|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-882 |
0e+00 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 795.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 1 MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYW--PLRIKDIKKDEFTKVGARDTYIDLIFEKD 78
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWghGSKPKGLKKDDFTRIGGSGTEIELKFEKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 79 GTKYRITRRFLKGyssgeIHAMKRLVGNEwkhVTEPSSKAISAFMEKLIPYNIFLNAIYIRQGQIDAILESDEAREKVVR 158
Cdd:PRK03918 81 GRKYRIVRSFNRG-----ESYLKYLDGSE---VLEEGDSSVREWVERLIPYHVFLNAIYIRQGEIDAILESDESREKVVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 159 EVLNLDKFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVLR 238
Cdd:PRK03918 153 QILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 239 LEETKVEIENSERLLEKRRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEFKNEYLDKKYKI 318
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 319 EKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKDHQLYEEIKAKKENLRQLKEKLGDKSPEDIKKL 398
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 399 LEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKCPVCGRELTDEHREELLSKYHLDLNNSKNTLAKLI 478
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 479 DRKSELERELRRIDMEIK---RLTPLLTVAEQIRSIEEELNVVNLEKIEKNATEYEKLLEELRTLEGRIRGLAEDLKKLA 555
Cdd:PRK03918 473 EKERKLRKELRELEKVLKkesELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 556 PLEKKLAALIHKKQELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKRYLTLLNSKKELEITQREIAKAKETLEMSF 635
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 636 EELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKKELEKRRDTIKSTLEKLKAEKENRERVKKE 715
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 716 IKDLEKAKDFTEELIEKVKKYKALAREAALSKIGELASEIFAEFTEGKYSEVVVRAEENKVRLFVVWEGKERPLTFLSGG 795
Cdd:PRK03918 713 LEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFEELTEGKYSGVRVKAEENKVKLFVVYQGKERPLTFLSGG 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 796 ERIALGLAFRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKDAADHVIRISLENGS 875
Cdd:PRK03918 793 ERIALGLAFRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDEELKDAADYVIRVSLEGGV 872
|
....*..
gi 499321815 876 SKVEVVS 882
Cdd:PRK03918 873 SKVEVVS 879
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
1-882 |
3.45e-58 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 214.96 E-value: 3.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 1 MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYwpLRIKDIKKDEFTKVGARDTYIDLIFEKDGT 80
Cdd:NF041034 1 MKIERIFLENFLSHESSEVNFKGSINAIIGHNGAGKSSIIDGIVFSLF--RESSRGNNEDLIKKGKKTATVELKLEDNGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 81 KYRITRRFLKGYSSGEIHAMKRLVGNEWKHVTEPSSKAISAFMEklipynIFLNAIYIRQGQIDAILESDEAREKVVREV 160
Cdd:NF041034 79 TYLIKRNIPNSYSDDDTISNLKTIARGSTEVNQKIQEILNLDKD------VLLSTVIVRQGEIESIFKNLPDVMKKILKI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 161 LNLDKFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVLRLE 240
Cdd:NF041034 153 ENLEKLTDSNGPIYSVIKEIENKLKYLESEKERYESKEAEKEKLEKEIEESKNKLEDLEIKKEEKEKELNDLKKEFEELE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 241 ETKVEIENSERLLEKRRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEFKnEYLDKKYKIEK 320
Cdd:NF041034 233 KKRERYDELTGRLSSLNKRINEIEEDLKDLEKLKKEKEKLEKEIKEKEKLEEKNEIISELKELIKSIK-ELKRQLNTLEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 321 ELTRVEELINEIQKrieelnekeseKEKLENEKKEILNKLAILEKDHQLYEEIKAK-KENLRQLKEKLGDKSPEDIKKLL 399
Cdd:NF041034 312 EIEEYKENLKKKKE-----------LEDKAKKYEELKREKEELEEKENEYNSLKSRlNSLKKKLEEIENEISKLGIIINI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 400 EELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKG-KCPVCGRELTDEHREELlskyhldLNNSKNTLAKLI 478
Cdd:NF041034 381 EELKKKLDKLSEEINNKNNEKGEIKGRKEQLLKILKNLNNVKGnKCPVCGRELDEEHKKKI-------REEIEEKIKDLN 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 479 DRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVNLEKIEKNATEYEKLLEELRTLEGRIRGLAEDLKKLAPL- 557
Cdd:NF041034 454 KQISKLEKEVNSLNKEKEELENKINKLQEEKLIKLEKLLKELQRLKKEIEEIEKELKELEESHEEYEEIKEELKELEPKy 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 558 ----------EKKLAALIHKKQELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKRYLTLLNSKKELEITQREIAKA 627
Cdd:NF041034 534 keylkvsnvtEEELEELERRLSEIKSELDELEKKYSELKEKIGDDREELTQIEKKIEKKIKEIKELKNKLEKLKEEIAKI 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 628 KETLemsfEELAEVEADIERIEKKLSQLkqKYNEEEYKKKREEKEELEKELARLEAQKKELEKRRDTIKSTLEKLKAEKE 707
Cdd:NF041034 614 EKEK----EEIEKIENEIKELEEEISSL--NFDEERYQNLKEKIEKLNKELNRIEQEISKLEGKIEALENDIDNLNSELE 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 708 NRERVKKEIKDLEKAKDFTEELIEKV--KKYKALAREAALSKIGELASEIFAEFtEGKYSEVVV------RAEENKVRLF 779
Cdd:NF041034 688 KIKEKLNKIPKLENAIKKLEKLREDLsgSGLQNYIISNVKSKIENNLNDILSKF-DLSFSRVEIdfeiggKTKKGKSEIK 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 780 VV-WEGKERPLTFLSGGERIALGLAFRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEE 858
Cdd:NF041034 767 AYnTAGQDLDVNALSGGERISIALALRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHDEE 846
|
890 900
....*....|....*....|....
gi 499321815 859 LKDAADHVIRISLENGSSKVEVVS 882
Cdd:NF041034 847 LKEISDYIISVEKKGDSSKVKVGS 870
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-881 |
1.79e-54 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 203.98 E-value: 1.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 1 MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYWPLRIKDIkkDEFTKVGARDTYIDLIFEKDGT 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIEFDTGINIITGKNGAGKSSIVDAIRFALFTDKRTEKI--EDMIKKGKNNLEVELEFRIGGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 81 KYRITRRFLKGYSSGEIHAMKRLVGNEWKHVTEPSSKAISAFMEKlIPYNIFLNAIYIRQGQIDAILESDEA-REKVVRE 159
Cdd:PRK01156 79 VYQIRRSIERRGKGSRREAYIKKDGSIIAEGFDDTTKYIEKNILG-ISKDVFLNSIFVGQGEMDSLISGDPAqRKKILDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 160 VLNLDKFETAYKKLSELKKTINNRIKEYRDI-------LARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDML 232
Cdd:PRK01156 158 ILEINSLERNYDKLKDVIDMLRAEISNIDYLeeklkssNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 233 RKEVLRLEETKVEIENSERLLEKRRGDKRTLEERIknteeyleklkEKEKELEEQVKEITSikkdvDAYLALKEFKNEYL 312
Cdd:PRK01156 238 KSALNELSSLEDMKNRYESEIKTAESDLSMELEKN-----------NYYKELEERHMKIIN-----DPVYKNRNYINDYF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 313 DKKYKIEKELTRVEELINEIQ------KRIEELNEKESEKEKLENEKKEILNKLAILEKDHQLY-------EEIKAKKEN 379
Cdd:PRK01156 302 KYKNDIENKKQILSNIDAEINkyhaiiKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYnsylksiESLKKKIEE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 380 LRQLKEKLGDK----------SPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKkAKGKCPVCGR 449
Cdd:PRK01156 382 YSKNIERMSAFiseilkiqeiDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLN-GQSVCPVCGT 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 450 ELTDEHREELLSKYhldlNNSKNTLAKLIDrksELERELRRIDMEIKRLTPLLTVAE------------QIRSIEEELN- 516
Cdd:PRK01156 461 TLGEEKSNHIINHY----NEKKSRLEEKIR---EIEIEVKDIDEKIVDLKKRKEYLEseeinksineynKIESARADLEd 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 517 -VVNLEKIEKNATEYEKLLEELRTLE-GRIRGLAED-LKKLAPLEK-KLAALIHKKQELEKELKELNTKLESF--GFKSV 590
Cdd:PRK01156 534 iKIKINELKDKHDKYEEIKNRYKSLKlEDLDSKRTSwLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIeiGFPDD 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 591 ED-LDSKLRELEEIYKRYLTLLNSKKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNEEEYKkkre 669
Cdd:PRK01156 614 KSyIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKA---- 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 670 ekeelekeLARLEAQKKELEKRRDTIKSTLEKLKAEKENRERVKKEIKDLEKAKDFTEELIEKVKK--YKALAREAALSK 747
Cdd:PRK01156 690 --------LDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKsgVPAMIRKSASQA 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 748 IGELASEIFAEFtEGKYSEVVVRAEENkvrLFVVWEGKERPLTFLSGGERIALGLAFRLAMSLYLAGEISLLILDEPTPY 827
Cdd:PRK01156 762 MTSLTRKYLFEF-NLDFDDIDVDQDFN---ITVSRGGMVEGIDSLSGGEKTAVAFALRVAVAQFLNNDKSLLIMDEPTAF 837
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 499321815 828 LDEERRRKLITIMERYLKK---IPQVILVSHDEELKDAADHVIRISLENGSSKVEVV 881
Cdd:PRK01156 838 LDEDRRTNLKDIIEYSLKDssdIPQVIMISHHRELLSVADVAYEVKKSSGSSKVIPL 894
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-869 |
1.91e-38 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 154.81 E-value: 1.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 1 MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYWPLRIKDIKKDEFTKvGARDTYIDLIFEKDGT 80
Cdd:PRK02224 1 MRFDRVRLENFKCYADADLRLEDGVTVIHGVNGSGKSSLLEACFFALYGSKALDDTLDDVITI-GAEEAEIELWFEHAGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 81 KYRITRRFlkgYSSGEIHAMKRLVGNEWKHVTEpSSKAISAFMEKLIPYN--IFLNAIYIRQGQIDA-ILESDEAREKVV 157
Cdd:PRK02224 80 EYHIERRV---RLSGDRATTAKCVLETPEGTID-GARDVREEVTELLRMDaeAFVNCAYVRQGEVNKlINATPSDRQDMI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 158 REVLNLDKFETAYKKLSELKKTINNRIKEYR----DILARTENIEE-----LIKENEQELIQVLQEISKIEEVLPSKRSK 228
Cdd:PRK02224 156 DDLLQLGKLEEYRERASDARLGVERVLSDQRgsldQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 229 VDMLRKEVLRLEETKVEIENSERLLEKrrgdkrtLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEFK 308
Cdd:PRK02224 236 RDEADEVLEEHEERREELETLEAEIED-------LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 309 NEYL-DKKYKIEKELTRVEELINE----IQKRIEELNEKESEKEKLENEKKEILNKLAILEKDHQ-LYEEIKAKKENLRQ 382
Cdd:PRK02224 309 AEAVeARREELEDRDEELRDRLEEcrvaAQAHNEEAESLREDADDLEERAEELREEAAELESELEeAREAVEDRREEIEE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 383 LKEKLGD--KSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKK--AKGKCPVCGRELTDEHREE 458
Cdd:PRK02224 389 LEEEIEElrERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAllEAGKCPECGQPVEGSPHVE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 459 LLSKYhldlnnsKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEelnvvNLEKIEKNATEYEKLLEELR 538
Cdd:PRK02224 469 TIEED-------RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEE-----RREDLEELIAERRETIEEKR 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 539 TLEGRIRGLAEDLKKLAPLEKKLAALIHKKQE--------LEKELKELNTKLESFGfkSVEDLDSKLRELEEIYKRYLTL 610
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEeareevaeLNSKLAELKERIESLE--RIRTLLAAIADAEDEIERLREK 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 611 LNSKKELEITQREIAKAK----ETLEMSFEE--LAEVEADIERIEKKLSQLKQKyneeeykkkreekeelekeLARLEAQ 684
Cdd:PRK02224 615 REALAELNDERRERLAEKrerkRELEAEFDEarIEEAREDKERAEEYLEQVEEK-------------------LDELREE 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 685 KKELEKRRDTIKSTLEKLKAEKENRERVKKEIKDLEKAKDFTEELIEKVKKYKALAREAALSKIGELASEIFA-EFTEGK 763
Cdd:PRK02224 676 RDDLQAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLERMLNETFDlVYQNDA 755
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 764 YSEVVVRAEENkvrlFVVWEGKERPLT--FLSGGERIALGLAFRLAMSLYLA----GEISL--LILDEPTPYLDEERRRK 835
Cdd:PRK02224 756 YSHIELDGEYE----LTVYQKDGEPLEpeQLSGGERALFNLSLRCAIYRLLAegieGDAPLppLILDEPTVFLDSGHVSQ 831
|
890 900 910
....*....|....*....|....*....|....*.
gi 499321815 836 LITIMErYLKKI--PQVILVSHDEELKDAADHVIRI 869
Cdd:PRK02224 832 LVDLVE-SMRRLgvEQIVVVSHDDELVGAADDLVRV 866
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
786-870 |
2.35e-27 |
|
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: 110.39 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 786 ERPLTFLSGGERIALGLAFRLAMSLYLAGEISLLILDEPTPYLDEERRR-KLITIMERYLK-KIPQVILVSHDEELKDAA 863
Cdd:cd03240 110 LDMRGRCSGGEKVLASLIIRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSqKNFQLIVITHDEELVDAA 189
|
....*..
gi 499321815 864 DHVIRIS 870
Cdd:cd03240 190 DHIYRVE 196
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-197 |
1.85e-23 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 98.93 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 2 KLERVTVKNFRSHSDT-VVEFKEGINLIIGQNGSGKSSLLDAILVGLYWPLRIKDIKKDEFTKVGARDTYIDLIFEKDGT 80
Cdd:COG0419 1 KLLRLRLENFRSYRDTeTIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 81 KYRITRrflkgyssgeihamkrlvgnewkhvtepsskaisafmeklipyniflnaiyiRQGQIDAILESD-EAREKVVRE 159
Cdd:COG0419 81 RYRIER----------------------------------------------------RQGEFAEFLEAKpSERKEALKR 108
|
170 180 190
....*....|....*....|....*....|....*...
gi 499321815 160 VLNLDKFETAYKKLSELKKTINNRIKEYRDILARTENI 197
Cdd:COG0419 109 LLGLEIYEELKERLKELEEALESALEELAELQKLKQEI 146
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
195-866 |
1.27e-21 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 100.23 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 195 ENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVLRLEETKVEIENSERLLEKRRGDKRTLEERIKNteeyl 274
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL----- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 275 eklkekekeleeqvkeitsiKKDVDAYLALKEFKNEYLDKKYKIEKELTRVEELINEIQkrieelnekesekeklenekk 354
Cdd:COG4717 128 --------------------LPLYQELEALEAELAELPERLEELEERLEELRELEEELE--------------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 355 eilnklailekdhQLYEEIKAKKENLRQLKEKLGDKSPEDIKKLLEELEtkktTIEEERNEITQRIGELKNKIGDLKTAI 434
Cdd:COG4717 167 -------------ELEAELAELQEELEELLEQLSLATEEELQDLAEELE----ELQQRLAELEEELEEAQEELEELEEEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 435 EELKKakgkcpvcgrELTDEHREELLSKYHLDLnNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEE 514
Cdd:COG4717 230 EQLEN----------ELEAAALEERLKEARLLL-LIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 515 LNVVNLEKIEKNAT----EYEKLLEELRTLEGRIRGLAEDLKKLAPLEKKLAALIHKKQELEKEL------KELNTKLES 584
Cdd:COG4717 299 SLGKEAEELQALPAleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqleeleQEIAALLAE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 585 FGFKSVEDldskLRELEEIYKRYLTLLNSKKELEITQREIAKAKETLeMSFEELAEVEADIERIEKKLSQLKQKYNeeey 664
Cdd:COG4717 379 AGVEDEEE----LRAALEQAEEYQELKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELE---- 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 665 kkkreekeELEKELARLEAQKKELEKRRdtiksTLEKLKAEKENRERVKKEIKDLEKAKDFTEELIEKVKKYkalAREAA 744
Cdd:COG4717 450 --------ELREELAELEAELEQLEEDG-----ELAELLQELEELKAELRELAEEWAALKLALELLEEAREE---YREER 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 745 LSKIGELASEIFAEFTEGKYSEVVVrAEENKVRLfVVWEGKERPLTFLSGGERIALGLAFRLAMSLYLAGEISLLILDEP 824
Cdd:COG4717 514 LPPVLERASEYFSRLTDGRYRLIRI-DEDLSLKV-DTEDGRTRPVEELSRGTREQLYLALRLALAELLAGEPLPLILDDA 591
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 499321815 825 TPYLDEERRRKLITIMERYLKKIpQVILVSHDEELKDAADHV 866
Cdd:COG4717 592 FVNFDDERLRAALELLAELAKGR-QVIYFTCHEELVELFQEE 632
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-148 |
5.64e-21 |
|
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: 91.90 E-value: 5.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 3 LERVTVKNFRS-HSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYW--PLRIKDIKKD-EFTKVGARDTYIDLIFEKD 78
Cdd:cd03240 1 IDKLSIRNIRSfHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGelPPNSKGGAHDpKLIREGEVRAQVKLAFENA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499321815 79 -GTKYRITRRFlkgyssgeihamkrlvgnewkhvtepsskaisafmeklipyNIFLNAIYIRQGQIDAILE 148
Cdd:cd03240 81 nGKKYTITRSL-----------------------------------------AILENVIFCHQGESNWPLL 110
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
374-878 |
5.56e-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: 79.73 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 374 KAKKENLRQLKEKLgdkspEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKCpvcgRELTD 453
Cdd:TIGR02169 670 RSEPAELQRLRERL-----EGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL----KERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 454 EHREELlSKYHLDLNNSKNTLAKLIDRKSELERELRRIDmeikrltplltvaEQIRSIEEELNVVNLEKIEKnatEYEKL 533
Cdd:TIGR02169 741 ELEEDL-SSLEQEIENVKSELKELEARIEELEEDLHKLE-------------EALNDLEARLSHSRIPEIQA---ELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 534 LEELRTLEGRIRGLAEDLKKLAPLEKKLAAlihKKQELEKELKELNTKLESFGfKSVEDLDSKLRELEEIYKRY-LTLLN 612
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLEK---EIQELQEQRIDLKEQIKSIE-KEIENLNGKKEELEEELEELeAALRD 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 613 SKKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLK-----QKYNEEEYKKKREEKEELEKELARLEAQKKE 687
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKakleaLEEELSEIEDPKGEDEEIPEEELSLEDVQAE 959
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 688 LEKRRDTIKSTLEKLKAEKENRERVKKEIKDLEKAKDFTEE----LIEKVKKYKALAREA---ALSKIGELASEIFAEFT 760
Cdd:TIGR02169 960 LQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEerkaILERIEEYEKKKREVfmeAFEAINENFNEIFAELS 1039
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 761 EGKYSEVVVRAE---ENKVRLFVVWEGKE-RPLTFLSGGERIALGLAFRLAMSLYLAGEISLliLDEPTPYLDEERRRKL 836
Cdd:TIGR02169 1040 GGTGELILENPDdpfAGGLELSAKPKGKPvQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYA--FDEVDMFLDGVNVERV 1117
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 499321815 837 ITiMERYLKKIPQVILVSHDEELKDAADHVIRISL-ENGSSKV 878
Cdd:TIGR02169 1118 AK-LIREKAGEAQFIVVSLRSPMIEYADRAIGVTMrRNGESQV 1159
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-878 |
8.38e-15 |
|
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: 78.86 E-value: 8.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 1 MKLERVTVKNFRSHSDTVVEF---KEGINLIIGQNGSGKSSLLDAILVGLYWPLRIK---DIKKDEFTKVGARDTYIDLI 74
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDftaLGPIFLICGKTGAGKTTLLDAITYALYGKLPRRsevIRSLNSLYAAPSEAAFAELE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 75 FEKDGTKYRITRRFLKGYSSGEIHAMKRLVGNEWKHVTEPSSKAISAFMEKL-----IPYNIFLNAIYIRQGQIDAIL-E 148
Cdd:TIGR00618 81 FSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIhdllkLDYKTFTRVVLLPQGEFAQFLkA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 149 SDEAREKVVREVLNLDKFET----AYKKLSELKKTINNRIKEY-----------RDILARTENIEELIKENEQELIQ--- 210
Cdd:TIGR00618 161 KSKEKKELLMNLFPLDQYTQlalmEFAKKKSLHGKAELLTLRSqlltlctpcmpDTYHERKQVLEKELKHLREALQQtqq 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 211 ----------VLQEISKIEEVLPSKRSKVDMLRKEVLRLEETKVEIENSERL---------LEKRRGDKRTLEERIKNTE 271
Cdd:TIGR00618 241 shayltqkreAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAaplaahikaVTQIEQQAQRIHTELQSKM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 272 EYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEFKNEYLDKKYKIEKELTRVEELINEIQKRIEELNEKESEKEKLEN 351
Cdd:TIGR00618 321 RSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 352 EKKEILNKLAILEKDHQLYEEIKAKKENLRQlKEKLGDKSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLK 431
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFRDLQGQLAHAKK-QQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 432 TAIEELKKAKG------------KCPVCGRELTDEHREELL-----------------SKYHLDLNNSKNTLAKLIDRKS 482
Cdd:TIGR00618 480 QIHLQETRKKAvvlarllelqeePCPLCGSCIHPNPARQDIdnpgpltrrmqrgeqtyAQLETSEEDVYHQLTSERKQRA 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 483 ELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVNLEKIEKNATEYEKLLEELRTLEGRIRGLAEDL----------- 551
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQdvrlhlqqcsq 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 552 ---KKLAPLEKKLAALIHKKQEL----------------EKELKELNTKLESFGF--KSVEDLDSKLRELEEIYKRY--- 607
Cdd:TIGR00618 640 elaLKLTALHALQLTLTQERVREhalsirvlpkellasrQLALQKMQSEKEQLTYwkEMLAQCQTLLRELETHIEEYdre 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 608 -------------------LTLLNSKKELEITQREIAKAKE-----------TLEMSFEELAEVEADIERIEKKLSQLKQ 657
Cdd:TIGR00618 720 fneienassslgsdlaareDALNQSLKELMHQARTVLKARTeahfnnneevtAALQTGAELSHLAAEIQFFNRLREEDTH 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 658 KYNEEEYKKKREEKEELEKELARLEAQKKELEKRRDTIKSTLEKLKAEKENRERVKKEIKDLEKAKDFTEELIEKVKK-- 735
Cdd:TIGR00618 800 LLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKln 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 736 -------------YKALAREAALSKIGELASEIFAEFTeGKYSEVVVRAEENKVRLFVVWE---GKERPLTFLSGGERIA 799
Cdd:TIGR00618 880 ginqikiqfdgdaLIKFLHEITLYANVRLANQSEGRFH-GRYADSHVNARKYQGLALLVADaytGSVRPSATLSGGETFL 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 800 LGLAFRLAMSLYLAGE----ISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKDAADHVIRISLENGS 875
Cdd:TIGR00618 959 ASLSLALALADLLSTSggtvLDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRILVKKTNAG 1038
|
...
