 144 LSYGQQRRLEIA------RALATDPKLLLLDEPAAGLNPEETEELAEL----IRELRErgitVLLVEHDMDVvMSLADRV 213
|
.
gi 18202079 864 I 864
Cdd:cd03219 214 T 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-106 |
3.18e-03 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 39.15 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 15 KNSEIEFKPG-INLIIGQNGAGKSSLLDAILvGLYWSkrmrlrglkkdeftrtgTRGaiiEITFEEDGTKYKVLRDFARN 93
Cdd:cd00267 16 DNVSLTLKAGeIVALVGPNGSGKSTLLRAIA-GLLKP-----------------TSG---EILIDGKDIAKLPLEELRRR 74
|
90
....*....|...
gi 18202079 94 VSYLKRLDGREWR 106
Cdd:cd00267 75 IGYVPQLSGGQRQ 87
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
390-670 |
3.22e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 390 EKINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKARGKCPVCGRELTEEHKA---------DLLRKY 460
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDElneklnelrEELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 461 SLELSSIEKEIQEAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKinLEDLKRDKEEYELLKSESNKLKGE 540
Cdd:COG1340 98 RKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEK--AKKALEKNEKLKELRAELKELRKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 541 VESLKKEVNELNDyknestkleiEIDKAKKELSEIedrllrlgFKTIDELSGRIRELekfHNKYIEAKnaekelrdilES 620
Cdd:COG1340 176 AEEIHKKIKELAE----------EAQELHEEMIEL--------YKEADELRKEADEL---HKEIVEAQ----------EK 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 18202079 621 LKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYEEKREKMMK 670
Cdd:COG1340 225 ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
18-47 |
3.43e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 40.13 E-value: 3.43e-03
10 20 30
....*....|....*....|....*....|
gi 18202079 18 EIEFKPGINLIIGQNGAGKSSLLDAILVGL 47
Cdd:COG3910 32 GLEFHPPVTFFVGENGSGKSTLLEAIAVAA 61
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
641-743 |
3.50e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 40.82 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 641 DIEKVTSQLNELQRKFDQKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEKLNIAI 720
Cdd:PRK05431 3 DIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEI 82
|
90 100
....*....|....*....|...
gi 18202079 721 KRIEElrgKIKEYKALIKEEALN 743
Cdd:PRK05431 83 KALEA---ELDELEAELEELLLR 102
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
221-714 |
3.66e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 221 RLRRELEGIKEEVKTLEATFNS-ITELKLRLGELNGKKGRLEERIRQLESGIEEK-------RKKSKELEEVVKELPELE 292
Cdd:pfam01576 201 KGRQELEKAKRKLEGESTDLQEqIAELQAQIAELRAQLAKKEEELQAALARLEEEtaqknnaLKKIRELEAQISELQEDL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 293 KKETEYRRLIE-----FKDEYLVKKNELEKRLG-------ILSNRLQEVK--RKIKDAESKVARIRWIEERLKEIQEkim 358
Cdd:pfam01576 281 ESERAARNKAEkqrrdLGEELEALKTELEDTLDttaaqqeLRSKREQEVTelKKALEEETRSHEAQLQEMRQKHTQA--- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 359 kLEPRVREFEDAMRLKAQMESLKSKLGGlEPEKINEKLLYLENRKKELEEEIDKITRKIGELNQRSKDRRLAIIELKKAR 438
Cdd:pfam01576 358 -LEELTEQLEQAKRNKANLEKAKQALES-ENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 439 GKCP-----VCGRELTEEHKADLLRKyslELSSIEKEIQEAKALerqLRAEFRKVENELSRL-------SSLKTIADQII 506
Cdd:pfam01576 436 SKLQselesVSSLLNEAEGKNIKLSK---DVSSLESQLQDTQEL---LQEETRQKLNLSTRLrqlederNSLQEQLEEEE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 507 EIRERLSK------INLEDLKRDKEEY----ELLKSESNKLKGEVESLKKEVNELNDYKNEstkleieIDKAKKEL-SEI 575
Cdd:pfam01576 510 EAKRNVERqlstlqAQLSDMKKKLEEDagtlEALEEGKKRLQRELEALTQQLEEKAAAYDK-------LEKTKNRLqQEL 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 576 EDRLLRLgfktiDELSGRIRELEKFHNKYIEAKNAEKelrDILESLKDEReelDKAFEELAKIETdieKVTSQLNELQRK 655
Cdd:pfam01576 583 DDLLVDL-----DHQRQLVSNLEKKQKKFDQMLAEEK---AISARYAEER---DRAEAEAREKET---RALSLARALEEA 648