gi 499321815 876 SKV 878
Cdd:TIGR00618 1039 SHV 1041
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
409-865 |
2.92e-14 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 77.08 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 409 IEEERNEITQRIGELKNKIGDLKTAIEELKKAKGK-CPVCGRELTDEHREELLSKYHL-DLNNSKNTLAKLIDRKS-ELE 485
Cdd:COG4694 104 LEEEIEELEKEIEDLKKELDKLEKELKEAKKALEKlLEDLAKSIKDDLKKLFASSGRNyRKANLEKKLSALKSSSEdELK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 486 RELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVnLEKIEKNA--TEYEKLLEEL------RTLEGRIRG----------- 546
Cdd:COG4694 184 EKLKLLKEEEPEPIAPITPLPDLKALLSEAETL-LEKSAVSSaiEELAALIQNPgnsdwvEQGLAYHKEeeddtcpfcqq 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 547 -LAEDLKKL------APLEKKLAALIHKKQELEKELKELNTKLESFGFKSVE----DLDSKLRELEEIYKRYLTLLNSKK 615
Cdd:COG4694 263 eLAAERIEAleayfdDEYEKLLAALKDLLEELESAINALSALLLEILRTLLPsakeDLKAALEALNALLETLLAALEEKI 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 616 ELEITQREIAKAKETLEMSfEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKKELEKRRDTI 695
Cdd:COG4694 343 ANPSTSIDLDDQELLDELN-DLIAALNALIEEHNAKIANLKAEKEEARKKLEAHELAELKEDLSRYKAEVEELIEELKTI 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 696 KSTLEKLKAEKENRERVKKEIKDLEKAKD-FTEELiekvkkykalareaalskigelaseifAEFTEGKYSEVVVRAEEN 774
Cdd:COG4694 422 KALKKALEDLKTEISELEAELSSVDEAADeINEEL---------------------------KALGFDEFSLEAVEDGRS 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 775 KVRLFVVWEGKERPLTFLSGGERIALGLAFRLAmSLYLAGEI---SLLILDEPTPYLDEERRRKLITIMERYLKKIPQVI 851
Cdd:COG4694 475 SYRLKRNGENDAKPAKTLSEGEKTAIALAYFLA-ELEGDENDlkkKIVVIDDPVSSLDSNHRFAVASLLKELSKKAKQVI 553
|
490
....*....|....*...
gi 499321815 852 LVSHDE----ELKDAADH 865
Cdd:COG4694 554 VLTHNLyflkELRDLADE 571
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
792-869 |
6.10e-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: 6.10e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499321815 792 LSGGERIALGLAFRLAMSLYlaGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKDAADHVIRI 869
Cdd:cd03227 78 LSGGEKELSALALILALASL--KPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
375-855 |
4.49e-13 |
|
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: 73.55 E-value: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 375 AKKENLRQLKEKLgdkspEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKcpvcgRELTDE 454
Cdd:TIGR02168 674 ERRREIEELEEKI-----EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-----LEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 455 HREELLSKYHLDLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVA--------EQIRSIEEELNVVNlEKIEKN 526
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLkeelkalrEALDELRAELTLLN-EEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 527 ATEYEKLLEELRTLEGRIRGLAEDLKKLaplEKKLAALIHKKQELEKELKELNTKLESFgfksVEDLDSKLRELEEIYKR 606
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEEL---SEDIESLAAEIEELEELIEELESELEAL----LNERASLEEALALLRSE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 607 YLTLLNSKKELEitqREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKK 686
Cdd:TIGR02168 896 LEELSEELRELE---SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 687 ELEKRRDTIKS-------TLEKLKAEKENRERVKKEIKDLEKAKDFTEELIEKVKKyKALAR-EAALSKIGELASEIFAE 758
Cdd:TIGR02168 973 RLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR-EARERfKDTFDQVNENFQRVFPK 1051
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 759 FTEGKYSEVVVRAEENK----VRLFVVWEGKE-RPLTFLSGGERIALGLAfrLAMSLYLAGEISLLILDEPTPYLDEERR 833
Cdd:TIGR02168 1052 LFGGGEAELRLTDPEDLleagIEIFAQPPGKKnQNLSLLSGGEKALTALA--LLFAIFKVKPAPFCILDEVDAPLDDANV 1129
|
490 500
....*....|....*....|..
gi 499321815 834 RKLITIMERYLKKIpQVILVSH 855
Cdd:TIGR02168 1130 ERFANLLKEFSKNT-QFIVITH 1150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
792-869 |
7.05e-13 |
|
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: 67.27 E-value: 7.05e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499321815 792 LSGGERialglaFRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHD-EELKDAADHVIRI 869
Cdd:cd00267 81 LSGGQR------QRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVL 153
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-220 |
3.15e-12 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 66.37 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 6 VTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYWplRIKDIKKDEFTKVGARDTYIDLIFEKDgTKYRIT 85
Cdd:pfam13476 1 LTIENFRSFRDQTIDFSKGLTLITGPNGSGKTTILDAIKLALYG--KTSRLKRKSGGGFVKGDIRIGLEGKGK-AYVEIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 86 RRFLKGYSSGEIHAMKRLVGNewkhvtepsskaisaFMEKLIPYNIFLNAIYIRQGQIDAILESDEARekvvrevLNLDK 165
Cdd:pfam13476 78 FENNDGRYTYAIERSRELSKK---------------KGKTKKKEILEILEIDELQQFISELLKSDKII-------LPLLV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499321815 166 FETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELiQVLQEISKIEE 220
Cdd:pfam13476 136 FLGQEREEEFERKEKKERLEELEKALEEKEDEKKLLEKLLQLK-EKKKELEELKE 189
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-583 |
6.31e-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: 69.71 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 3 LERVTVKNFRSHSD-TVVEFKEGINLIIGQNGSGKSSLLDAILVGLyWPLRIKDIKKDEFTkvgardtyiDLIFEKDGTK 81
Cdd:TIGR02169 2 IERIELENFKSFGKkKVIPFSKGFTVISGPNGSGKSNIGDAILFAL-GLSSSKAMRAERLS---------DLISNGKNGQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 82 ------YRITRRFLKGYSSGEIHAMKRLVgnewkhVTEPSSKAIsafmeklipynIFLNAIYIRQGQIDAILESDEAREK 155
Cdd:TIGR02169 72 sgneayVTVTFKNDDGKFPDELEVVRRLK------VTDDGKYSY-----------YYLNGQRVRLSEIHDFLAAAGIYPE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 156 VVREVLNLDkfetaykklseLKKTINNRIKEYRDILARTENIEELIKENEqeliQVLQEISKIEEVLPSKRSKVDMLRKE 235
Cdd:TIGR02169 135 GYNVVLQGD-----------VTDFISMSPVERRKIIDEIAGVAEFDRKKE----KALEELEEVEENIERLDLIIDEKRQQ 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 236 VLRLEETKVEIENSERLLEKRRgdKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDaylalkefkneyldkk 315
Cdd:TIGR02169 200 LERLRREREKAERYQALLKEKR--EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS---------------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 316 yKIEKELTRVEELINEIQKRIeelnekeseKEKLENEKKEILNKLAILEKD-HQLYEEIKAKKENLRQLKEKLGdKSPED 394
Cdd:TIGR02169 262 -ELEKRLEEIEQLLEELNKKI---------KDLGEEEQLRVKEKIGELEAEiASLERSIAEKERELEDAEERLA-KLEAE 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 395 IKKLLEELETKKTTIEEERNE---ITQRIGELKNKIGDLKTAIEELKKAkgkcpvcGRELTDEH--REELLSKYHLDLNN 469
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRrdkLTEEYAELKEELEDLRAELEEVDKE-------FAETRDELkdYREKLEKLKREINE 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 470 SKNTLAKLIDRKSELERELRRIDMEIKRLtplltvaeqirsieeelnvvnLEKIEKNATEYEKLLEELRTLEGRIRGLAE 549
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGI---------------------EAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
570 580 590
....*....|....*....|....*....|....
gi 499321815 550 DLKKlapLEKKLAALIHKKQELEKELKELNTKLE 583
Cdd:TIGR02169 463 DLSK---YEQELYDLKEEYDRVEKELSKLQRELA 493
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-43 |
1.46e-11 |
|
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: 66.95 E-value: 1.46e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 499321815 1 MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAI 43
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSIELSDDLTVLVGENNSGKSSILEAL 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
474-749 |
3.27e-11 |
|
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: 67.39 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 474 LAKLIDRKSELERELRRIDMEIKRLTPLL-TVAEQIRSIEEELNVVNLEKIEKNA------TEYEKLLEELRTLEGRIRG 546
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELeELTAELQELEEKLEELRLEVSELEEeieelqKELYALANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 547 LAEDLK----KLAPLEKKLAALIHKKQELEKELKELNTKLESFGfKSVEDLDSKLRELEEIYKRYLTLLNSKKELEITQR 622
Cdd:TIGR02168 307 LRERLAnlerQLEELEAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 623 -EIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKKELEKRRDTIKSTLEK 701
Cdd:TIGR02168 386 sKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 499321815 702 LKAE-KENRERVKKEIKDLEKAK---DFTEELIEKVKKYKALAREAALSKIG 749
Cdd:TIGR02168 466 LREElEEAEQALDAAERELAQLQarlDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-61 |
4.17e-11 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 64.63 E-value: 4.17e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499321815 1 MKLERVTVKNFRSHSDTVVEF--KEGINLIIGQNGSGKSSLLDAILVGLYWPL-RIKDIKKDEF 61
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEIDFdnPPRLTVLVGENGSGKTTLLEAIALALSGLLsRLDDVKFRKL 64
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
317-704 |
8.16e-11 |
|
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: 66.24 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 317 KIEKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKDhqlyeeiKAKKENLRQLKEKLGDKSPEDIK 396
Cdd:TIGR02169 157 KIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-------REKAERYQALLKEKREYEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 397 KLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKCPVCGRELTDEHREEL---LSKYHLDLNNSKNT 473
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkekIGELEAEIASLERS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 474 LAKLIDRKSELERELRRIDMEIKRLtplltvAEQIRSIEEELNVVNLEKiEKNATEYEKLLEELRTLEGRIRGLAEDLK- 552
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKL------LAEIEELEREIEEERKRR-DKLTEEYAELKEELEDLRAELEEVDKEFAe 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 553 ---KLAPLEKKLAALIHKKQELEKELKELNTKLESfgfksvedLDSKLRELEEIYKRyltLLNSKKELEITQREIAKAKE 629
Cdd:TIGR02169 383 trdELKDYREKLEKLKREINELKRELDRLQEELQR--------LSEELADLNAAIAG---IEAKINELEEEKEDKALEIK 451
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499321815 630 TLEmsfEELAEVEADIERIEKKLSQLKQKYNeeeykKKREEKEELEKELARLEAQKKELEKRRDTIKSTLEKLKA 704
Cdd:TIGR02169 452 KQE---WKLEQLAADLSKYEQELYDLKEEYD-----RVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
472-731 |
1.30e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 472 NTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVnleKIEKNATEYEKLLEELRTLEGRIRGLAEDL 551
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAEL---EYLRAALRLWFAQRRLELLEAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 552 KKLaplEKKLAALIHKKQELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYK-------RY--------LTLLNSKKE 616
Cdd:COG4913 305 ARL---EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEererrraRLeallaalgLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 617 LEITQREIAKAKETLEmsfEELAEVEADIERIEKKLSQLKQKyneeeykkkreekeelekeLARLEAQKKELEKRRDTIK 696
Cdd:COG4913 382 FAALRAEAAALLEALE---EELEALEEALAEAEAALRDLRRE-------------------LRELEAEIASLERRKSNIP 439
|
250 260 270
....*....|....*....|....*....|....*
gi 499321815 697 STLEKLkaekenRERVKKEIKDLEKAKDFTEELIE 731
Cdd:COG4913 440 ARLLAL------RDALAEALGLDEAELPFVGELIE 468
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
2-43 |
1.47e-10 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 63.64 E-value: 1.47e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 499321815 2 KLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAI 43
Cdd:COG1195 1 RLKRLSLTNFRNYESLELEFSPGINVLVGPNGQGKTNLLEAI 42
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
3-47 |
1.56e-10 |
|
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: 61.46 E-value: 1.56e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 499321815 3 LERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGL 47
Cdd:cd03276 1 IESITLKNFMCHRHLQIEFGPRVNFIVGNNGSGKSAILTALTIGL 45
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
792-870 |
1.71e-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: 59.77 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGERIalglafRLAMSLYLAGEISLLILDEPTPYLDEERRRKLitimERYLKKIPQ-VILVSHDEELKDA-ADHVIRI 869
Cdd:cd03221 71 LSGGEKM------RLALAKLLLENPNLLLLDEPTNHLDLESIEAL----EEALKEYPGtVILVSHDRYFLDQvATKIIEL 140
|
.
gi 499321815 870 S 870
Cdd:cd03221 141 E 141
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
139-733 |
1.86e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 139 RQGQIDAILESDEAREKVVREVLNLD-KFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISK 217
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 218 IEEVLPSKRSKVDMLRKEVLRLEETKVEIENSERLLEKRRGDKRTLEERIKNTEEYLEKlkekekeleeqvkeitsikkd 297
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE--------------------- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 298 vdaylALKEFKNEYLDKKYKIEKELTRVEELINEIQKRieeLNEKESEKEKLENEKKEILNKLAILEKDHQLYEEIKAKK 377
Cdd:COG1196 380 -----ELEELAEELLEALRAAAELAAQLEELEEAEEAL---LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 378 ENLRQLKEKLGDKSpEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDL------KTAIEELKKAKGKCPVCGREL 451
Cdd:COG1196 452 AELEEEEEALLELL-AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegflegVKAALLLAGLRGLAGAVAVLI 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 452 TDEHREELLSkYHLDLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVNLEKIEKNATEYE 531
Cdd:COG1196 531 GVEAAYEAAL-EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLR 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 532 KLLEELRTLEGRIRGLAEDLKKLAPLEKKLAALIHKKQELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKRYLTLL 611
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 612 NSKKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKkELEKR 691
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE-ELERE 768
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 499321815 692 RDTIKSTLEKL-----------KAEKENRERVKKEIKDLEKAKDFTEELIEKV 733
Cdd:COG1196 769 LERLEREIEALgpvnllaieeyEELEERYDFLSEQREDLEEARETLEEAIEEI 821
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
785-867 |
3.11e-10 |
|
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: 61.19 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 785 KERPLTFLSGGE--RIALglAFRLAMslylagEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHD-EELKD 861
Cdd:COG1122 128 ADRPPHELSGGQkqRVAI--AGVLAM------EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAE 199
|
....*.
gi 499321815 862 AADHVI 867
Cdd:COG1122 200 LADRVI 205
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
170-722 |
6.09e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 6.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 170 YKKLSELKKTINN--RIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVLRLEETKVEIE 247
Cdd:COG1196 215 YRELKEELKELEAelLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 248 NSerlLEKRRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAylALKEFKNEYLDKKYKIEKELTRVEE 327
Cdd:COG1196 295 AE---LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE--ELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 328 LINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKDHQlyeEIKAKKENLRQLKEKLgDKSPEDIKKLLEELETKKT 407
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE---ALLERLERLEEELEEL-EEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 408 TIEEERNEITQRIGELKNKIGDLKTAIEELKKAkgkcpvcgRELTDEHREELLSKYHLDLNNSKNTLAKLID-RKSELER 486
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAA--------LAELLEELAEAAARLLLLLEAEADYEGFLEGvKAALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 487 ELRRIDMEIKRLtpLLTVAEQIRSIEEELNVVNLEKIEKNATEYEKLLEEL-RTLEGRIRGLAEDL---KKLAPLEKKLA 562
Cdd:COG1196 518 GLRGLAGAVAVL--IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLkAAKAGRATFLPLDKiraRAALAAALARG 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 563 ALIHKKQELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKR---------------------YLTLLNSKKELEITQ 621
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAvtlagrlrevtlegeggsaggSLTGGSRRELLAALL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 622 REIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKKELEKRRDTIKSTLEK 701
Cdd:COG1196 676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
570 580
....*....|....*....|.
gi 499321815 702 LkAEKENRERVKKEIKDLEKA 722
Cdd:COG1196 756 L-PEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
475-755 |
1.18e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 475 AKLIDRKSELERELRRIDMEIKRLTPLLT--------------VAEQIRSIEEELNVVnleKIEKNATEYEKLLEELRTL 540
Cdd:COG1196 168 SKYKERKEEAERKLEATEENLERLEDILGelerqleplerqaeKAERYRELKEELKEL---EAELLLLKLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 541 EGRIRGLAEDLKKLaplEKKLAALIHKKQELEKELKELNTKLESFGfKSVEDLDSKLRELEEIYKRYLTLL-NSKKELEI 619
Cdd:COG1196 245 EAELEELEAELEEL---EAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRrELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 620 TQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKKELEKRRD------ 693
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAaaelaa 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499321815 694 TIKSTLEKLKAEKENRERVKKEIKDLEKAKDFTEELIEKVKKYKALAREAALSKIGELASEI 755
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-88 |
1.50e-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: 58.82 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 1 MKLERVTVKNFRS-HSDTVVEF----KEGINLIIGQNGSGKSSLLDAILVGLYW--PLRIKDIKKDEFTKVGARDTYIDL 73
Cdd:cd03279 1 MKPLKLELKNFGPfREEQVIDFtgldNNGLFLICGPTGAGKSTILDAITYALYGktPRYGRQENLRSVFAPGEDTAEVSF 80
|
90
....*....|....*
gi 499321815 74 IFEKDGTKYRITRRF 88
Cdd:cd03279 81 TFQLGGKKYRVERSR 95
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
785-874 |
1.73e-09 |
|
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: 58.63 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 785 KERPLTFLSGGE--RIALGLAfrlamslyLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHD-EELKD 861
Cdd:cd03225 128 RDRSPFTLSGGQkqRVAIAGV--------LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDlDLLLE 199
|
90
....*....|...
gi 499321815 862 AADHVIRisLENG 874
Cdd:cd03225 200 LADRVIV--LEDG 210
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-77 |
1.76e-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: 57.70 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 3 LERVTVKNFRSHSD-TVVEFKEGINLIIGQNGSGKSSLLDAILVGL---YWPLRIKDIKKD--EFTKVGARDTYIDLIFE 76
Cdd:cd03239 1 IKQITLKNFKSYRDeTVVGGSNSFNAIVGPNGSGKSNIVDAICFVLggkAAKLRRGSLLFLagGGVKAGINSASVEITFD 80
|
.
gi 499321815 77 K 77
Cdd:cd03239 81 K 81
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
5-71 |
1.79e-09 |
|
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: 58.76 E-value: 1.79e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499321815 5 RVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYWPL----RIKDIKkdEFTKVGARDTYI 71
Cdd:cd03277 5 RIKLENFVTYDETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPkllgRAKKVG--EFVKRGCDEGTI 73
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-755 |
2.19e-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: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 1 MKLERVTVKNFRSHSD-TVVEFKEGINLIIGQNGSGKSSLLDAILvglyWPL---RIKDIKKDEFTkvgardtyiDLIFe 76
Cdd:COG1196 1 MRLKRLELAGFKSFADpTTIPFEPGITAIVGPNGSGKSNIVDAIR----WVLgeqSAKSLRGGKME---------DVIF- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 77 kDGTKYR---------------------------ITRR-FLKGYSSGEIHAMK-RLvgnewKHVTE--------PSSkai 119
Cdd:COG1196 67 -AGSSSRkplgraevsltfdnsdgtlpidydevtITRRlYRSGESEYYINGKPcRL-----KDIQDlfldtglgPES--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 120 safmeklipYNIflnaiyIRQGQIDAILES---------DEA---------REK-----------------VVREV-LNL 163
Cdd:COG1196 138 ---------YSI------IGQGMIDRIIEAkpeerraiiEEAagiskykerKEEaerkleateenlerledILGELeRQL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 164 DKF----ETA--YKKLSELKKTINN--RIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKE 235
Cdd:COG1196 203 EPLerqaEKAerYRELKEELKELEAelLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 236 VLRLEETKVEIENSerlLEKRRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAylALKEFKNEYLDKK 315
Cdd:COG1196 283 LEEAQAEEYELLAE---LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE--ELEEAEEELEEAE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 316 YKIEKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKDHQlyeEIKAKKENLRQLKEKLgDKSPEDI 395
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE---ALLERLERLEEELEEL-EEALAEL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 396 KKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAkgkcpvcgRELTDEHREELLSKYHLDLNNSKNTLA 475
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA--------LAELLEELAEAAARLLLLLEAEADYEG 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 476 KLID-RKSELERELRRIDMEIKRLtpLLTVAEQIRSIEEELNVVNLEKIEKNATEYEKLLEEL-RTLEGRIRGLAEDL-- 551
Cdd:COG1196 506 FLEGvKAALLLAGLRGLAGAVAVL--IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLkAAKAGRATFLPLDKir 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 552 -KKLAPLEKKLAALIHKKQELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKRyLTLLNSKKELEITQREIAKAKET 630
Cdd:COG1196 584 aRAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA-VTLAGRLREVTLEGEGGSAGGSL 662
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 631 LEMSFEELAEVEADIERIEKKLSQLKQKyneeeykkkreEKEELEKELARLEAQKKELEKRRDTIKSTLEKLKAEKENRE 710
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAE-----------EELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 499321815 711 RVKKEIKDLEKAKDFTEELIEKVKKYKALAREAALSKIGELASEI 755
Cdd:COG1196 732 AEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
310-717 |
2.31e-09 |
|
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: 61.24 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 310 EYLDKKYKIEKELTRVEELINEIQKRIEELNEKesekeklenekkeiLNKLAILEKDHQLYEEIKAKKENLRQ---LKEK 386
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQ--------------LERLRREREKAERYQALLKEKREYEGyelLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 387 LG-DKSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELkkakgkcpvcGRELTDEHREELLSkYHL 465
Cdd:TIGR02169 233 EAlERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL----------GEEEQLRVKEKIGE-LEA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 466 DLNNSKNTLAKLIDRKSELERELRRIDMEIKRLtplltvAEQIRSIEEELNVVNLEKiEKNATEYEKLLEELRTLEGRIR 545
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKL------LAEIEELEREIEEERKRR-DKLTEEYAELKEELEDLRAELE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 546 GLAEDLK----KLAPLEKKLAALIHKKQELEKELKELNTKLESfgfksvedLDSKLRELEEIYKRyltLLNSKKELEITQ 621
Cdd:TIGR02169 375 EVDKEFAetrdELKDYREKLEKLKREINELKRELDRLQEELQR--------LSEELADLNAAIAG---IEAKINELEEEK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 622 REIAKAKETLEmsfEELAEVEADIERIEKKLSQLKQKYNEEEYkkkreekeelekelaRLEAQKKELEKRRDTIKSTLEK 701
Cdd:TIGR02169 444 EDKALEIKKQE---WKLEQLAADLSKYEQELYDLKEEYDRVEK---------------ELSKLQRELAEAEAQARASEER 505
|
410
....*....|....*.
gi 499321815 702 LKAEKENRERVKKEIK 717
Cdd:TIGR02169 506 VRGGRAVEEVLKASIQ 521
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-43 |
2.98e-09 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 59.79 E-value: 2.98e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 499321815 1 MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAI 43
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDLELSPGVNVLVGENGQGKTNLLEAI 43
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
158-747 |
3.52e-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: 60.42 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 158 REVLNLDKFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVL 237
Cdd:TIGR04523 90 KLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 238 RLEETKVEIENserllekrrgDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVdayLALKEFKNEYLDKKYK 317
Cdd:TIGR04523 170 ELENELNLLEK----------EKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQI---SELKKQNNQLKDNIEK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 318 IEKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEIL--NKLAILEKDHQLyEEIKAKKENLRQLKEKLGDKspeDI 395
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELeqNNKKIKELEKQL-NQLKSEISDLNNQKEQDWNK---EL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 396 KKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKCPvcgRELTDEHREelLSKYHLDLNNSKNTLA 475
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQ---RELEEKQNE--IEKLKKENQSYKQEIK 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 476 KLIDRKSELERELRRIDMEIKRLTplltvaEQIRSIEEElnvvnLEKIEKnatEYEKLLEELRTLEGRIRGLAEdlkKLA 555
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKD------EQIKKLQQE-----KELLEK---EIERLKETIIKNNSEIKDLTN---QDS 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 556 PLEKKLAALIHKKQELEKELKELNTKLEsfgfKSVEDLDSKLRELEEIYKRYLTLLNSKKELEITQREIAKAKETLEMSF 635
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSIN----KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKI 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 636 EELaevEADIERIEKKLSQLKQKYNEEEYkkkreekeelekelarlEAQKKELEKRRDTIKSTLEKLKAEKENRERVKKE 715
Cdd:TIGR04523 527 EKL---ESEKKEKESKISDLEDELNKDDF-----------------ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
570 580 590
....*....|....*....|....*....|....*..
gi 499321815 716 IKDL-----EKAKDFTEELIEKVKKYKALAREAALSK 747
Cdd:TIGR04523 587 KQELidqkeKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
165-755 |
6.75e-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: 59.65 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 165 KFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVLRLEEtkv 244
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 245 EIENSERLLEKRRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDvdaylaLKEFKNEYLDKKYKIEKELTR 324
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND------LKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 325 VEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILE-KDHQLYEEIKAKKENLRQLKEKLgDKSPEDIKKLLEELE 403
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKkQNNQLKDNIEKKQQEINEKTTEI-SNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 404 TKKTTIEEERNEITQ---RIGELKNKIGDLKTAIEELKKAKGKcpvcgrELTDEHREELLSKYHlDLNNSKNTLAKLIDR 480
Cdd:TIGR04523 264 KIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLNNQKEQ------DWNKELKSELKNQEK-KLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 481 KSELERELRRIDMEIKRLTplLTVAEQIRSIEEELNvvnleKIEKNATEYEKLLEELRTLEGRIRGLAEDLKKLAPLEKK 560
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSE--SENSEKQRELEEKQN-----EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 561 LAALIHK----KQELEKE---LKELNTKLESfgfkSVEDLDSKLRELEEIYKRYLTLLNS-KKELEITQREIAKAKETLE 632
Cdd:TIGR04523 410 KDEQIKKlqqeKELLEKEierLKETIIKNNS----EIKDLTNQDSVKELIIKNLDNTRESlETQLKVLSRSINKIKQNLE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 633 MSFEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEkelarLEAQKKELEKRRDTIKSTLEKLKAEKeNRERV 712
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK-----LESEKKEKESKISDLEDELNKDDFEL-KKENL 559
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 499321815 713 KKEI----KDLEKAKDFTEELIEKVKKYKALAREAAlSKIGELASEI 755
Cdd:TIGR04523 560 EKEIdeknKEIEELKQTQKSLKKKQEEKQELIDQKE-KEKKDLIKEI 605
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
2-43 |
9.69e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 58.40 E-value: 9.69e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 499321815 2 KLERVTVKNFRSHSDTVVEFkEGINLIIGQNGSGKSSLLDAI 43
Cdd:COG4637 1 MITRIRIKNFKSLRDLELPL-GPLTVLIGANGSGKSNLLDAL 41
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
786-881 |
1.11e-08 |
|
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: 55.41 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 786 ERPLTFLSGGERIALglafRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKDAADH 865
Cdd:cd03238 82 GQKLSTLSGGELQRV----KLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADW 157
|
90
....*....|....*.
gi 499321815 866 VIRISLENGSSKVEVV 881
Cdd:cd03238 158 IIDFGPGSGKSGGKVV 173
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-755 |
1.26e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 165 KFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVLRLE---- 240
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEekle 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 241 ETKVEIENSERLLEKRRGDKRTLEERIKNteeYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEFKNEYLDKkYKIEK 320
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEE---LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER-LQQEI 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 321 ELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKD-HQLYEEIKAKKENLRQLKEKLgdKSPEDIKKLL 399
Cdd:TIGR02168 424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREElEEAEQALDAAERELAQLQARL--DSLERLQENL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 400 EELETKKTTIEEERNEITQRIGELKNKI---------------GDL-----------KTAIEELKKA-KGKCPVC----- 447
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLSELIsvdegyeaaieaalgGRLqavvvenlnaaKKAIAFLKQNeLGRVTFLpldsi 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 448 -GRELTDEHREELLSKyhldlNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVNLE----- 521
Cdd:TIGR02168 582 kGTEIQGNDREILKNI-----EGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDgdlvr 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 522 ----------KIEKNATEYEKlleELRTLEGRIRGLAEDLKKLaplEKKLAALIHKKQELEKELKELNTKLESFGFKSVE 591
Cdd:TIGR02168 657 pggvitggsaKTNSSILERRR---EIEELEEKIEELEEKIAEL---EKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 592 DLDSKLRELEEIYKRYLTLLNSKKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQ--KYNEEEYKKKRE 669
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEelKALREALDELRA 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 670 EKEELEKELARLEAQKKELEKRRDTIKSTLEKLKAEK----ENRERVKKEIKDLEKAKD-FTEELIEKVKKYKAL--ARE 742
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIeelsEDIESLAAEIEELEELIEeLESELEALLNERASLeeALA 890
|
650
....*....|...
gi 499321815 743 AALSKIGELASEI 755
Cdd:TIGR02168 891 LLRSELEELSEEL 903
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-220 |
1.98e-08 |
|
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: 57.61 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 1 MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAIlvglYWPLRIKDIKKDEFTKVGARDTYIDLIFEKDGT 80
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEIDLDEDLTVLIGKNNSGKSSILEAL----DIFLNNKEKFFEDDFLVLYLKDVIKIDKEDLNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 81 KYRItrrflkgYSSGEIHAMKRLVGNEWKHVTEPSSKAISAFMEKLIPYNIFLNAIYIRQGQIDAILESDEAREKVVREV 160
Cdd:pfam13175 77 FENI-------SFSIDIEIDVEFLLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISDLKKYLKQFK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499321815 161 LNLDKFETAYKKLSELKKTINNRIKEYRDILARTENIE-ELIKENEQELIQVLQEISKIEE 220
Cdd:pfam13175 150 IYIYNNYYLDEKKNVFDKKSKYELPSLKEEFLNSEKEEiKVDKEDLKKLINELEKSINYHE 210
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
150-735 |
2.12e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 150 DEAREKVVREVLNLDKFETAYKKLSELKKTINNRIKEYrdilARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKV 229
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE----ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 230 DMLRKEVLRLEETKVEIENSERLLEKRRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEFKN 309
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 310 EYLDKKYKIEKELTRVEELineiqKRIEELNEKESEKEKLENEKKEILNKLAILEKDHQLYEEIKAKKENLR---QLKEK 386
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEA-----KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKkadEAKKK 1452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 387 LGD-KSPEDIKKLLEE---LETKKTTIEEER--NEITQRIGELKNKIGDLKTAIEELKKAKGKCPVCGRELTDEHREELL 460
Cdd:PTZ00121 1453 AEEaKKAEEAKKKAEEakkADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 461 SKYHLDLNNSKNTLAKLIDRKSElerELRRIDmEIKRltplltvAEQIRSIEEELNVVNLEKIEKNATEYEKLLEELRTL 540
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAE---ELKKAE-EKKK-------AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 541 EGRIRGLAEDLKKlAPLEKKLAALIHKKQELEKELKELNTKLESFGFKSVEdldskLRELEEIYKRYLTLLNSKKELEIT 620
Cdd:PTZ00121 1602 EEEKKMKAEEAKK-AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE-----LKKAEEENKIKAAEEAKKAEEDKK 1675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 621 QREIAKAKETLEMSFEELAEVEADIERiekKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKKELEKRRDTikstlE 700
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAK---KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA-----E 1747
|
570 580 590
....*....|....*....|....*....|....*
gi 499321815 701 KLKAEKENRERVKKEIKDLEKAKDFTEELIEKVKK 735
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
138-719 |
2.20e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 138 IRQGQIDAILESDEAREKVVREVLNLDKFETAYKKLSELKKTINNRIKEY----RDILARTENIEELIKENEQELIQVLQ 213
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELeeelAELEEELEELEEELEELEEELEEAEE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 214 EISKIEEVLPSKRSKVDMLRKEVLRLEETKVEIENSERLLEKRRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKeiTS 293
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE--EA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 294 IKKDVDAYLALKEFKNEYLDKKYKIEKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKDHQLYEEI 373
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 374 KAKKENLRQLKEKLGDkspedIKKLLEELETKKTTIEEERNEITQRIGElkNKIGDLKTAIEELKKAKGkcpvcGR---- 449
Cdd:COG1196 510 VKAALLLAGLRGLAGA-----VAVLIGVEAAYEAALEAALAAALQNIVV--EDDEVAAAAIEYLKAAKA-----GRatfl 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 450 ELTDEHREELLSKYHLDLNNSKNTLAKLIDRKSELERELRRID---MEIKRLTPLLTVAEQIRSIEEELNVVNLEKIEKN 526
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 527 ATEYEKLLEELRTLEGRIRGLAEDLKKLAPLEKKLAALIHKKQELEKELKELNTKLEsfgfksvEDLDSKLRELEEIYKR 606
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE-------ERLEEELEEEALEEQL 730
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 607 YLTLLNSKKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQL--------------KQKYNEeeykkkreeke 672
Cdd:COG1196 731 EAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgpvnllaieeyeelEERYDF----------- 799
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 499321815 673 elekelarLEAQKKELEKRRDTIKSTLEKLKAEKENR-----ERVKKEIKDL 719
Cdd:COG1196 800 --------LSEQREDLEEARETLEEAIEEIDRETRERfletfDAVNENFQEL 843
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1-755 |
2.44e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 1 MKLERVTVKN---FrsHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYWPLRIK------DIKKDE----------- 60
Cdd:COG4913 1 FRLQRLQLINwgtF--DGVHTIDFDGRGTLLTGDNGSGKSTLLDAIQTLLVPAKRPRfnkaanDAGKSDrtllsyvrgky 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 61 --------FTKVGARD----TYIDLIFEKDGTKYRIT---RRFLKGySSGEIHAMKRLvgnewkHVTEPSSKAISAFMEK 125
Cdd:COG4913 79 gserdeagTRPVYLRPgdtwSAIAATFANDGSGQTVTlaqVFWLKG-DASSLGDVKRF------FVIADGPLDLEDFEEF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 126 LIPYNIflNAIYIRQGQIDA-ILESDEAREKVVREVLNL--DKFETAYKKLSELK--KTINNRIKEY----RDILARTEN 196
Cdd:COG4913 152 AHGFDI--RALKARLKKQGVeFFDSFSAYLARLRRRLGIgsEKALRLLHKTQSFKpiGDLDDFVREYmleePDTFEAADA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 197 IEELIK---------ENEQELIQVLQEISKIEEVLPSKRSKVDMLR--KEVLRLEETKVEIENSERLLEKRRGDKRTLEE 265
Cdd:COG4913 230 LVEHFDdlerahealEDAREQIELLEPIRELAERYAAARERLAELEylRAALRLWFAQRRLELLEAELEELRAELARLEA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 266 RIKNTEEYLEKLKEKEKeleeqvkeitsikkdvDAYLALKEFKNEYLDkkyKIEKELTRVEELINEIQKRIEELNEKese 345
Cdd:COG4913 310 ELERLEARLDALREELD----------------ELEAQIRGNGGDRLE---QLEREIERLERELEERERRRARLEAL--- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 346 keklenekkeiLNKLAILEKDHQlyEEIKAKKENLRQLKEKLGDKSpEDIKKLLEELETKKTTIEEERNEITQRIGELKN 425
Cdd:COG4913 368 -----------LAALGLPLPASA--EEFAALRAEAAALLEALEEEL-EALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 426 KIG-------DLKTAI-EELKKAKGKCPVCGrELTD---EHRE-----ELLskyhldLNNSKNTLakLIDRK--SELERE 487
Cdd:COG4913 434 RKSniparllALRDALaEALGLDEAELPFVG-ELIEvrpEEERwrgaiERV------LGGFALTL--LVPPEhyAAALRW 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 488 LRRIDMEiKRLtplltVAEQIRSIEEELNVVNL------EKIEKNATEYEKLL----------------EELR------T 539
Cdd:COG4913 505 VNRLHLR-GRL-----VYERVRTGLPDPERPRLdpdslaGKLDFKPHPFRAWLeaelgrrfdyvcvdspEELRrhpraiT 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 540 LEGRIRG--------------------------LAEDLKKLAPLEKKLAALIHKKQELEKELKELNT------KLESFGF 587
Cdd:COG4913 579 RAGQVKGngtrhekddrrrirsryvlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQErrealqRLAEYSW 658
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 588 KSVeDLDSKLRELEEIYKRYLTLLNSKKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNEEEYKKK 667
Cdd:COG4913 659 DEI-DVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 668 REEKEELEKELARLEAQKKEL--EKRRDTIKSTLEK-LKAEKENRERVKKEI-------------------KDLEKAKDF 725
Cdd:COG4913 738 AAEDLARLELRALLEERFAAAlgDAVERELRENLEErIDALRARLNRAEEELeramrafnrewpaetadldADLESLPEY 817
|
890 900 910
....*....|....*....|....*....|....*...