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18202079 656 FDQKKYEEKREKMMKLSME------------IKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELE 714
Cdd:pfam01576 649 LEAKEELERTNKQLRAEMEdlvsskddvgknVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLE 719
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
539-741 |
3.90e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 539 GEVESLKKEVNEL-NDYKnestKLEIEIDKAKKELSEIEDR--LLRLGFKTIDELSGRIRELEKFHNKYIEAKNAEK--- 612
Cdd:COG0497 151 AGLEELLEEYREAyRAWR----ALKKELEELRADEAERAREldLLRFQLEELEAAALQPGEEEELEEERRRLSNAEKlre 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 613 ---------------------ELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDqkkYEEKRekmmkl 671
Cdd:COG0497 227 alqealealsggeggaldllgQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLE---FDPER------ 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18202079 672 smeikgletkLEELERRRDEIKS-------TIEKLKEERkerESAKMELEKLNIAIKRIEELRGKIKEYKALIKEEA 741
Cdd:COG0497 298 ----------LEEVEERLALLRRlarkygvTVEELLAYA---EELRAELAELENSDERLEELEAELAEAEAELLEAA 361
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
587-766 |
4.14e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.68 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 587 IDELSGRIRELEKFHnkyIEAKNAEKELrdilESLKDEREELDKAFEELAKIETDIEKvtsqlnelqrkfdQKKYEEKRE 666
Cdd:PRK05771 18 KDEVLEALHELGVVH---IEDLKEELSN----ERLRKLRSLLTKLSEALDKLRSYLPK-------------LNPLREEKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 667 KMMKLSME--IKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEKL-NIAIKRIEELRGK-IKEYKALIKEEAL 742
Cdd:PRK05771 78 KVSVKSLEelIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWgNFDLDLSLLLGFKyVSVFVGTVPEDKL 157
|
170 180
....*....|....*....|....
gi 18202079 743 NKIGEIASEIFSEFTDGKYSGIAI 766
Cdd:PRK05771 158 EELKLESDVENVEYISTDKGYVYV 181
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
447-739 |
4.29e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.97 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 447 ELTEEHKADLLRKYSLELSSIEKEIQEAKALERQLRAEFRKvENELSRLS--SLKTIADQIIEIrERLSKINLEDLKRDK 524
Cdd:PTZ00440 298 NFIQEEIGDIIKRYNFHLKKIEKGKEYIKRIQNNNIPPQVK-KDELKKKYfeSAKHYASFKFSL-EMLSMLDSLLIKKEK 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 525 EEYELLKSESNKLKGEVESLKKEVNELNDYKNESTKLEIEIDKAKKELSE----IEDRLLRLGFKTID---ELSGRIREL 597
Cdd:PTZ00440 376 ILNNLFNKLFGDLKEKIETLLDSEYFISKYTNIISLSEHTLKAAEDVLKEnsqkIADYALYSNLEIIEikkKYDEKINEL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 598 EKFHNKYIEAKNAEKELRDILESLKDEREELDkafEELAKIETDIEKVTSQLNELQR-KFDQKKYEEKREKMMKLSMEIK 676
Cdd:PTZ00440 456 KKSINQLKTLISIMKSFYDLIISEKDSMDSKE---KKESSDSNYQEKVDELLQIINSiKEKNNIVNNNFKNIEDYYITIE 532
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18202079 677 GLETKLEELERRRDEIKSTIEKLKEERKERESAKMELEKlniAIKRIEELRGKIKEYKALIKE 739
Cdd:PTZ00440 533 GLKNEIEGLIELIKYYLQSIETLIKDEKLKRSMKNDIKN---KIKYIEENVDHIKDIISLNDE 592
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-58 |
4.34e-03 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 39.59 E-value: 4.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 18202079 3 IERVIVQNFRSHKNSEI--EFKPGINLIIGQNGAGKSSLLDAIL-VGLYWSKRMRLRGL 58
Cdd:cd03274 3 ITKLVLENFKSYAGEQVigPFHKSFSAIVGPNGSGKSNVIDSMLfVFGFRASKMRQKKL 61
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
574-685 |
4.84e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 40.10 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 574 EIEDRLLRLGFKTIDelsgRIRELEKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEELakiETDIEKVTSQLNELQ 653
Cdd:COG4026 111 EIKNAIIRAGLKSLQ----NIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEEL---REEYKKLREENSILE 183
|
90 100 110
....*....|....*....|....*....|....