gi 499321815 726 --------TEELIEKVKKYKALAREAALSKIGELASEI 755
Cdd:COG4913 818 lalldrleEDGLPEYEERFKELLNENSIEFVADLLSKL 855
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-83 |
2.96e-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: 54.78 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 3 LERVTVKNFRSHSD-TVVEFKEGINLIIGQNGSGKSSLLDAILvglyWPL---RIKDIKKDEFTkvgardtyiDLIFekD 78
Cdd:cd03278 1 LKKLELKGFKSFADkTTIPFPPGLTAIVGPNGSGKSNIIDAIR----WVLgeqSAKSLRGEKMS---------DVIF--A 65
|
....*
gi 499321815 79 GTKYR 83
Cdd:cd03278 66 GSETR 70
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
150-775 |
3.52e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 150 DEAREKVVREVLNLDKFETAYKKLSELKKTINNRIKEYRdilaRTENIEELIKENEQELIQVLQEISKIEEVlpsKRSKV 229
Cdd:PTZ00121 1150 DAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVR----KAEELRKAEDARKAEAARKAEEERKAEEA---RKAED 1222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 230 DMLRKEVLRLEETKVEIENSERLLEKRRGD--KRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEF 307
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 308 KNEYLDKKYKIEKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAI-LEKDHQLYEEIKAKKENLRQLKEK 386
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADeAEAAEEKAEAAEKKKEEAKKKADA 1382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 387 LGDKSPEdiKKLLEELEtKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKA-KGKCPVCGRELTDEHREELLSKYHL 465
Cdd:PTZ00121 1383 AKKKAEE--KKKADEAK-KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKA 1459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 466 DLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVNlekiEKNATEYEKLLEELRTLEGRIR 545
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD----EAKKAEEAKKADEAKKAEEAKK 1535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 546 glAEDLKKLAplEKKLAALIHKKQELEKelKELNTKLESfGFKSVEDLDSKLRELEEIYK----RYLTLLNSKKELEITQ 621
Cdd:PTZ00121 1536 --ADEAKKAE--EKKKADELKKAEELKK--AEEKKKAEE-AKKAEEDKNMALRKAEEAKKaeeaRIEEVMKLYEEEKKMK 1608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 622 REIAKAKETLEMSFEELAEVEAdieriEKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKKELEKRRDTIKSTLEK 701
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEE-----EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499321815 702 LKAEKENRERVKKEIKDLEKAKDFTEELIEKVKKYKALAREAALSKIGELASEIFAEFTEGKYSEVVVRAEENK 775
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-746 |
3.66e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 304 LKEFKNEYLDKKYKIEKELTRVEELINEIQKRieelnekesekeklenekkeiLNKLailekdhqlyeEIKAKK-ENLRQ 382
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQ---------------------LKSL-----------ERQAEKaERYKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 383 LKEKLGDKSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKcpvcgreltdehREELLSK 462
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE------------LEEEIEE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 463 YHLDLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTplltvaeqirsieeelnvvnlEKIEKNATEYEKLLEELRTLEG 542
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELE---------------------AQLEELESKLDELAEELAELEE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 543 RIrglAEDLKKLAPLEKKLAALIHKKQELEKELKELNTKLESFgfksVEDLDSKLRELEEIYKRYLTLLNSKKELEITQR 622
Cdd:TIGR02168 345 KL---EELKEELESLEAELEELEAELEELESRLEELEEQLETL----RSKVAQLELQIASLNNEIERLEARLERLEDRRE 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 623 EIAKAKETLEMSFEE--LAEVEADIERIEKKLSQLKQKYN--EEEYKKKREEKEELEKELARLEAQKKELEKRRDTIKST 698
Cdd:TIGR02168 418 RLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELErlEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 499321815 699 LEKLKAEKENRERVKKEIKDLEKAKDFTEELIEKVKKYKAlAREAALS 746
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEA-AIEAALG 544
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
506-758 |
3.66e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 506 EQIRSIEEELNVVNlEKIEKNATEYEKLLEELRTLEGRIRGLAEDLKKLaplEKKLAAlihKKQELEKELKELNTKLESF 585
Cdd:COG3883 30 AELEAAQAELDALQ-AELEELNEEYNELQAELEALQAEIDKLQAEIAEA---EAEIEE---RREELGERARALYRSGGSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 586 GF-------KSVEDLDSKLRELEEIYKRYLTLLNSKKELEitqreiakaketlemsfeelAEVEADIERIEKKLSQLKQK 658
Cdd:COG3883 103 SYldvllgsESFSDFLDRLSALSKIADADADLLEELKADK--------------------AELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 659 yneeeykkkreekeelekeLARLEAQKKELEKRRDTIKSTLEKLKAEKENRErvkKEIKDLEKAKDFTEELIEKVKKYKA 738
Cdd:COG3883 163 -------------------KAELEAAKAELEAQQAEQEALLAQLSAEEAAAE---AQLAELEAELAAAEAAAAAAAAAAA 220
|
250 260
....*....|....*....|
gi 499321815 739 LAREAALSKIGELASEIFAE 758
Cdd:COG3883 221 AAAAAAAAAAAAAAAAAAAA 240
|
|
| Rad50_zn_hook |
pfam04423 |
Rad50 zinc hook motif; The Mre11 complex (Mre11 Rad50 Nbs1) is central to chromosomal ... |
423-474 |
4.70e-08 |
|
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: 49.88 E-value: 4.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 499321815 423 LKNKIGDLKTAIEELKKAKGKCPVCGRELTDEHREELLSKYHLDLNNSKNTL 474
Cdd:pfam04423 1 LHQETLELNKKIEELKEAEGCCPLCGRPLDEEHRSELIKELQSKLERLPEEL 52
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
792-874 |
5.90e-08 |
|
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: 56.31 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGERIALGLAfRLamslyLAGEISLLILDEPTPYLDEERRRKLITIMERYLK-KIpqVILVSHDEELKDAADHVIRis 870
Cdd:COG4987 472 LSGGERRRLALA-RA-----LLRDAPILLLDEPTEGLDAATEQALLADLLEALAgRT--VLLITHRLAGLERMDRILV-- 541
|
....
gi 499321815 871 LENG 874
Cdd:COG4987 542 LEDG 545
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
786-876 |
6.98e-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: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 786 ERPLTFLSGGE--RIALGLAFRLAMSLYLAGEISL--LILDEPTPYLDEERRRKLITImeryLKKIPQ----VILVSHDE 857
Cdd:cd03279 118 ARPVSTLSGGEtfLASLSLALALSEVLQNRGGARLeaLFIDEGFGTLDPEALEAVATA----LELIRTenrmVGVISHVE 193
|
90 100
....*....|....*....|
gi 499321815 858 ELKDAADHVIRIS-LENGSS 876
Cdd:cd03279 194 ELKERIPQRLEVIkTPGGSR 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
792-869 |
7.38e-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: 56.14 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGE--RIALGLAFrlamsLYLAGeisLLILDEPTPYLDEERRRKLITIMERYLKKiPQVILVSHDEELKDAADHVIRI 869
Cdd:TIGR02857 459 LSGGQaqRLALARAF-----LRDAP---LLLLDEPTAHLDAETEAEVLEALRALAQG-RTVLLVTHRLALAALADRIVVL 529
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
174-735 |
8.00e-08 |
|
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: 56.27 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 174 SELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKvdmlRKEVLRLEETKVEIENSERLL 253
Cdd:pfam05483 99 AELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNAT----RHLCNLLKETCARSAEKTKKY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 254 EKRRGDKRTLEERIKNteeyleklkekekeleeqvkeitSIKKDVDAYLALK-EFKNEYLDKKYKIEKELTRVEELINEI 332
Cdd:pfam05483 175 EYEREETRQVYMDLNN-----------------------NIEKMILAFEELRvQAENARLEMHFKLKEDHEKIQHLEEEY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 333 QKRIEELNEKESEKEKLENEKKEILNKLAIL-----EKDHQLYEEIKAKKENLRQLKEKLG--DKSPEDIKKLLEELETK 405
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLleesrDKANQLEEKTKLQDENLKELIEKKDhlTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 406 KTTIEEERNEITQRIGELKNkigDLKTAIEELKKAKGKCPVCGREL--TDEHREELLSKYHLDLNNSKNTLAKLIdrkse 483
Cdd:pfam05483 312 QKALEEDLQIATKTICQLTE---EKEAQMEELNKAKAAHSFVVTEFeaTTCSLEELLRTEQQRLEKNEDQLKIIT----- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 484 leRELRRIDMEIKRLTPlLTVAEQIRSIEEELNVVNLEKIEKNATEYEKLLEELRTLEGRIRGLAEDL-KKLAPLEKKLA 562
Cdd:pfam05483 384 --MELQKKSSELEEMTK-FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAReKEIHDLEIQLT 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 563 ALIHKKQELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKRYLTLLNSKKELEITQREIAKAKETLEMSFEElaeve 642
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQ----- 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 643 adIERIEKKLSQLKQKyneeeykkkreekeelekelarLEAQKKELEKRRDTIKSTLEKlkaEKENRERVKKEIKDLEKA 722
Cdd:pfam05483 536 --IENLEEKEMNLRDE----------------------LESVREEFIQKGDEVKCKLDK---SEENARSIEYEVLKKEKQ 588
|
570
....*....|...
gi 499321815 723 KDFTEELIEKVKK 735
Cdd:pfam05483 589 MKILENKCNNLKK 601
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-200 |
9.86e-08 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 54.66 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 3 LERVTVKNFRS-HSDTVVEFKEG------INLIIGQNGSGKSSLLDAILVgLYWPLRIKDIKKDEFTKVGARD------- 68
Cdd:COG1106 2 LISFSIENFRSfKDELTLSMVASglrllrVNLIYGANASGKSNLLEALYF-LRNLVLNSSQPGDKLVEPFLLDsesknep 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 69 TYIDLIFEKDGTKYRItrrflkgyssgEIHAMKRLVGNEWKHVTEPSSKAISAFMEKLipYNIFLNAIYI--RQGQIDAI 146
Cdd:COG1106 81 SEFEILFLLDGVRYEY-----------GFELDKERIISEWLYFLSTAAQLNVPLLSPL--YDWFDNNISLdtSSDGLTLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499321815 147 LESDEAREKVVREVLNldKFETAYKKLsELKKTINNRIKEYRDILARTENIEEL 200
Cdd:COG1106 148 LKEDESLKEELLELLK--IADPGIEDI-EVEEEEIEDLVERKLIFKHKGGNVPL 198
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
171-721 |
1.10e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 171 KKLSELKKTINNRIKEYRDILARTENieeliKENEQELIQVLQEISKIEEVL--PSKRSKVDMLRKevlRLEETKVEIEN 248
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAA-----KKKADEAKKKAEEKKKADEAKkkAEEAKKADEAKK---KAEEAKKAEEA 1462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 249 SERLLEKRRGD--KRTLEERiKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEFKNEYLDKKYKIEK--ELTR 324
Cdd:PTZ00121 1463 KKKAEEAKKADeaKKKAEEA-KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadEAKK 1541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 325 VEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKDHQLYEEIKAKKENLRQLKEKLGDKSPEDIKKllEELET 404
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK--AEEAK 1619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 405 KKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKCPVCGRELTDEHREEllSKYHLDLNNSKNTLAKLIDRKSEL 484
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKAAEALKKE 1697
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 485 ERELRRIDMEIKRLTPLLTVAEQIRSiEEELNVVNLEKIEKNATEYEKLLEELRTLEGRIRGLAEDLKKlaplEKKLAAL 564
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKK-AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKE----EEKKAEE 1772
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 565 IHKKQE--LEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKRYLTLLNSKKELEITqrEIAKAKETLEMSFEELAEVE 642
Cdd:PTZ00121 1773 IRKEKEavIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDS--AIKEVADSKNMQLEEADAFE 1850
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 643 ADI--------ERIEKKLSQLKQKYNEEEYKKKREEKEELEKE----LARLEAQKKELEKRRDTIKSTLEKLKAEKENRE 710
Cdd:PTZ00121 1851 KHKfnknnengEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIdkddIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAE 1930
|
570
....*....|.
gi 499321815 711 RVKKEIKDLEK 721
Cdd:PTZ00121 1931 ETREEIIKISK 1941
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
792-870 |
1.83e-07 |
|
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: 52.88 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGE--RIALGLAfrlamslyLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQ-VILVSHDEELKDAADHVIR 868
Cdd:cd03255 141 LSGGQqqRVAIARA--------LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTtIVVVTHDPELAEYADRIIE 212
|
..
gi 499321815 869 IS 870
Cdd:cd03255 213 LR 214
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
146-554 |
1.92e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 146 ILESDEAREKVVREVLNL-DKFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEvlps 224
Cdd:TIGR02168 672 ILERRREIEELEEKIEELeEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE---- 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 225 krskvdMLRKEVLRLEETKVEIENSERLLEKRRGDKRTLEERIKNteeyleKLKEKEKELEEQVKEITSIKKDVDAYLAL 304
Cdd:TIGR02168 748 ------RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEE------LEAQIEQLKEELKALREALDELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 305 KEFKNEYLDKKYKIEKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAilEKDHQLYEEIKAKKENLRQLK 384
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE--SELEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 385 EKLGDKSPEdikklLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKkakgkcpvcgreltdehrEELLSKYH 464
Cdd:TIGR02168 894 SELEELSEE-----LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ------------------ERLSEEYS 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 465 LDLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPlltvaeqirsieeelnvVNLEKIEknatEYEKLLEELRTLEGRI 544
Cdd:TIGR02168 951 LTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP-----------------VNLAAIE----EYEELKERYDFLTAQK 1009
|
410
....*....|
gi 499321815 545 RGLAEDLKKL 554
Cdd:TIGR02168 1010 EDLTEAKETL 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
480-757 |
2.18e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 480 RKSELERELRRIDMEIKRLTPLLTvaeqirsiEEELNVVNLEKIEKNATEYEKLLEELRTLEGRIRG--LAEDLKKLAPL 557
Cdd:TIGR02168 173 RRKETERKLERTRENLDRLEDILN--------ELERQLKSLERQAEKAERYKELKAELRELELALLVlrLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 558 EKKLAALIHKKQELEKELKELNTKLEsfgfksveDLDSKLRELEEiykryltllnskkeleitqrEIAKAKETLEMSFEE 637
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLE--------ELRLEVSELEE--------------------EIEELQKELYALANE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 638 LAEVEADIERIEKKLSQLKQKyneeeykkkreekeelekeLARLEAQKKELEKRRDTIKSTLEKLKAEKenrERVKKEIK 717
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQ-------------------LEELEAQLEELESKLDELAEELAELEEKL---EELKEELE 354
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 499321815 718 DLEkakdftEELIEKVKKYKAL--AREAALSKIGELASEIFA 757
Cdd:TIGR02168 355 SLE------AELEELEAELEELesRLEELEEQLETLRSKVAQ 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
318-606 |
2.28e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 318 IEKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILNkLAILEKDH-QLYEEIKAKKENLRQLkeklgDKSPEDIK 396
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE-YSWDEIDVaSAEREIAELEAELERL-----DASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 397 KL---LEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKCPVCGRELTDEHREELLSKYHLDLNNSK-- 471
Cdd:COG4913 689 ALeeqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERElr 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 472 ----NTLAKLIDRKSELERELRRIDMEIKRLTPLLTvAEQIRSIEEelnvvnlekieknATEYEKLLEELRTLEgrirgl 547
Cdd:COG4913 769 enleERIDALRARLNRAEEELERAMRAFNREWPAET-ADLDADLES-------------LPEYLALLDRLEEDG------ 828
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 548 aedlkklaplekklaaLIHKKQELEKELKELNTklesfgfKSVEDLDSKL-RELEEIYKR 606
Cdd:COG4913 829 ----------------LPEYEERFKELLNENSI-------EFVADLLSKLrRAIREIKER 865
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
787-874 |
2.34e-07 |
|
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: 53.95 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 787 RPLTfLSGGE--RIALGLAfrlamslyLAGEISLLILDEPTPYLDEERRRKLITIMERyLKK---IPqVILVSHD-EELK 860
Cdd:COG4148 130 RPAT-LSGGErqRVAIGRA--------LLSSPRLLLMDEPLAALDLARKAEILPYLER-LRDeldIP-ILYVSHSlDEVA 198
|
90
....*....|....
gi 499321815 861 DAADHVirISLENG 874
Cdd:COG4148 199 RLADHV--VLLEQG 210
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-480 |
2.43e-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: 54.68 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 138 IRQGQIDAILESDEAREKVVREvlnLDKFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISK 217
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARL---EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 218 IEEVLPSKRSKVDMLRKEVLRLEETKVEIENSERLLEKRRGDK-RTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKK 296
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATeRRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 297 DVDAYLALKEFKNEYLDkkyKIEKELTRVEELINEIQKRIEELNEKesekeklenekkeilnklaiLEKDHQLYEEIKAK 376
Cdd:TIGR02168 874 ELEALLNERASLEEALA---LLRSELEELSEELRELESKRSELRRE--------------------LEELREKLAQLELR 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 377 KENLRQLKEKLGDKSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLK----TAIEELKKAKGkcpvcgrelt 452
Cdd:TIGR02168 931 LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlAAIEEYEELKE---------- 1000
|
330 340
....*....|....*....|....*...
gi 499321815 453 dehREELLSKYHLDLNNSKNTLAKLIDR 480
Cdd:TIGR02168 1001 ---RYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
148-708 |
2.62e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 148 ESDEARE-KVVREVLNLDKFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKR 226
Cdd:PTZ00121 1291 KADEAKKaEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 227 SKVDMLRKEVLRLEETKVEIENSERLLEKRRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEitSIKKDVDAYLALKE 306
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD--EAKKKAEEAKKADE 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 307 FKNEYLDKKyKIEKELTRVEEL--INEIQKRIEELNEKesekeklenekkeilnklailEKDHQLYEEIKAKKENLRQLK 384
Cdd:PTZ00121 1449 AKKKAEEAK-KAEEAKKKAEEAkkADEAKKKAEEAKKA---------------------DEAKKKAEEAKKKADEAKKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 385 EKlgDKSPEDIKKLLEELETKKTTIEEERNEITQ-RIGELKNKIGDLKTAiEELKKAKGKCPVCGRELTDEHREELLSKY 463
Cdd:PTZ00121 1507 EA--KKKADEAKKAEEAKKADEAKKAEEAKKADEaKKAEEKKKADELKKA-EELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 464 HLDLNNSKntlAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVnlEKIEKNATEYEKLLEELRTLEGR 543
Cdd:PTZ00121 1584 EEAKKAEE---ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV--EQLKKKEAEEKKKAEELKKAEEE 1658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 544 IRGLAEDLKKLAPLEKKLAALIHKKQELEKELKELNTKLESFGFKSVEdldskLRELEEIYKRYLTLLNSKKELEITQRE 623
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE-----LKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 624 IAKAKETLEMSFEELAEVEadiERIEKKLSQLKQKYNEEEYKKKREEKEELEkelarlEAQKKELEKRRDTIKSTLEKLK 703
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKD---EEEKKKIAHLKKEEEKKAEEIRKEKEAVIE------EELDEEDEKRRMEVDKKIKDIF 1804
|
....*
gi 499321815 704 AEKEN 708
Cdd:PTZ00121 1805 DNFAN 1809
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
792-874 |
2.75e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 54.30 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGERialglaFRLAMSLYLAGEISLLILDEPTPYLDEErrrkLITIMERYLKKIP-QVILVSHDEELKDA-ADHVIRI 869
Cdd:COG0488 433 LSGGEK------ARLALAKLLLSPPNVLLLDEPTNHLDIE----TLEALEEALDDFPgTVLLVSHDRYFLDRvATRILEF 502
|
....*
gi 499321815 870 slENG 874
Cdd:COG0488 503 --EDG 505
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
616-861 |
2.95e-07 |
|
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: 53.16 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 616 ELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKKELEKRRDTI 695
Cdd:pfam13304 59 EFEISEFLEDGVRYRYGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 696 KSTLEKLKAEKENRERVKKEIKDLEKAKDFTEELIEKVKKYKALAREAALSKIGELA--SEIFAEFTEGKYSEVVVRAEE 773
Cdd:pfam13304 139 ISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLAdlNLSDLGEGIEKSLLVDDRLRE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 774 NKVRLFVVWEGKERPLTFLSGGERIALGLAFRLamsLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILV 853
Cdd:pfam13304 219 RGLILLENGGGGELPAFELSDGTKRLLALLAAL---LSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILT 295
|
....*...
gi 499321815 854 SHDEELKD 861
Cdd:pfam13304 296 THSPLLLD 303
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
391-638 |
3.34e-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: 53.61 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 391 SPEDIKKLLEELETKKTTIEEERNEITQrigeLKNKIGDLKTAIEELKKAKGKcpvcgreltdehREELLSKYHLDLNNS 470
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAA----LKKEEKALLKQLAALERRIAA------------LARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 471 KNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVNLEKIEKNATEYEKLLEELRTlegRIRGLAED 550
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE---QAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 551 LKKLAPLEKKLAALIHKKQELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKRYLTLLNSKKELE-----ITQREIA 625
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEaliarLEAEAAA 238
|
250
....*....|...
gi 499321815 626 KAKETLEMSFEEL 638
Cdd:COG4942 239 AAERTPAAGFAAL 251
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-79 |
3.75e-07 |
|
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: 52.68 E-value: 3.75e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499321815 3 LERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAIlvGLYWPLRIKDIKKD-EFTKVGARDTYIDLIFEKDG 79
Cdd:cd03242 1 LKSLELRNFRNYAELELEFEPGVTVLVGENAQGKTNLLEAI--SLLATGKSHRTSRDkELIRWGAEEAKISAVLERQG 76
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
727-874 |
3.88e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.53 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 727 EELIEKVKKY-KALAREAALSKIGELASEIFAEFTEGKYSEVVVRAEENKVRLFVVWEGKERPLTFLSGGERIALGLAfR 805
Cdd:COG0488 87 AELRALEAELeELEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRRVALA-R 165
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499321815 806 LamslyLAGEISLLILDEPTPYLDEERRRKLitimERYLKKIPQ-VILVSHDEELKDA-ADHVirISLENG 874
Cdd:COG0488 166 A-----LLSEPDLLLLDEPTNHLDLESIEWL----EEFLKNYPGtVLVVSHDRYFLDRvATRI--LELDRG 225
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
522-753 |
5.81e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 522 KIEKNATEYEKLLEELRTLEGRIRGLAEDL----KKLAPLEKKLAALIHKKQELEKELKELNTKLEsfgfKSVEDLDSKL 597
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELeelnEEYNELQAELEALQAEIDKLQAEIAEAEAEIE----ERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 598 RELeeiYKR-----YLT-LLNSK------KELEITQREIAKAKETLEmsfeelaEVEADIERIEKKLSQLKQKyneeeyk 665
Cdd:COG3883 93 RAL---YRSggsvsYLDvLLGSEsfsdflDRLSALSKIADADADLLE-------ELKADKAELEAKKAELEAK------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 666 kkreekeelekeLARLEAQKKELEKRrdtiKSTLEKLKAEKENR-ERVKKEIKDLEKAKDFTEELIEKVKKYKALAREAA 744
Cdd:COG3883 156 ------------LAELEALKAELEAA----KAELEAQQAEQEALlAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
....*....
gi 499321815 745 LSKIGELAS 753
Cdd:COG3883 220 AAAAAAAAA 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
786-870 |
6.61e-07 |
|
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: 50.94 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 786 ERPLTFLSGGE--RIALGLAfrlamslyLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDeELKDAA 863
Cdd:COG4133 126 DLPVRQLSAGQkrRVALARL--------LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ-PLELAA 196
|
....*..
gi 499321815 864 DHVIRIS 870
Cdd:COG4133 197 ARVLDLG 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
792-869 |
6.84e-07 |
|
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: 50.09 E-value: 6.84e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499321815 792 LSGGERIalglafRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHD-EELKDAADHVIRI 869
Cdd:cd03230 96 LSGGMKQ------RLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHIlEEAERLCDRVAIL 168
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
792-874 |
7.46e-07 |
|
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: 49.91 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGERIALGLAfRlamSLYlaGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKDAADHVirISL 871
Cdd:cd03246 97 LSGGQRQRLGLA-R---ALY--GNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRI--LVL 168
|
...
gi 499321815 872 ENG 874
Cdd:cd03246 169 EDG 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
792-874 |
8.35e-07 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 52.91 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGERIALGLAfRLamslyLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIpQVILVSHDEELKDAADHVIRisL 871
Cdd:COG2274 612 LSGGQRQRLAIA-RA-----LLRNPRILILDEATSALDAETEAIILENLRRLLKGR-TVIIIAHRLSTIRLADRIIV--L 682
|
...
gi 499321815 872 ENG 874
Cdd:COG2274 683 DKG 685
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
3-54 |
8.96e-07 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 46.82 E-value: 8.96e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 499321815 3 LERVTVKNFRSHSDTVVEFKE-GINLIIGQNGSGKSSLLDAILVGLYWPLRIK 54
Cdd:pfam13555 1 LTRLQLINWGTFDGHTIPIDPrGNTLLTGPSGSGKSTLLDAIQTLLVPAKRAR 53
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
363-537 |
9.37e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 52.62 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 363 LEKDHQLYEEIKAKKENLRQLKEKLG-------DKSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIE 435
Cdd:PRK05771 45 LRKLRSLLTKLSEALDKLRSYLPKLNplreekkKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 436 ELKK----------------AKGKCPVCGRELTDEHREELLSKYHLDLNNSKNT----LAKLIDRKSELERELRRIDMEI 495
Cdd:PRK05771 125 RLEPwgnfdldlslllgfkyVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvVVVLKELSDEVEEELKKLGFER 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499321815 496 KRLTPLLTVAEQIRSIEEELNVVN--LEKIEKNATEYEKLLEEL 537
Cdd:PRK05771 205 LELEEEGTPSELIREIKEELEEIEkeRESLLEELKELAKKYLEE 248
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
792-874 |
9.58e-07 |
|
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: 49.69 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGE--RIALGLAfrlamslyLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIpQVILVSHDEELKDAADHVIRi 869
Cdd:cd03228 97 LSGGQrqRIAIARA--------LLRDPPILILDEATSALDPETEALILEALRALAKGK-TVIVIAHRLSTIRDADRIIV- 166
|
....*
gi 499321815 870 sLENG 874
Cdd:cd03228 167 -LDDG 170
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
786-867 |
1.12e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 50.78 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 786 ERPLTFLSGGERialGLAFrLAMSLylAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDeeLKDA--- 862
Cdd:PRK11231 133 DRRLTDLSGGQR---QRAF-LAMVL--AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHD--LNQAsry 204
|
....*
gi 499321815 863 ADHVI 867
Cdd:PRK11231 205 CDHLV 209
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
791-877 |
1.47e-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: 49.23 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 791 FLSGGERIALGLAFRLAMSLYlaGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKDAADHVIRIS 870
Cdd:cd03239 94 ILSGGEKSLSALALIFALQEI--KPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLIGVL 171
|
....*..
gi 499321815 871 LENGSSK 877
Cdd:cd03239 172 FVHGVST 178
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
298-579 |
1.70e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 298 VDAYLALKEFKNEYLDKKYKIEKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAIL--EKDHQLyEEIKA 375
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisRLEQQK-QILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 376 KKENLRQLKEKLGDKSPEDIKKlLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKCpvcgreltDEH 455
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESK-LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL--------EEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 456 REELLSKYH---LDLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEqIRSIEEELNVVNLEkIEKNATEYEK 532
Cdd:TIGR02168 381 LETLRSKVAqleLQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEE-LEELQEELER 458
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 499321815 533 LLEELRTLEGRIRGLAEDLKKLAPLEKKLAALIHKKQELEKELKELN 579
Cdd:TIGR02168 459 LEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFS 505
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
785-867 |
1.70e-06 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 49.84 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 785 KERPLTFLSGGERIALGLAfRLamslyLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHD-EELKDAA 863
Cdd:cd03235 126 ADRQIGELSGGQQQRVLLA-RA-----LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDlGLVLEYF 199
|
....
gi 499321815 864 DHVI 867
Cdd:cd03235 200 DRVL 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
754-867 |
2.51e-06 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 49.68 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 754 EIFAEFTEGKYSEVVVRAEE--NKVRLfvvWEGKERPLTFLSGGERIALGLAfrLAmslyLAGEISLLILDEPTPYLDEE 831
Cdd:COG1131 95 RFFARLYGLPRKEARERIDEllELFGL---TDAADRKVGTLSGGMKQRLGLA--LA----LLHDPELLILDEPTSGLDPE 165
|
90 100 110
....*....|....*....|....*....|....*..
gi 499321815 832 RRRKLITIMERYLKKIPQVILVSHD-EELKDAADHVI 867
Cdd:COG1131 166 ARRELWELLRELAAEGKTVLLSTHYlEEAERLCDRVA 202
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
521-755 |
2.55e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 521 EKIEKNATEYEKLLEELRTLEGRIRGLAEDLKKLaplEKKLAALIHKKQELEKELKELNTKLESFGfKSVEDLDSKLREL 600
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAELE-KEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 601 EEIYKRYLTLLnskkeleitQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKyneeeykkkreeKEELEKELAR 680
Cdd:COG4942 103 KEELAELLRAL---------YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ------------AEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499321815 681 LEAQKKELEKRRDTIKSTLEKLKAEKENRERVKKEIKDLEKAKDFTEELIEKVKKYKALAREAALSKIGELASEI 755
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
1-43 |
2.68e-06 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273173 [Multi-domain] Cd Length: 365 Bit Score: 50.43 E-value: 2.68e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 499321815 1 MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAI 43
Cdd:TIGR00611 1 MYLSRLELTDFRNYDAVDLELSPGVNVIVGPNGQGKTNLLEAI 43
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
233-600 |
2.71e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 233 RKEVLRLEETKVEIENSERLLEKRRGDKRTLEERIKnteEYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEFKNEYL 312
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD---ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 313 DKkykIEKELTRVEELINEIQKRIEELNEKESEKEKLenekkeiLNKLaileKDHQLYEEIKAKKENLRQLKEKLG--DK 390
Cdd:TIGR02169 747 SS---LEQEIENVKSELKELEARIEELEEDLHKLEEA-------LNDL----EARLSHSRIPEIQAELSKLEEEVSriEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 391 SPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKCPVCGRELTDEHR--EELLSKYHLDLN 468
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRdlESRLGDLKKERD 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 469 NSKNTLAKLIDRKSELERELRRIDMEIKRLTPLL-TVAEQIRSIEEELN-----VVNLEKIEKNATEYEKLLEELRTLE- 541
Cdd:TIGR02169 893 ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLeALEEELSEIEDPKGedeeiPEEELSLEDVQAELQRVEEEIRALEp 972
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499321815 542 ---GRIRGLAEDLKKLAPLEKKLAALIHKKQELEKELKELNTKLESFGFKSVEDLDSKLREL 600
Cdd:TIGR02169 973 vnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEI 1034
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
785-875 |
2.86e-06 |
|
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: 49.70 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 785 KERPLTFLSGGERialglafRLAMslyLA----GEISLLILDEPTPYLDEERRRKLITIMERYLKK-IPQVILVSHD-EE 858
Cdd:COG1119 136 ADRPFGTLSQGEQ-------RRVL---IAralvKDPELLILDEPTAGLDLGARELLLALLDKLAAEgAPTLVLVTHHvEE 205
|
90
....*....|....*..
gi 499321815 859 LKDAADHVIRisLENGS 875
Cdd:COG1119 206 IPPGITHVLL--LKDGR 220
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
786-869 |
2.86e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 786 ERPLTFLSGGERIalglafRLAMSLYLAGEIS--LLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKDAA 863
Cdd:PRK00635 471 ERALATLSGGEQE------RTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLA 544
|
....*.
gi 499321815 864 DHVIRI 869
Cdd:PRK00635 545 DRIIDI 550
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
787-874 |
3.05e-06 |
|
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: 49.54 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 787 RPLTFLSGGERIALGLAFRLAM-----SLYlageisllILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKD 861
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSKrstgkTLY--------ILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK 236
|
90
....*....|...
gi 499321815 862 AADHVIRISLENG 874
Cdd:cd03271 237 CADWIIDLGPEGG 249
|
|
| YydB |
COG5293 |
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown]; |
1-439 |
3.34e-06 |
|
Uncharacterized conserved protein YydD, contains DUF2326 domain [Function unknown];
Pssm-ID: 444096 [Multi-domain] Cd Length: 572 Bit Score: 50.72 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 1 MKLERVTVKNFRSHSdtvVEFKEGINLIIGQ-----------NGSGKSSLLDAILVGLywpLRIKDIKKDEFTKVGARDT 69
Cdd:COG5293 1 MMLKKLYSNLPRFKP---IEFNPGLNVILGEisspendkdstNGVGKSTLLELIDFCL---GADKDKKRFLKHEDELGDH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 70 YIDLIFEKDGTKYRITRRFlkgysSGEIHAMKRLVGNEWKHVTEPSSKAISAFMEKLIPYNIF-------LNAIYIR--Q 140
Cdd:COG5293 75 TFFLEFELDGKDLTIRRSV-----SDPKKISLCGDGYEWDHEKVSLEEAKALLEELLFGLPALkgpsfrsLLGYFLRrqG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 141 GQIDAILESDEAREKVVREVLNLDKFETAYKKLSELKKTINNRIKEYRDILARTE-----NIEELIKENEQELIQVLQEI 215
Cdd:COG5293 150 DDFKDPLQLFSTAQKDADWKLYLAYLLGLDWDLAAEKYELKEEIKELKKLRKALKdeligSVVKSISELRAEILELEEEI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 216 SKIEEVLPSKR--SKVDMLRKEVLRLEETKVEIENSERLLEKRRgdkrtleERIKNTEEYLEKLKEKEKELEEQVKEIT- 292
Cdd:COG5293 230 EKLEKDLEKFDvaENYEELEKELDELKREINELRNERYSLERRL-------KKIERSLEEEIDIDPDELEKLYEEAGVFf 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 293 --SIKKDVDA----YLALKEFKNEYLdkkykiEKELTRVEELINEIQKRIEELNEKESEkeklenekkeilnKLAILeKD 366
Cdd:COG5293 303 pdQVKKRFEEveafHKSIVENRREYL------EEEIAELEAELEELEAELAELGKERAE-------------LLSLL-DS 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499321815 367 HQLYEEIKAKKENLRQLKEKLGdkSPEDIKKLLEELETKKTTIEEERNEITQRIgelKNKIGDLKTAIEELKK 439
Cdd:COG5293 363 KGALDKYKELQEELAELEAELE--ELESRLEKLQELEDEIRELKEERAELKEEI---ESDIEERKELLDEINK 430
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
785-859 |
4.18e-06 |
|
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: 48.19 E-value: 4.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499321815 785 KERPLTFLSGGERIALGLAFRLAMslylagEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEEL 859
Cdd:TIGR01166 121 RERPTHCLSGGEKKRVAIAGAVAM------RPDVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDL 189
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
164-775 |
5.42e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 164 DKFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEqelIQVLQEISKIEEVlpskRSKVDMLRKEVLRLEETK 243
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEE---ARKAEDARKAEEA----RKAEDAKRVEIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 244 VEIENSERLLEKRRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEFKNEYLDKKYKIEKELT 323
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 324 RVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKdhqlyEEIKAKKENLRQLKEKlgdKSPEDIKKLLEEle 403
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK-----AEEKKKADEAKKAEEK---KKADEAKKKAEE-- 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 404 tkkttiEEERNEITQRIGELKNKIGDLKTAIEELKKAKgkcpvcgrelTDEHREELLSKYHLDLNNSKNTLAKLidRKSE 483
Cdd:PTZ00121 1314 ------AKKADEAKKKAEEAKKKADAAKKKAEEAKKAA----------EAAKAEAEAAADEAEAAEEKAEAAEK--KKEE 1375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 484 lerelrridmEIKRLTPLLTVAEQIRSIEEelnvvnlekIEKNATEYEKLLEELRTLEGRiRGLAEDLKKLAPlEKKLAA 563
Cdd:PTZ00121 1376 ----------AKKKADAAKKKAEEKKKADE---------AKKKAEEDKKKADELKKAAAA-KKKADEAKKKAE-EKKKAD 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 564 LIHKKQELEKELKELNTKLESFgfKSVEDLDSKLREleeiyKRYLTLLNSKKELEITQREIAKAKETLEMSFEELAEVEA 643
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEA--KKAEEAKKKAEE-----AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 644 DieriEKKLSQLKQkyneEEYKKKREEKEELEKELARLEAQKKELEKRRDTIKSTLEKLKAEKENR-ERVKKEIKDLEKA 722
Cdd:PTZ00121 1508 A----KKKADEAKK----AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaEEAKKAEEDKNMA 1579
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 499321815 723 KDFTEELIEKVKKYKALAREAALSKIGELASEIFAEFTEGKYSEVVVRAEENK 775
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
786-869 |
6.10e-06 |
|
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: 48.41 E-value: 6.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 786 ERPLTFLSGGE--RIALglAFRLAMSLylageISLL-ILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKDA 862
Cdd:cd03270 132 SRSAPTLSGGEaqRIRL--ATQIGSGL-----TGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA 204
|
....*..