gi 18202079 654 RKFDQKKYEEKREKMMKLSMEIKGLET--KLEEL 685
Cdd:COG4026 184 EEFDNIKSEYSDLKSRFEELLKKRLLEvfSLEEL 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
785-858 |
5.14e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.32 E-value: 5.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18202079 785 PLTFLSGGERIALGLAfRLamsmyLIGKVDLLILDEPTPFLDEERRRKLIEIMERHLrkiSQVIIVSHDEELKD 858
Cdd:PRK11147 437 PVKALSGGERNRLLLA-RL-----FLKPSNLLILDEPTNDLDVETLELLEELLDSYQ---GTVLLVSHDRQFVD 501
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
463-740 |
5.39e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.61 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 463 ELSSIEKEIQEAKAL-----ERQLRAEFRKVENELSRLSSLKTIA----DQIIEIRERLSKINLEDLKRD---KEEYELL 530
Cdd:PLN03229 437 EVEKLKEQILKAKESsskpsELALNEMIEKLKKEIDLEYTEAVIAmglqERLENLREEFSKANSQDQLMHpvlMEKIEKL 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 531 KSESNK---LKGEVESLKKEVNELNDY---------KNESTKLEIEIDKAKKELSE----------IEDRLLRLGFKTID 588
Cdd:PLN03229 517 KDEFNKrlsRAPNYLSLKYKLDMLNEFsrakalsekKSKAEKLKAEINKKFKEVMDrpeikekmeaLKAEVASSGASSGD 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 589 ELSGRIRELEKFHNKYIEAknaekELRDILESLKDEREELDKAFEELAKIETDiekvtsqlNELQRKFDqkKYEEKREKM 668
Cdd:PLN03229 597 ELDDDLKEKVEKMKKEIEL-----ELAGVLKSMGLEVIGVTKKNKDTAEQTPP--------PNLQEKIE--SLNEEINKK 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 669 MKLSMEIKGLETKLEELE--------RRRDEIKSTIEKLKEERKERESAKMELEKLNiaiKRIEELRGKIKEYKALIKEE 740
Cdd:PLN03229 662 IERVIRSSDLKSKIELLKlevakaskTPDVTEKEKIEALEQQIKQKIAEALNSSELK---EKFEELEAELAAARETAAES 738
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
532-739 |
5.51e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 532 SESNKLKGEVESLKKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLGFKTIDELSGRIRELEKFHNKYIEAKNAE 611
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 612 KELRDILESLKDEREELDKAFEELAKIETDIEKVTSQLNELQRKFDQKKYEEKREKmmKLSMEIKGLETKLEELERRRD- 690
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK--ELVEKIKELEKELEKAKKALEk 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18202079 691 --EIKSTIEKLKEERKERESAKMEL-----------EKLNIAIKRIEELRGKIKEYKALIKE 739
Cdd:COG1340 159 neKLKELRAELKELRKEAEEIHKKIkelaeeaqelhEEMIELYKEADELRKEADELHKEIVE 220
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
565-714 |
5.73e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 565 IDKAKKELSEIEDRLLRLgfktIDELSGRIRELEKfhnKYIEAKNAEKELRDILESLKDEREELDKAFEELakietdiek 644
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNEL----IASLEELERELEQ---KAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL--------- 567