gi 499321815 863 ADHVIRI 869
Cdd:cd03270 205 ADHVIDI 211
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-146 |
6.28e-06 |
|
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: 48.34 E-value: 6.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 3 LERVTVKNFRSHSDT-VVEFKEGINLIIGQNGSGKSSLLDAILVGL---YWPLRIKDIK----KDEFTKVGARDTYIDLI 74
Cdd:cd03275 1 LKRLELENFKSYKGRhVIGPFDRFTCIIGPNGSGKSNLMDAISFVLgekSSHLRSKNLKdliyRARVGKPDSNSAYVTAV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499321815 75 FEKDGTKYR-ITRRFLKGYSSGEIHamKRLVgnewkhvtepSSKAISAFMEKLipyNIFLNA--IYIRQGQIDAI 146
Cdd:cd03275 81 YEDDDGEEKtFRRIITGGSSSYRIN--GKVV----------SLKEYNEELEKI---NILVKArnFLVFQGDVESI 140
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
189-734 |
8.05e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.73 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 189 DILARTENIEELIKENEQELIQVLQEISKI-EEVLPSKRSKVDMLRKEVLRLEETKVEIENSERLLEKRRGdKRTLEERI 267
Cdd:pfam15921 131 DIRRRESQSQEDLRNQLQNTVHELEAAKCLkEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASG-KKIYEHDS 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 268 KNTEEYLEKLKEKEKELEEQVKEITSIKKDV-DAYLALKEFKNEYLDK-KYKIEKELTRVEELINEIQKRIEELNEKESE 345
Cdd:pfam15921 210 MSTMHFRSLGSAISKILRELDTEISYLKGRIfPVEDQLEALKSESQNKiELLLQQHQDRIEQLISEHEVEITGLTEKASS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 346 KEKLENEkkeILNKLAILEKdhqlyeeiKAKKEN---LRQLKEKlgdksPEDIKKLLEELETKKTTIEEERNEITQRIGE 422
Cdd:pfam15921 290 ARSQANS---IQSQLEIIQE--------QARNQNsmyMRQLSDL-----ESTVSQLRSELREAKRMYEDKIEELEKQLVL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 423 LKNKIGDLKTAIEELKKAKGKcpvcgrelTDEHREELLSKYHL---DLNNSKNTLAKLIDRKS-------ELERELRRID 492
Cdd:pfam15921 354 ANSELTEARTERDQFSQESGN--------LDDQLQKLLADLHKrekELSLEKEQNKRLWDRDTgnsitidHLRRELDDRN 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 493 MEIKRLTPLLTV--AEQIRSIEEELNVV-----NLEKIEKNATEYEKLLEELRTLegrIRGLAEDLKKLAPLEKKLAALI 565
Cdd:pfam15921 426 MEVQRLEALLKAmkSECQGQMERQMAAIqgkneSLEKVSSLTAQLESTKEMLRKV---VEELTAKKMTLESSERTVSDLT 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 566 HKKQELEKELKELNTKLEsfgfKSVEDLDSKLRELEEIYKRYLTLLNSKKELEITQREIA---KAKETLEMSFEELAEVE 642
Cdd:pfam15921 503 ASLQEKERAIEATNAEIT----KLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAekdKVIEILRQQIENMTQLV 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 643 ADIER----IEKKLSQLKQKYNEEEYKKKREEKEELEKelarlEAQKKELEKRRDTIKstLEKLKAEKENRERVKKeIKD 718
Cdd:pfam15921 579 GQHGRtagaMQVEKAQLEKEINDRRLELQEFKILKDKK-----DAKIRELEARVSDLE--LEKVKLVNAGSERLRA-VKD 650
|
570
....*....|....*.
gi 499321815 719 LEKAKDfteELIEKVK 734
Cdd:pfam15921 651 IKQERD---QLLNEVK 663
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
792-874 |
8.06e-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: 47.18 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGERIALGLAFRLAMslylagEISLLILDEPTPYLDEERRRKlitiMERYLKKIPQ-----VILVSHD-EELKDAADH 865
Cdd:cd03229 101 LSGGQQQRVALARALAM------DPDVLLLDEPTSALDPITRRE----VRALLKSLQAqlgitVVLVTHDlDEAARLADR 170
|
....*....
gi 499321815 866 VIRisLENG 874
Cdd:cd03229 171 VVV--LRDG 177
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
785-867 |
8.42e-06 |
|
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: 48.12 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 785 KERPLTFLSGGER-IALglafrLAMSlyLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQ-VILVSHDeeLKDA 862
Cdd:COG1120 131 ADRPVDELSGGERqRVL-----IARA--LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRtVVMVLHD--LNLA 201
|
....*...
gi 499321815 863 A---DHVI 867
Cdd:COG1120 202 AryaDRLV 209
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
367-612 |
8.77e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.24 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 367 HQLYEEIKAK-KENLRQLKEKLGD--KSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKK---- 439
Cdd:PHA02562 201 NKNIEEQRKKnGENIARKQNKYDElvEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikm 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 440 --AKGKCPVCGRELTDEhrEELLSKYHLDLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSieeelnv 517
Cdd:PHA02562 281 yeKGGVCPTCTQQISEG--PDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQ------- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 518 vNLEKIEKNATEYEKLLEELRTlegrirGLAEDLKKLAPLEKKLAALIHKKQELEKELKELNTK---LESFGFKSVedld 594
Cdd:PHA02562 352 -SLITLVDKAKKVKAAIEELQA------EFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVtdlLKDSGIKAS---- 420
|
250
....*....|....*...
gi 499321815 595 sklreleeIYKRYLTLLN 612
Cdd:PHA02562 421 --------IIKKYIPYFN 430
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-778 |
9.70e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 2 KLERVTVKNFRSHSD-TVVEFKEGINLIIGQNGSGKSSLLDAILvglyWPL---RIKDIKKDEFTKV---------GARD 68
Cdd:TIGR02168 1 RLKKLELAGFKSFADpTTINFDKGITGIVGPNGCGKSNIVDAIR----WVLgeqSAKALRGGKMEDVifngsetrkPLSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 69 TYIDLIFE--------KDGTKYRITRRFLK-GYSSGEIHAMK-RLvgnewKHVTE--------PSSKAIsafmeklipyn 130
Cdd:TIGR02168 77 AEVELVFDnsdgllpgADYSEISITRRLYRdGESEYFINGQPcRL-----KDIQDlfldtglgKRSYSI----------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 131 iflnaiyIRQGQIDAILES----------------------DEAREKVVREVLNLDKFETAykkLSELKKTINN------ 182
Cdd:TIGR02168 141 -------IEQGKISEIIEAkpeerraifeeaagiskykerrKETERKLERTRENLDRLEDI---LNELERQLKSlerqae 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 183 ---RIKEYRD---------ILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVLRLEETKVEIEnsE 250
Cdd:TIGR02168 211 kaeRYKELKAelrelelalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ--K 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 251 RLLEKrRGDKRTLEERIKNTEEYLEKLKekekeleeqvkeiTSIKKDVDAYLALKEFKNEYLDKKYKIEKELTRVEELIN 330
Cdd:TIGR02168 289 ELYAL-ANEISRLEQQKQILRERLANLE-------------RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 331 EIQKRIEELNEKESEKEKLENEKKEILNKLAilEKDHQLYEEIKAKKENLRQLKEKLGDkSPEDIKKLLEELETKKTTIE 410
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLR--SKVAQLELQIASLNNEIERLEARLER-LEDRRERLQQEIEELLKKLE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 411 E-ERNEITQRIGELKNKIGDLKTAIEELKKAKGKCpvcgRELTDEHREELLS--KYHLDLNNSKNTLAKLIDRKSELERE 487
Cdd:TIGR02168 432 EaELKELQAELEELEEELEELQEELERLEEALEEL----REELEEAEQALDAaeRELAQLQARLDSLERLQENLEGFSEG 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 488 LRRIDMEIKRLTPLLTVAEQIRSIEEE----LNVV---NLEKIE-KNATEYEKLLEELR-TLEGRIRGLAEDLKKLAPLE 558
Cdd:TIGR02168 508 VKALLKNQSGLSGILGVLSELISVDEGyeaaIEAAlggRLQAVVvENLNAAKKAIAFLKqNELGRVTFLPLDSIKGTEIQ 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 559 KKLAALIHKKQELEKELKELNTKLESF---------GFKSVEDLDSKLRELEEIYKRY---------------------- 607
Cdd:TIGR02168 588 GNDREILKNIEGFLGVAKDLVKFDPKLrkalsyllgGVLVVDDLDNALELAKKLRPGYrivtldgdlvrpggvitggsak 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 608 --LTLLNSKKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKyneeeYKKKREEKEELEKELARLEAQK 685
Cdd:TIGR02168 668 tnSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE-----LEELSRQISALRKDLARLEAEV 742
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 686 KELEKRRDTIKSTLEKLKAEKE-NRERVKKEIKDLEKAKDFTEELIEKVKKYKAlAREAALSKIGELASEIFAefTEGKY 764
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEeLEERLEEAEEELAEAEAEIEELEAQIEQLKE-ELKALREALDELRAELTL--LNEEA 819
|
890
....*....|....
gi 499321815 765 SEVVVRAEENKVRL 778
Cdd:TIGR02168 820 ANLRERLESLERRI 833
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
786-869 |
1.11e-05 |
|
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: 49.24 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 786 ERPLTFLSGGE----RIALGLAFRLAMSLYlageisllILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKD 861
Cdd:TIGR00630 483 SRAAGTLSGGEaqriRLATQIGSGLTGVLY--------VLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIR 554
|
....*...
gi 499321815 862 AADHVIRI 869
Cdd:TIGR00630 555 AADYVIDI 562
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2-86 |
1.18e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 2 KLERVTVKNFRSHSDTVVEF---KEGINLIIGQNGSGKSSLLDAILVGLYW-PLRikDIKKDEF-TKVGARDTYIDLIFE 76
Cdd:PHA02562 3 KFKKIRYKNILSVGNQPIEIqldKVKKTLITGKNGAGKSTMLEALTFALFGkPFR--DIKKGQLiNSINKKDLLVELWFE 80
|
90
....*....|
gi 499321815 77 KDGTKYRITR 86
Cdd:PHA02562 81 YGEKEYYIKR 90
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-75 |
1.40e-05 |
|
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: 46.20 E-value: 1.40e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499321815 5 RVTVKNFRSH-SDTVVEFKEG-INLIIGQNGSGKSSLLDAILVGLYwpLRIKDIKKDEFTKVGARDTYIDLIF 75
Cdd:cd03227 1 KIVLGRFPSYfVPNDVTFGEGsLTIITGPNGSGKSTILDAIGLALG--GAQSATRRRSGVKAGCIVAAVSAEL 71
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
780-867 |
1.71e-05 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 45.88 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 780 VVWEGKerPLTFLSGGERIALGLAF----------RLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQ 849
Cdd:cd03216 57 ILVDGK--EVSFASPRDARRAGIAMvyqlsvgerqMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVA 134
|
90
....*....|....*....
gi 499321815 850 VILVSHD-EELKDAADHVI 867
Cdd:cd03216 135 VIFISHRlDEVFEIADRVT 153
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
368-589 |
1.74e-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: 47.84 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 368 QLYEEIKAKKENLRQLKEKLGD--KSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKCP 445
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKAllKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 446 VCGRELTDEHREELL--SKYHLDLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVNLEKI 523
Cdd:COG4942 111 RALYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499321815 524 EKNATEYEKLLEELRTlegRIRGLAEDLKKLAPLEKKLAALIhkkQELEKELKELNTKLESFGFKS 589
Cdd:COG4942 191 EALKAERQKLLARLEK---ELAELAAELAELQQEAEELEALI---ARLEAEAAAAAERTPAAGFAA 250
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
300-721 |
1.77e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 300 AYLALKEFKNEYLDKKYKIEKELTRVEELINEIQKRIEELNEKESEkeklenekkeILNKLAILEKDHQ----------- 368
Cdd:PRK04863 273 DYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAE----------LNEAESDLEQDYQaasdhlnlvqt 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 369 ---LYEEIKAKKENLRQLKEKLGDKSP--EDIKKLLEELETKKTTIEEErneitqrIGELKNKIGDLKTAIEELKKAKGK 443
Cdd:PRK04863 343 alrQQEKIERYQADLEELEERLEEQNEvvEEADEQQEENEARAEAAEEE-------VDELKSQLADYQQALDVQQTRAIQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 444 CPVCGRELtdEHREELLSKYHLDLNNSKNTLAKLIDRKSELERELRriDMEIKrltplLTVAEQIRSIeeelnvvnleki 523
Cdd:PRK04863 416 YQQAVQAL--ERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELL--SLEQK-----LSVAQAAHSQ------------ 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 524 eknateYEKLLEELRTLEGRI---------RGLAEDLKKLAPLEKKLAALIHKKQELEKELKELNTklesfgfksVEdld 594
Cdd:PRK04863 475 ------FEQAYQLVRKIAGEVsrseawdvaRELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQR---------AE--- 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 595 sklRELEEIYKRYLTLLNSKKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYneeeyKKKREEKEEL 674
Cdd:PRK04863 537 ---RLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRL-----AARAPAWLAA 608
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 499321815 675 EKELARLEAQKKE-LEKRRD---TIKSTLEKLKAEKENRERVKKEIKDLEK 721
Cdd:PRK04863 609 QDALARLREQSGEeFEDSQDvteYMQQLLERERELTVERDELAARKQALDE 659
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
759-877 |
2.26e-05 |
|
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: 46.48 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 759 FTEGKYSEVVVRAE---------ENKVRLFVVWEGKER-PLTfLSGGERIalglafRLAMSLYLAGEISLLILDEPTPYL 828
Cdd:cd03226 85 FTDSVREELLLGLKeldagneqaETVLKDLDLYALKERhPLS-LSGGQKQ------RLAIAAALLSGKDLLIFDEPTSGL 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 499321815 829 DEERRRKLITIMERYLKKIPQVILVSHDEE-LKDAADHVIRisLENGSSK 877
Cdd:cd03226 158 DYKNMERVGELIRELAAQGKAVIVITHDYEfLAKVCDRVLL--LANGAIV 205
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
127-775 |
2.40e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.50 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 127 IPYNIFLNAIYIRQGQIDAILESDEAREKVVREVLNLDKFETAYKKLSELKKTINNRIKEY-----------------RD 189
Cdd:TIGR00606 145 VSKAVLNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHqmelkylkqykekaceiRD 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 190 ILARTENIE----ELIKENEQELIQVLQEISKIEEvlpsKRSKVDMLRKEVLRLEETKVEIENSERLLEKRRGDK-RTLE 264
Cdd:TIGR00606 225 QITSKEAQLessrEIVKSYENELDPLKNRLKEIEH----NLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfQGTD 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 265 ERIKNTEEYLEKLKEKEKELEEQVKEitSIKKDVDAYLALKEFKNEYLDKKYKIEKELTRVEELINEIQKRIEELNEKES 344
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQR--ELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 345 EKEKLENEKKEILNKLAILEKDHQLYEEIKAKKENLRQLKEKLGDKSpEDIKKLLEELETKKTTIEEERNEITQRIGELK 424
Cdd:TIGR00606 379 LDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ-EQADEIRDEKKGLGRTIELKKEILEKKQEELK 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 425 NKIGDLKTAIEELKKAKGKcpvcGRELTDEHREELLSKYHLDLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTV 504
Cdd:TIGR00606 458 FVIKELQQLEGSSDRILEL----DQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTT 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 505 AEQIRSIEEElNVVNLEKIEKNATEYEKLLEEL-------RTLEGRIRGLAEDLK----KLAPLEKKLAALIHKKQELEK 573
Cdd:TIGR00606 534 RTQMEMLTKD-KMDKDEQIRKIKSRHSDELTSLlgyfpnkKQLEDWLHSKSKEINqtrdRLAKLNKELASLEQNKNHINN 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 574 ELKELNTKLESFGFK-----SVEDLDSKLRELEE-----------------IYKRYLTLLNSKKE--LEITQREIAKAKE 629
Cdd:TIGR00606 613 ELESKEEQLSSYEDKlfdvcGSQDEESDLERLKEeieksskqramlagataVYSQFITQLTDENQscCPVCQRVFQTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 630 TLEMSFEELAEVEADIERIEKKLSQLKQKynEEEYKKKREEKEELEKELARLEAQKKELEKRRDTIKSTLEKLKAEKENR 709
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLKSTESELKKK--EKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499321815 710 ERVKKEIK-DLEKAKD----------FTEELIEKVKKYKALAREAALSKIGELASEIFAEFTEG--KYSEVVVRAEENK 775
Cdd:TIGR00606 771 ETLLGTIMpEEESAKVcltdvtimerFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKqhELDTVVSKIELNR 849
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
788-877 |
2.40e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.56 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 788 PLTfLSGGE--RIALGLAfrlamslyLAGEISLLILDEPTPYLDEERRRKLITIMERYLK--KIPqVILVSHD-EELKDA 862
Cdd:PRK11144 126 PGS-LSGGEkqRVAIGRA--------LLTAPELLLMDEPLASLDLPRKRELLPYLERLAReiNIP-ILYVSHSlDEILRL 195
|
90
....*....|....*
gi 499321815 863 ADHVirISLENGSSK 877
Cdd:PRK11144 196 ADRV--VVLEQGKVK 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
765-869 |
2.61e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 47.04 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 765 SEVVVRAEEnKVRLFVVWEGKERPLTFLSGGERIALGLAFRLAMslylagEISLLILDEPTPYLDEERRRKLITIMERYL 844
Cdd:PRK13647 113 DEVERRVEE-ALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM------DPDVIVLDEPMAYLDPRGQETLMEILDRLH 185
|
90 100
....*....|....*....|....*.
gi 499321815 845 KKIPQVILVSHDEELK-DAADHVIRI 869
Cdd:PRK13647 186 NQGKTVIVATHDVDLAaEWADQVIVL 211
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
787-881 |
2.93e-05 |
|
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: 48.09 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 787 RPLTFLSGGErialglafrlAMSLYLAGEIS-------LLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEEL 859
Cdd:TIGR00630 825 QPATTLSGGE----------AQRIKLAKELSkrstgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDV 894
|
90 100
....*....|....*....|..
gi 499321815 860 KDAADHVIRISLENGSSKVEVV 881
Cdd:TIGR00630 895 IKTADYIIDLGPEGGDGGGTVV 916
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
368-583 |
3.16e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 368 QLYEEIKAKKENLRQLKEKLGDKSPEDIKKL----LEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELkkakgk 443
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKNGLVDLSEEAKLllqqLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL------ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 444 cpvcgreltdehreellskyhldlnNSKNTLAKLIDRKSELERELRRIDmeiKRLTP----LLTVAEQIRSIEEELNVVN 519
Cdd:COG3206 260 -------------------------LQSPVIQQLRAQLAELEAELAELS---ARYTPnhpdVIALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499321815 520 LEKIEKNATEYEKLLEELRTLEGRIRGLAEDLKKLAPLEKKLAALIHKKQELEKELKELNTKLE 583
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
785-867 |
3.92e-05 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 45.12 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 785 KERPLTFLSGGER-IALglafrLAMSLylAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQ-VILVSHDEELkdA 862
Cdd:cd03214 91 ADRPFNELSGGERqRVL-----LARAL--AQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKtVVMVLHDLNL--A 161
|
....*...
gi 499321815 863 ---ADHVI 867
Cdd:cd03214 162 aryADRVI 169
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
787-874 |
4.09e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 787 RPLTFLSGGERIALGLAFRLamsLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKDAADHV 866
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYEL---LAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
|
....*...
gi 499321815 867 IRISLENG 874
Cdd:PRK00635 882 LELGPEGG 889
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
791-867 |
5.51e-05 |
|
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: 45.27 E-value: 5.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499321815 791 FLSGGERIALGLAfRLamslyLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIpQVILVSHDEELKDAADHVI 867
Cdd:cd03245 140 GLSGGQRQAVALA-RA-----LLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK-TLIIITHRPSLLDLVDRII 209
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
786-867 |
5.52e-05 |
|
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: 45.48 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 786 ERPLTFLSGGERIalglafRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERY-LKKIPQVILVSHDEELKD-AA 863
Cdd:cd03237 110 DREVPELSGGELQ------RVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaENNEKTAFVVEHDIIMIDyLA 183
|
....
gi 499321815 864 DHVI 867
Cdd:cd03237 184 DRLI 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
389-646 |
7.51e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 389 DKSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKgkcpvcgreltDEHREELlskyhldln 468
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI-----------DKLQAEI--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 469 nsKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQiRSIEEELN-VVNLEKIEKNATEyekLLEELRTLEGRIRgl 547
Cdd:COG3883 75 --AEAEAEIEERREELGERARALYRSGGSVSYLDVLLGS-ESFSDFLDrLSALSKIADADAD---LLEELKADKAELE-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 548 aedlKKLAPLEKKLAALIHKKQELEKELKELNTKLESFGfKSVEDLDSKLRELEEIYKRYLTLLNSKKELEITQREIAKA 627
Cdd:COG3883 147 ----AKKAELEAKLAELEALKAELEAAKAELEAQQAEQE-ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
250
....*....|....*....
gi 499321815 628 KETLEMSFEELAEVEADIE 646
Cdd:COG3883 222 AAAAAAAAAAAAAAAAAAA 240
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
792-867 |
7.88e-05 |
|
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: 46.05 E-value: 7.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499321815 792 LSGGERIalglafRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQ-VILVSHD-EELKDAADHVI 867
Cdd:COG1123 143 LSGGQRQ------RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTtVLLITHDlGVVAEIADRVV 214
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
199-440 |
1.32e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 199 ELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVLRLEEtkvEIENSERLLEKRRGDKRTLEERIKNTEEYLEKLK 278
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER---RIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 279 EkekeleeqvkeitsikkdvdaylalkefkneyldkkyKIEKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILN 358
Cdd:COG4942 97 A-------------------------------------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 359 KL-AILEKDHQLYEEIKAKKENLRQLKEKLGDKSpEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEEL 437
Cdd:COG4942 140 YLkYLAPARREQAEELRADLAELAALRAELEAER-AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
...
gi 499321815 438 KKA 440
Cdd:COG4942 219 QQE 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
783-874 |
2.08e-04 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 43.55 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 783 EGKERPLTF-LSGGE--RIALGLAfrlamslyLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEEL 859
Cdd:cd03292 127 SHKHRALPAeLSGGEqqRVAIARA--------IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKEL 198
|
90
....*....|....*
gi 499321815 860 KDAADHViRISLENG 874
Cdd:cd03292 199 VDTTRHR-VIALERG 212
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
25-243 |
2.68e-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: 43.92 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 25 INLIIGQNGSGKSSLLDAILVGLYWPLRIKDIKKDEFTKVGARD--TYIDLIFEKDGTKYRITRRFLKGYSSGEIHAMKR 102
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGipSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 103 LVGNEWKHVTEPSSKAISAFMEKLIPYNIFLNAIYIRQGQI------DAILESDEAREKVVREVLNLDKFETAYKKLSEL 176
Cdd:pfam13304 81 EDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGldveerIELSLSELSDLISGLLLLSIISPLSFLLLLDEG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499321815 177 KKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVLRLEETK 243
Cdd:pfam13304 161 LLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENG 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
785-859 |
3.49e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 43.46 E-value: 3.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499321815 785 KERPLTFLSGGERIalglafRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEEL 859
Cdd:PRK13638 130 RHQPIQCLSHGQKK------RVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL 198
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2-780 |
3.73e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.58 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 2 KLERVTVKNFRSHSDTVV-EFKEGINLIIGQNGSGKSSLLDAILVGL----YWPLRIKDIKKDEFTKVGAR--------- 67
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVIlPFSPGFTAIVGPNGSGKSNILDAILFVLgersAKSLRSERLSDLIHSKSGAFvnsaeveit 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 68 DTYIDLIFEKDGTKYRITRRFLKGYSSgEIHAMKRLVgnewkhvtepSSKAISAFMEKLipyNIFLNA--IYIRQGQIDA 145
Cdd:pfam02463 81 FDNEDHELPIDKEEVSIRRRVYRGGDS-EYYINGKNV----------TKKEVAELLESQ---GISPEAynFLVQGGKIEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 146 ILESDEAREKVVREVLNLDKFETAYKKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSK 225
Cdd:pfam02463 147 IAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 226 RSKVDM-LRKEVLRLEETKVEIENSERLLEKRRGDK------RTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDV 298
Cdd:pfam02463 227 LYLDYLkLNEERIDLLQELLRDEQEEIESSKQEIEKeeeklaQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 299 DAYLALKEFKNEYLDKKYKIEKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKDHQLY-------- 370
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKkkleserl 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 371 ---EEIKAKKENLRQLKEKLGDKSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKcpvc 447
Cdd:pfam02463 387 ssaAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK---- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 448 gRELTDEHREELLSKYHLDLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVNLEKIEKNA 527
Cdd:pfam02463 463 -DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 528 tEYEKLLEELRTLEGRIRGLAEDLKKLAPLEKKLAALIHKKQELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKRY 607
Cdd:pfam02463 542 -KVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDK 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 608 LTLLNSKKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKKE 687
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 688 LEKRRDTIKSTLEKLKAEKENRERVKKEIKdLEKAKDFTEELIEKVKKYKALAREAALSKIGELASEIFAEFTEGKYSEV 767
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEA-QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE 779
|
810
....*....|...
gi 499321815 768 VVRAEENKVRLFV 780
Cdd:pfam02463 780 REKTEKLKVEEEK 792
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
788-856 |
4.18e-04 |
|
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: 43.77 E-value: 4.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499321815 788 PLTFLSGGE--RIALGlafRLAMSlylagEISLLILDEPTPYLDEERrrklITIMERYLKKIP-QVILVSHD 856
Cdd:TIGR03719 158 DVTKLSGGErrRVALC---RLLLS-----KPDMLLLDEPTNHLDAES----VAWLERHLQEYPgTVVAVTHD 217
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
476-755 |
4.19e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 476 KLIDRKS---ELERELRRIDMEIKRLTPLLtvaEQIRSIEEELNVvNLEKIEK---NATEYEKLLEELRTLEG--RIRGL 547
Cdd:TIGR02169 157 KIIDEIAgvaEFDRKKEKALEELEEVEENI---ERLDLIIDEKRQ-QLERLRRereKAERYQALLKEKREYEGyeLLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 548 AEDLKKLAPLEKKLAALIHKKQELEKELKELNTKLESFGfKSVEDLDSKLREL--EEIYKRYLTLLNSKKELEITQREIA 625
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLgeEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 626 KAKETLEMSFEELAEVEADIERIEKKLSQlkqkyneeeykkkreekeeLEKELARLEAQK-------KELEKRRDTIKST 698
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEE-------------------LEREIEEERKRRdklteeyAELKEELEDLRAE 372
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 499321815 699 LEKLKAE-KENRERVKKEIKDLEKAKDFTEELIEKVKKYKALAREAAlSKIGELASEI 755
Cdd:TIGR02169 373 LEEVDKEfAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS-EELADLNAAI 429
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
5-43 |
4.23e-04 |
|
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: 43.02 E-value: 4.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 499321815 5 RVTVKNFRSHSD-TVVE-FKEGINLIIGQNGSGKSSLLDAI 43
Cdd:cd03272 3 QVIIQGFKSYKDqTVIEpFSPKHNVVVGRNGSGKSNFFAAI 43
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
3-97 |
5.28e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 43.03 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 3 LERVTVKNFRSHSDTVVEFKeGINLIIGQNGSGKSSLLDAILvGLYW------------PLRIKDIKKDEFTKVGARDTY 70
Cdd:COG4938 1 IKSISIKNFGPFKEAELELK-PLTLLIGPNGSGKSTLIQALL-LLLQsnfiylpaersgPARLYPSLVRELSDLGSRGEY 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 499321815 71 ----------IDLIFEKDGTKYRITRRFLKGYSSGEI 97
Cdd:COG4938 79 tadflaelenLEILDDKSKELLEQVEEWLEKIFPGKV 115
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
741-882 |
5.43e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.38 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 741 REAALSKIGELASEIFAEFTEgkysEVVVRAEENKVRLFVVWEGKERPLT--FLSGGERIALGLAfrlaMSLYLAGEISL 818
Cdd:COG4637 210 HPERFERILEALRDAFPGFED----IEVEPDEDGRVLLEFREKGLDRPFParELSDGTLRFLALL----AALLSPRPPPL 281
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499321815 819 LILDEPTPYLDEERRRKLITIMERYLKKIpQVILVSHDEELKDA--ADHVIRISLEN-GSSKVEVVS 882
Cdd:COG4637 282 LCIEEPENGLHPDLLPALAELLREASERT-QVIVTTHSPALLDAlePEEVLVLEREDdGETRIRRLS 347
|
|
| recF |
PRK14079 |
recombination protein F; Provisional |
1-91 |
5.79e-04 |
|
recombination protein F; Provisional
Pssm-ID: 184491 [Multi-domain] Cd Length: 349 Bit Score: 43.23 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 1 MKLERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAILVGLYWPLRIKDIkkDEFTKVGARDTYIDLIFEKDGT 80
Cdd:PRK14079 1 MRLLSLRQLNYRNLAPPTLAFPPGVTAVVGENAAGKTNLLEAIYLALTGELPNGRL--ADLVRFGEGEAWVHAEVETGGG 78
|
90
....*....|.
gi 499321815 81 KYRITRRFLKG 91
Cdd:PRK14079 79 LSRLEVGLGPG 89
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
389-660 |
6.12e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 389 DKSPEDIKKLLEEL---------ETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGkcpvcgreltdehreel 459
Cdd:COG3206 144 SPDPELAAAVANALaeayleqnlELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG----------------- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 460 lskyhldLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTplltvaEQIRSIEEELNVVNLEKIE-KNATEYEKLLEELR 538
Cdd:COG3206 207 -------LVDLSEEAKLLLQQLSELESQLAEARAELAEAE------ARLAALRAQLGSGPDALPElLQSPVIQQLRAQLA 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 539 TLEGRIRGLAEDLKKLAP----LEKKLAALihkKQELEKELKELNTKLESfgfkSVEDLDSKLRELEEIYKRYLTLLNSK 614
Cdd:COG3206 274 ELEAELAELSARYTPNHPdviaLRAQIAAL---RAQLQQEAQRILASLEA----ELEALQAREASLQAQLAQLEARLAEL 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499321815 615 KELEItqreiakaketlemsfeELAEVEADIERIEKKLSQLKQKYN 660
Cdd:COG3206 347 PELEA-----------------ELRRLEREVEVARELYESLLQRLE 375
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
363-710 |
8.23e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 363 LEKDHQLYEEIKAKKENLRQLKEKLGDK------SPEDIKKLLEELETKKTTIEEERNEITQ---RIGELKNKIGDLKTA 433
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTAKkmtlesSERTVSDLTASLQEKERAIEATNAEITKlrsRVDLKLQELQHLKNE 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 434 IEELKKAKGKCPVCGRELTDEH------REELLSKYHLDLNNSKNTLAKLIDrKSELERELRRIDMEIKRLTPLLTVAE- 506
Cdd:pfam15921 540 GDHLRNVQTECEALKLQMAEKDkvieilRQQIENMTQLVGQHGRTAGAMQVE-KAQLEKEINDRRLELQEFKILKDKKDa 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 507 QIRSIEEELNVVNLEKIE-KNA------------TEYEKLLEELRTLEGRIRGLAEDLKKLAplekklAALIHKKQELEK 573
Cdd:pfam15921 619 KIRELEARVSDLELEKVKlVNAgserlravkdikQERDQLLNEVKTSRNELNSLSEDYEVLK------RNFRNKSEEMET 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 574 ELKELNTKLESfGFKSVEDLDSKLRELEEIYKRYLTL-LNSKKELEITQREIakakETLEMSFEELAEVEADIERIEKKL 652
Cdd:pfam15921 693 TTNKLKMQLKS-AQSELEQTRNTLKSMEGSDGHAMKVaMGMQKQITAKRGQI----DALQSKIQFLEEAMTNANKEKHFL 767
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 499321815 653 SQLKQKyneeeykkkreekeeLEKELARLEAQKKELEKRRDTIKSTLEKLKAEKENRE 710
Cdd:pfam15921 768 KEEKNK---------------LSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
457-723 |
8.74e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 457 EELLSKYHLDLNNSKNTLAKLIDRKSELERELRRIDMeikrltplltVAEQIrsieEELNVVNLEkieknATEYEKLLEE 536
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEAERARELDL----------LRFQL----EELEAAALQ-----PGEEEELEEE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 537 LRTLEGrirglAEDLKKLapLEKKLAALIHKKQELEKELKELNTKLESfgfksVEDLDSKLRELEEiykrylTLLNSKKE 616
Cdd:COG0497 215 RRRLSN-----AEKLREA--LQEALEALSGGEGGALDLLGQALRALER-----LAEYDPSLAELAE------RLESALIE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 617 LEITQREIAKAKETLEMSFEELAEVEadiERIEKkLSQLKQKYNEEEYKKKREEKEELEKeLARL---EAQKKELEKRRD 693
Cdd:COG0497 277 LEEAASELRRYLDSLEFDPERLEEVE---ERLAL-LRRLARKYGVTVEELLAYAEELRAE-LAELensDERLEELEAELA 351
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 499321815 694 TIKSTLEKLkAEK--ENR--------ERVKKEIKDL--EKAK 723
Cdd:COG0497 352 EAEAELLEA-AEKlsAARkkaakkleKAVTAELADLgmPNAR 392
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
399-632 |
9.01e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 399 LEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKC------PVCGRELTD--EHREEL----------- 459
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAEleAELERLdassddlaale 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 460 --LSKYHLDLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELnvvNLEKIEKNATEYEKLLEEL 537
Cdd:COG4913 692 eqLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA---LLEERFAAALGDAVERELR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 538 RTLEGRIRGLAEdlkKLAPLEKKLAALIHK-KQELEKELKELNTKLEsfgfkSVEDLDSKLRELEEI-----YKRYLTLL 611
Cdd:COG4913 769 ENLEERIDALRA---RLNRAEEELERAMRAfNREWPAETADLDADLE-----SLPEYLALLDRLEEDglpeyEERFKELL 840
|
250 260
....*....|....*....|....*..
gi 499321815 612 NSKKELEITQ------REIAKAKETLE 632
Cdd:COG4913 841 NENSIEFVADllsklrRAIREIKERID 867
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
792-869 |
9.01e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.09 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGE--RIalglafRLAMSL--YLAGeiSLLILDEPTPYL---DEERrrkLITIMERyLKKIPQ-VILVSHDEELKDAA 863
Cdd:COG0178 486 LSGGEaqRI------RLATQIgsGLVG--VLYVLDEPSIGLhqrDNDR---LIETLKR-LRDLGNtVIVVEHDEDTIRAA 553
|
....*.