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18202079 645 vtsqLNELQRKFDQKKYEEKRE-----KMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERESAKMELE 714
Cdd:PRK00409 568 ----LEEAEKEAQQAIKEAKKEadeiiKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| PTZ00419 |
PTZ00419 |
valyl-tRNA synthetase-like protein; Provisional |
634-687 |
6.10e-03 |
|
valyl-tRNA synthetase-like protein; Provisional
Pssm-ID: 240411 [Multi-domain] Cd Length: 995 Bit Score: 40.37 E-value: 6.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18202079 634 ELAKIETDIEKVTSQLNELQRKFDQKKYEEK---------REKMMKLSMEIKGLETKLEELER 687
Cdd:PTZ00419 930 ELAKLEKKLAKLQKSLESYLKKISIPNYEDKvpedvrklnDEKIDELNEEIKQLEQAIEELKS 992
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
464-739 |
6.10e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 39.68 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 464 LSSIEKEIQEAKALERQLRAEFRKVENELSRLS----SLKTIADQIIEIRERLSKINLEDLKRDKEEYELLKSESNKLKG 539
Cdd:pfam04108 2 LSSAQDLCRWANELLTDARSLLEELVVLLAKIAflrrGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 540 EVESLKKEVNE------------LNDYKNESTkLEIEIDKAKKELSEIEDRLLRLGfKTIDELSGRIRELekfhNKYIEA 607
Cdd:pfam04108 82 TLDKLRNTPVEpalppgeekqktLLDFIDEDS-VEILRDALKELIDELQAAQESLD-SDLKRFDDDLRDL----QKELES 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 608 KNAEKELRDILESLKDEREELDKAFEELA-KIETDIEKVTSQLnelqrKFDQKKYEEKREKMMKLSMEikgLETKLEELE 686
Cdd:pfam04108 156 LSSPSESISLIPTLLKELESLEEEMASLLeSLTNHYDQCVTAV-----KLTEGGRAEMLEVLENDARE---LDDVVPELQ 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 18202079 687 RRRDEIKSTIEKLKEERKERESAKMELEKlniAIKRIEELRGKIKEYKALIKE 739
Cdd:pfam04108 228 DRLDEMENNYERLQKLLEQKNSLIDELLS---ALQLIAEIQSRLPEYLAALKE 277
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
497-744 |
6.29e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 497 SLKTIADQIIEIRERLSKINLEDLKRDKEEYELLKSESNKLKgevesLKKEVNELNDYKNESTKLEIEIDKAKKELSEie 576
Cdd:PRK05771 13 TLKSYKDEVLEALHELGVVHIEDLKEELSNERLRKLRSLLTK-----LSEALDKLRSYLPKLNPLREEKKKVSVKSLE-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 577 dRLLRLGFKTIDELSGRIRELEkfhnkyieakNAEKELRDILESLKDEREELD--KAFEELAKIETDIEKVTSQLNELQR 654
Cdd:PRK05771 86 -ELIKDVEEELEKIEKEIKELE----------EEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYVSVFVGTVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 655 KFDQkkyeekrekmmklsmEIKGLETKLEELERRRDEIKSTI----EKLKEERKERESAKMELEKLNI--------AIKR 722
Cdd:PRK05771 155 DKLE---------------ELKLESDVENVEYISTDKGYVYVvvvvLKELSDEVEEELKKLGFERLELeeegtpseLIRE 219
|
250 260
....*....|....*....|..
gi 18202079 723 IEELRGKIKEYKALIKEEALNK 744
Cdd:PRK05771 220 IKEELEEIEKERESLLEELKEL 241
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
782-866 |
6.55e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 782 VERPLTFLSGGERIALGLAfrlamsMYLIGKVDLLILDEPTPFLDEERrrklIEIMERHLRKIS-QVIIVSHDEELKDA- 859
Cdd:PRK10636 143 LERPVSDFSGGWRMRLNLA------QALICRSDLLLLDEPTNHLDLDA----VIWLEKWLKSYQgTLILISHDRDFLDPi 212
|
....*..
gi 18202079 860 ADHVIRI 866
Cdd:PRK10636 213 VDKIIHI 219
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
458-725 |
6.65e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 458 RKYSLELSSIEKEIQEAKALE-----RQLRAEFRKVENELSrLSSLKTIADQIIEIRERLSKINLedlKRDKEEYELLKS 532
Cdd:PRK04778 37 RKQELENLPVNDELEKVKKLNltgqsEEKFEEWRQKWDEIV-TNSLPDIEEQLFEAEELNDKFRF---RKAKHEINEIES 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 533 ESNKLKGEVESLKKEVNELndyKNESTKLEIEIDKAKKELSEIEDRLLRLGFK---TIDELSGRIRELEKFHNKYIEAKN 609
Cdd:PRK04778 113 LLDLIEEDIEQILEELQEL---LESEEKNREEVEQLKDLYRELRKSLLANRFSfgpALDELEKQLENLEEEFSQFVELTE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 610 AEkelrDILESlkdeREELDKAFEELAKIETDIEKVTSQLNELQRKF-DQ---------------------------KKY 661
Cdd:PRK04778 190 SG----DYVEA----REILDQLEEELAALEQIMEEIPELLKELQTELpDQlqelkagyrelveegyhldhldiekeiQDL 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18202079 662 EEKREKMMKL--SMEIKGLETKLEELERRRDEIKSTIEKlkeERKERESAKMELEKLNIAIKRIEE 725
Cdd:PRK04778 262 KEQIDENLALleELDLDEAEEKNEEIQERIDQLYDILER---EVKARKYVEKNSDTLPDFLEHAKE 324
|
|
| PRK05776 |
PRK05776 |
DNA topoisomerase I; Provisional |
390-521 |
7.46e-03 |
|
DNA topoisomerase I; Provisional
Pssm-ID: 235602 [Multi-domain] Cd Length: 670 Bit Score: 39.98 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 390 EKINEKLLYLENRKKELEEEIDKITRKIGELNQRSKD--RRLA-IIELKKARGKCPVCGRELTEehkaDLLRKYSLE-LS 465
Cdd:PRK05776 545 EKLEMIRTGKATREEVIEEAKETLNKLLEEFKKNKDEigEELAkALGLIKPVGKCKICGREAYK----DGLCKYHYEaKK 620
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 18202079 466 SIEKEIQEAKaleRQLRAEFRKVeneLSRLSSLKTIADQIIEIRERLSKINLEDLK 521
Cdd:PRK05776 621 RLVKAYEEWK---ERTGYDHKEY---LEKISKLKSTGKWVKDVITYMLNMNDKSWK 670
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
222-733 |
7.59e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 222 LRRELEGIKEEVKTLEATFNSITELKL-RLGELNGKKGRLEERIRQLESGIEEKRKKSKELEEVVKElpELEKKETEYRR 300
Cdd:pfam01576 297 LGEELEALKTELEDTLDTTAAQQELRSkREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTE--QLEQAKRNKAN 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 301 LIEFKDEYLVKKNELEKRLGILSNRLQEVKRKIKDAESKvarirwieerLKEIQEKIMKLEPRVREFEDAM-RLKAQMES 379
Cdd:pfam01576 375 LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQ----------LQELQARLSESERQRAELAEKLsKLQSELES 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 380 LKSKLGGLEPE--KINEKLLYLENRKKELEEEIDKITRKigELNQRSKDRRLaiielkkargkcpvcgreltEEHKADLL 457
Cdd:pfam01576 445 VSSLLNEAEGKniKLSKDVSSLESQLQDTQELLQEETRQ--KLNLSTRLRQL--------------------EDERNSLQ 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 458 RKyslelssIEKEIQEAKALERQLRAEFRKVENELSRLSSLKTIADQIIEIRERLSKiNLEDLKRDKEE----YELLKSE 533
Cdd:pfam01576 503 EQ-------LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQR-ELEALTQQLEEkaaaYDKLEKT 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 534 SNKLKGEVESL------------------KKEVNELNDYKNESTKLEIEIDKAKKELSEIEDRLLRLGfktidelsgriR 595
Cdd:pfam01576 575 KNRLQQELDDLlvdldhqrqlvsnlekkqKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA-----------R 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 596 ELEKFHNKYIEAKNAEKELRDILESLKDEREELDKAFEELAK----IETDIEKVTSQLNELQRKFD-------------- 657
Cdd:pfam01576 644 ALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERskraLEQQVEEMKTQLEELEDELQatedaklrlevnmq 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 658 ----------QKKYEEKREKMMKLSMEIKGLETKLEELERRRDEIKSTIEKLKEERKERES-AKMELEKLNIAIKRIEEL 726
Cdd:pfam01576 724 alkaqferdlQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAqIDAANKGREEAVKQLKKL 803
|
....*..
gi 18202079 727 RGKIKEY 733
Cdd:pfam01576 804 QAQMKDL 810
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
799-870 |
9.30e-03 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 38.67 E-value: 9.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18202079 799 LAFRLAMSMyligKVDLLILDEPTPFLDEERRRKLIEIMERHLRKISQVIIVSHDEE-LKDAADHVI-----RIRLEG 870
Cdd:cd03220 151 LAFAIATAL----EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSsIKRLCDRALvlekgKIRFDG 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
768-867 |
9.58e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 39.71 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 768 AEDNkVKLFVIYDGVERP---------LTFLSGGERIAL-------GLAFRLAMSMYLIGKVDLLILDEPTPFLDEERRR 831
Cdd:PRK10535 103 AAQN-VEVPAVYAGLERKqrllraqelLQRLGLEDRVEYqpsqlsgGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
90 100 110
....*....|....*....|....*....|....*.
gi 18202079 832 KLIEIMERHLRKISQVIIVSHDEELKDAADHVIRIR 867
Cdd:PRK10535 182 EVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIR 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1-43 |
9.75e-03 |
|
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: 37.90 E-value: 9.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 18202079 1 MKIERVIVQNFRSH---KNSEIEFKPGIN-LIIGQNGAGKSSLLDAI 43
Cdd:cd03223 1 IELENLSLATPDGRvllKDLSFEIKPGDRlLITGPSGTGKSSLFRAL 47
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| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
190-381 |
9.91e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 39.63 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 190 KTENIEDLIRTQEKsftevlnEIRNISSNLPRLRRELEGIKEEVKTLEATfnsitelklrlgelngkkgrleerIRQLES 269
Cdd:pfam05667 322 KVETEEELQQQREE-------ELEELQEQLEDLESSIQELEKEIKKLESS------------------------IKQVEE 370
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202079 270 GIEEKRKKSKELEE-------VVKELPELEKKETEYRRLIEFKDEYLVK-KNELEKRLGILSNRLQEVKRKI----KDAE 337
Cdd:pfam05667 371 ELEELKEQNEELEKqykvkkkTLDLLPDAEENIAKLQALVDASAQRLVElAGQWEKHRVPLIEEYRALKEAKsnkeDESQ 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18202079 338 SKVARIRWIEERLKEIQEKIMKLEPRVREfedamrLKAQMESLK 381
Cdd:pfam05667 451 RKLEEIKELREKIKEVAEEAKQKEELYKQ------LVAEYERLP 488
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