gi 499321815 864 DHVIRI 869
Cdd:COG0178 554 DYIIDI 559
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
785-866 |
9.20e-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: 41.72 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 785 KERPLTFLSGGE--RIALGLAfrlamslyLAGEISLLILDEPTPYLDEERRRKLITIMERyLKKIPQVILVSHDEELKDA 862
Cdd:cd03263 127 ANKRARTLSGGMkrKLSLAIA--------LIGGPSVLLLDEPTSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEA 197
|
....*
gi 499321815 863 -ADHV 866
Cdd:cd03263 198 lCDRI 202
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
3-44 |
9.60e-04 |
|
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: 42.19 E-value: 9.60e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 499321815 3 LERVTVKNFRSHSDTVVEFKEGINLIIGQNGSGKSSLLDAIL 44
Cdd:cd03241 1 LLELSIKNFALIEELELDFEEGLTVLTGETGAGKSILLDALS 42
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
452-736 |
1.06e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 452 TDEHREELLSKYHlDLNnskntLAKLIDRKSELERElrRIDMEIKRLTPLLTVAEQIRSIEEELNVVNLEKIEKNATEYE 531
Cdd:PRK05771 14 LKSYKDEVLEALH-ELG-----VVHIEDLKEELSNE--RLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 532 KLL----EELRTLEGRIRGLAEDLKKLaplEKKLAALIHKKQELEK------ELKELNT-----------KLESFGFKSV 590
Cdd:PRK05771 86 ELIkdveEELEKIEKEIKELEEEISEL---ENEIKELEQEIERLEPwgnfdlDLSLLLGfkyvsvfvgtvPEDKLEELKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 591 EDLDSKLRELEEIYKRYLTLLNSKKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQlkqkyneeeykkkree 670
Cdd:PRK05771 163 ESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEE---------------- 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499321815 671 keeLEKELARLEAQKKEL-EKRRDTIKSTLEKLKAEKEnRERVKKEIKDLEKA--------KDFTEELIEKVKKY 736
Cdd:PRK05771 227 ---IEKERESLLEELKELaKKYLEELLALYEYLEIELE-RAEALSKFLKTDKTfaiegwvpEDRVKKLKELIDKA 297
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
786-856 |
1.07e-03 |
|
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: 42.46 E-value: 1.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499321815 786 ERPLTFLSGGE--RIALGLAfrlamslyLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHD 856
Cdd:COG1245 207 DRDISELSGGElqRVAIAAA--------LLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHD 271
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
593-733 |
1.14e-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: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 593 LDSKLRELEEIYKRYltllnskKELEItQREIAKaKETLEMSFEELAEVEADIERIEKKLSQLKQKYneeeykkkreekE 672
Cdd:COG0542 406 IDSKPEELDELERRL-------EQLEI-EKEALK-KEQDEASFERLAELRDELAELEEELEALKARW------------E 464
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499321815 673 ELEKELARLEAQKKELEKRRDTIKSTLEKLKAEKENRERVKKEIKDlekakDFTEELIEKV 733
Cdd:COG0542 465 AEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLRE-----EVTEEDIAEV 520
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
785-877 |
1.45e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 40.91 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 785 KERPLTFLSGGER--IALGLAFrlamSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIpQVILVSHDEELKDA 862
Cdd:cd03278 107 KVQRLSLLSGGEKalTALALLF----AIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKET-QFIVITHRKGTMEA 181
|
90
....*....|....*.
gi 499321815 863 ADHVIRISLEN-GSSK 877
Cdd:cd03278 182 ADRLYGVTMQEsGVSK 197
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-50 |
1.47e-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: 40.31 E-value: 1.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 499321815 2 KLERVTVKNFRSH--SDTVVEFKEG-INLIIGQNGSGKSSLLDAILvGLYWP 50
Cdd:cd00267 1 EIENLSFRYGGRTalDNVSLTLKAGeIVALVGPNGSGKSTLLRAIA-GLLKP 51
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
792-867 |
1.61e-03 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 41.17 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGERIALGLAFRLAMslylagEISLLILDEPTPYLDEERRRKLitimERYLKKIPQ-----VILVSHD-EELKDAADH 865
Cdd:cd03296 137 LSGGQRQRVALARALAV------EPKVLLLDEPFGALDAKVRKEL----RRWLRRLHDelhvtTVFVTHDqEEALEVADR 206
|
..
gi 499321815 866 VI 867
Cdd:cd03296 207 VV 208
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
140-716 |
1.62e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 140 QGQIDAILESDEAREKVVREvLNLDKFETAYKKLSELKKTINNRIkeYRDILARTENIEELIKENEQELIQVLQEISKIE 219
Cdd:TIGR01612 702 KSKIDKEYDKIQNMETATVE-LHLSNIENKKNELLDIIVEIKKHI--HGEINKDLNKILEDFKNKEKELSNKINDYAKEK 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 220 EVLPSKRSKVDMLRKEVlrleETKVEIENSERLLEKRRGDKRtlEERIKNTEEYLEKLKEKEKELEEQVKEITSikkDVD 299
Cdd:TIGR01612 779 DELNKYKSKISEIKNHY----NDQINIDNIKDEDAKQNYDKS--KEYIKTISIKEDEIFKIINEMKFMKDDFLN---KVD 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 300 AYLALKEFKNEYLDKKYKIEKELTR------VEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKDHQLYEEI 373
Cdd:TIGR01612 850 KFINFENNCKEKIDSEHEQFAELTNkikaeiSDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENT 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 374 KAKKENLRQLKEKLGDKSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKgkcpvcgreltd 453
Cdd:TIGR01612 930 KESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLNDYEAKNNE------------ 997
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 454 ehreelLSKYHLDL-----NNSKNTLAKLIDRK----SELERELRRI-----DMEIKRLTPLLTVAEQIRSI----EEEL 515
Cdd:TIGR01612 998 ------LIKYFNDLkanlgKNKENMLYHQFDEKekatNDIEQKIEDAnknipNIEIAIHTSIYNIIDEIEKEigknIELL 1071
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 516 NVVNLEKIEKNATEYEKLLEELRTLEGRIRGLAEDLKKLAPLEKKLAALIHKKQELEKELKELnTKLESFGFKSVEDLDS 595
Cdd:TIGR01612 1072 NKEILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKAL-EEIKKKSENYIDEIKA 1150
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 596 KLRELEEIYKRYLTLLNSkKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNeeeyKKKREEKEELE 675
Cdd:TIGR01612 1151 QINDLEDVADKAISNDDP-EEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKG----INLSYGKNLGK 1225
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 499321815 676 KELARLEAQKKELEKRRDTIKSTLEKLKAEKENRERVKKEI 716
Cdd:TIGR01612 1226 LFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEM 1266
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
698-856 |
1.63e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.76 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 698 TLEKLKAEKENRERVKKEIKDLEKAkdftEELIEKVKKYKALARE--AALSKIGELASEIFAEFTEGKysevvvraeenk 775
Cdd:COG0419 91 FAEFLEAKPSERKEALKRLLGLEIY----EELKERLKELEEALESalEELAELQKLKQEILAQLSGLD------------ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 776 vrlfvvwegkerPLTFLSGGERIALGLAFRLAmslylageislLILDepTPYLDEERRRKLITIMERylkkipqVILVSH 855
Cdd:COG0419 155 ------------PIETLSGGERLRLALADLLS-----------LILD--FGSLDEERLERLLDALEE-------LAIITH 202
|
.
gi 499321815 856 D 856
Cdd:COG0419 203 V 203
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-44 |
1.78e-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: 40.74 E-value: 1.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 499321815 3 LERVTVKNFRSHSDTVV--EFKEGINLIIGQNGSGKSSLLDAIL 44
Cdd:cd03274 3 ITKLVLENFKSYAGEQVigPFHKSFSAIVGPNGSGKSNVIDSML 46
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
762-856 |
1.80e-03 |
|
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: 41.20 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 762 GKYSEVVVRAEENKVRlfvvwegkERPLTFLSGGErialglAFRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIME 841
Cdd:cd03236 118 GKLDELVDQLELRHVL--------DRNIDQLSGGE------LQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIR 183
|
90
....*....|....*
gi 499321815 842 RYLKKIPQVILVSHD 856
Cdd:cd03236 184 ELAEDDNYVLVVEHD 198
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1-52 |
1.86e-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: 39.83 E-value: 1.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 499321815 1 MKLERVTVKNFRSH---SDTVVEFKEGIN-LIIGQNGSGKSSLLdAILVGLyWPLR 52
Cdd:cd03223 1 IELENLSLATPDGRvllKDLSFEIKPGDRlLITGPSGTGKSSLF-RALAGL-WPWG 54
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
291-702 |
1.95e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 291 ITSIKKDVDAylaLKEFKNEYLDKKYKIEKELTRVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKDHQLY 370
Cdd:TIGR01612 1357 LNKIKKIIDE---VKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKELKNHILS 1433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 371 EEIKAKKENlrqlkeKLGDKSPEDIKKLLEELETKkttieeerNEITQRIGELK--NKIGDLKTAIEELKKAKGKCPVCG 448
Cdd:TIGR01612 1434 EESNIDTYF------KNADENNENVLLLFKNIEMA--------DNKSQHILKIKkdNATNDHDFNINELKEHIDKSKGCK 1499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 449 RELTD-----EHREELLSKYHLDLNN--SKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVaeQIRSIEEELNVVNLE 521
Cdd:TIGR01612 1500 DEADKnakaiEKNKELFEQYKKDVTEllNKYSALAIKNKFAKTKKDSEIIIKEIKDAHKKFIL--EAEKSEQKIKEIKKE 1577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 522 K--IEKNATEYEKLLEELRTLEGRIRGLAEDLKKLAPLEKKLAALIHKKQELEKELKELntklesfgfkSVEDLDSKLRE 599
Cdd:TIGR01612 1578 KfrIEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSF----------SIDSQDTELKE 1647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 600 LEEIYKRYLTLLNSKKEleitqreiakAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEelekela 679
Cdd:TIGR01612 1648 NGDNLNSLQEFLESLKD----------QKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAI------- 1710
|
410 420
....*....|....*....|...
gi 499321815 680 rleAQKKELEKRRDTIKSTLEKL 702
Cdd:TIGR01612 1711 ---ANKEEIESIKELIEPTIENL 1730
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
171-724 |
2.10e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 171 KKLSELKKTINNRIKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEVLRLEETKVEIENse 250
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ-- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 251 rLLEKRRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAYLaLKEFKNEYLDKKYK---IEKELTRVEE 327
Cdd:TIGR04523 258 -LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW-NKELKSELKNQEKKleeIQNQISQNNK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 328 LINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEKdhQLYEEIKAKKENLRQLKEKLGD--KSPEDIKKLLEELETK 405
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE--KLKKENQSYKQEIKNLESQINDleSKIQNQEKLNQQKDEQ 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 406 KTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKGKCPVCGREL--TDEHREELLSKYHLDLNNSKNTLAKLIDRKSE 483
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLdnTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 484 LERELRRIDMEIKRLT-PLLTVAEQIRSIEEELNVVNLEKIEKNA------TEYEKLLEELR--TLEGRIRGLAEDLKKL 554
Cdd:TIGR04523 494 KEKELKKLNEEKKELEeKVKDLTKKISSLKEKIEKLESEKKEKESkisdleDELNKDDFELKkeNLEKEIDEKNKEIEEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 555 APLEKKLAALIHKKQELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKRYLTLLNSKKELEITQREIAKAKETLEMS 634
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 635 FEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEKELARLeAQKKELEKRRDTIKSTLEKLKAEKENRERVKK 714
Cdd:TIGR04523 654 IKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRM-IRIKDLPKLEEKYKEIEKELKKLDEFSKELEN 732
|
570
....*....|
gi 499321815 715 EIKDLEKAKD 724
Cdd:TIGR04523 733 IIKNFNKKFD 742
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
788-856 |
2.14e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.64 E-value: 2.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499321815 788 PLTFLSGGE--RIALGlafRLAMSlylagEISLLILDEPTPYLDEERrrklITIMERYLKKIP-QVILVSHD 856
Cdd:PRK11819 160 KVTKLSGGErrRVALC---RLLLE-----KPDMLLLDEPTNHLDAES----VAWLEQFLHDYPgTVVAVTHD 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
754-867 |
2.23e-03 |
|
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: 40.61 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 754 EIFAEFTEGKYSEVVVRAEEnKVRLFVVWEGKERPLTFLSGGERIALGLAFrlamslYLAGEISLLILDEPTPYLDEERR 833
Cdd:COG4555 96 RYFAELYGLFDEELKKRIEE-LIELLGLEEFLDRRVGELSTGMKKKVALAR------ALVHDPKVLLLDEPTNGLDVMAR 168
|
90 100 110
....*....|....*....|....*....|....*.
gi 499321815 834 RKLITIMERyLKKIPQVILVS-HD-EELKDAADHVI 867
Cdd:COG4555 169 RLLREILRA-LKKEGKTVLFSsHImQEVEALCDRVV 203
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
792-879 |
2.29e-03 |
|
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: 39.99 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGERIALGLAfRLAMSlylagEISLLILDEPTPYLDEERRRKLITIMERYLKKiPQVILVSHDEELKDAADHVirISL 871
Cdd:cd03247 99 FSGGERQRLALA-RILLQ-----DAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHMDKI--LFL 169
|
....*...
gi 499321815 872 ENGSSKVE 879
Cdd:cd03247 170 ENGKIIMQ 177
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
788-867 |
2.41e-03 |
|
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: 40.45 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 788 PLTFlSGGERIALGLAfRLAMSLYlageiSLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEELKDA-ADHV 866
Cdd:TIGR02324 147 PATF-SGGEQQRVNIA-RGFIADY-----PILLLDEPTASLDAANRQVVVELIAEAKARGAALIGIFHDEEVRELvADRV 219
|
.
gi 499321815 867 I 867
Cdd:TIGR02324 220 M 220
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
382-775 |
2.71e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 382 QLKEKLGDKSPEDIKKLLEEL-ETKKTTIEEERneitqRIGELKNKIGDLKTAIEELKKAKGKCPVCGRELTDEHREELL 460
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAkKTETGKAEEAR-----KAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 461 SKyhldlnnSKNTLAKLIDRKSELER--ELRRIDMEIKRLTPLLTvAEQIRSIEEELNVVNLEKIEK-NATEYEKLLEEL 537
Cdd:PTZ00121 1158 RK-------AEDARKAEEARKAEDAKkaEAARKAEEVRKAEELRK-AEDARKAEAARKAEEERKAEEaRKAEDAKKAEAV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 538 RTLEgRIRGLAEDLKKlaplekklaalIHKKQELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKRYltllNSKKEL 617
Cdd:PTZ00121 1230 KKAE-EAKKDAEEAKK-----------AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE----EKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 618 EITQREIAKAKETLEMSFEE---LAEVEADIERIEKKLSQLKQKYNEEEYKKkreekeelekelarlEAQKKELEKRRDT 694
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEakkADEAKKKAEEAKKKADAAKKKAEEAKKAA---------------EAAKAEAEAAADE 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 695 IKSTLEKLKAEKENRERVKKEIKDLEKAKDFTEELIEKVKKYKALAREAALSKIGELASEIFAEFTegKYSEVVVRAEEN 774
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK--KKAEEKKKADEA 1436
|
.
gi 499321815 775 K 775
Cdd:PTZ00121 1437 K 1437
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
787-855 |
2.83e-03 |
|
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: 40.03 E-value: 2.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499321815 787 RPLTFLSGGERIALGLAfrlamSLYLAGEiSLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSH 855
Cdd:TIGR01189 123 LPAAQLSAGQQRRLALA-----RLWLSRR-PLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
786-873 |
2.87e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 786 ERPLTFLSGGERIALGLAFRLAMslylagEISLLILDEPTPYLDEERrrklITIMERYLKKIP-QVILVSHDEELKDA-A 863
Cdd:PRK10636 144 ERPVSDFSGGWRMRLNLAQALIC------RSDLLLLDEPTNHLDLDA----VIWLEKWLKSYQgTLILISHDRDFLDPiV 213
|
90
....*....|
gi 499321815 864 DHVIRISLEN 873
Cdd:PRK10636 214 DKIIHIEQQS 223
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
776-865 |
2.92e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.93 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 776 VRLFVVWEGKERPLTFLSGGERIALGLaFRLAMSlylagEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSH 855
Cdd:PRK13540 112 CRLFSLEHLIDYPCGLLSSGQKRQVAL-LRLWMS-----KAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
90
....*....|
gi 499321815 856 DEELKDAADH 865
Cdd:PRK13540 186 QDLPLNKADY 195
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
786-870 |
2.98e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 40.08 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 786 ERPLTFLSGGERIALGLAFRLAmslYLAgeiSLLILDEPTPYLDEERRRKLITIMERYLK-KIPQVILVSHDEELKDAAD 864
Cdd:PRK10247 132 TKNIAELSGGEKQRISLIRNLQ---FMP---KVLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTHDKDEINHAD 205
|
....*.
gi 499321815 865 HVIRIS 870
Cdd:PRK10247 206 KVITLQ 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
812-866 |
3.09e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.16 E-value: 3.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 499321815 812 LAGEISLLILDEPTPYLDEERRRKLITIMERyLKKipQ---VILVSHD-EELKDAADHV 866
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRR-LKA--QgvaIIYISHRlDEVFEIADRV 210
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
786-859 |
3.15e-03 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 40.98 E-value: 3.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499321815 786 ERPLTFLSGGERIalglafRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHDEEL 859
Cdd:PRK09536 134 DRPVTSLSGGERQ------RVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDL 201
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
483-584 |
3.16e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 483 ELERELRRIDMEIKRLtplltvaeqirsiEEELNVVNLEKIEKNATEYEKLLEELRTLEGRIRGLAEDLKKLAPLEKKLA 562
Cdd:COG0542 415 ELERRLEQLEIEKEAL-------------KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELE 481
|
90 100
....*....|....*....|..
gi 499321815 563 ALIHKKQELEKELKELNTKLES 584
Cdd:COG0542 482 QRYGKIPELEKELAELEEELAE 503
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
291-859 |
3.19e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 291 ITSIKKDVDAYLALKEFKNEYLDKKYKIEKEL----TRVEELINEIQKRIEELNEKESEKEKLENEKKEILNKLAILEkd 366
Cdd:TIGR00606 718 LKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELrnklQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIME-- 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 367 hQLYEEIKAKKENLRQLKEKL----GDKSPEDIKKLLEELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKG 442
Cdd:TIGR00606 796 -RFQMELKDVERKIAQQAAKLqgsdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 443 KCPvcgrelTDEHREELLSKYHLDLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVNLEK 522
Cdd:TIGR00606 875 QIG------TNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 523 IEKNATEYEKLLEElRTLEGRIRGLAEDLKKLAPLEKKLAALIHKKQELEKELKELNTKLESFGFK--------SVEDLD 594
Cdd:TIGR00606 949 KVKNIHGYMKDIEN-KIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQerwlqdnlTLRKRE 1027
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 595 SKLRELEEIYKRYLTLLNSKKELEITQrEIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEEL 674
Cdd:TIGR00606 1028 NELKEVEEELKQHLKEMGQMQVLQMKQ-EHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREM 1106
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 675 EKELARLEAQKKELEKRRDTIKSTLEKLKAEKenRERVKKEIKDLEKaKDFTEELIEKVKKYKALAREAALSKigelase 754
Cdd:TIGR00606 1107 MIVMRTTELVNKDLDIYYKTLDQAIMKFHSMK--MEEINKIIRDLWR-STYRGQDIEYIEIRSDADENVSASD------- 1176
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 755 ifaeftegKYSEVVVRAEENKVRLFVVWEGKerpltfLSGGERIALGLAFRLAMSLYLAGEISLLILDEPTPYLDEERRR 834
Cdd:TIGR00606 1177 --------KRRNYNYRVVMLKGDTALDMRGR------CSAGQKVLASLIIRLALAETFCLNCGIIALDEPTTNLDRENIE 1242
|
570 580 590
....*....|....*....|....*....|
gi 499321815 835 KLI-----TIMERYLKKIPQVILVSHDEEL 859
Cdd:TIGR00606 1243 SLAhalveIIKSRSQQRNFQLLVITHDEDF 1272
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
162-735 |
3.23e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.58 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 162 NLDKFETAYKKLSELKKTINNRIKEYrdilARTENIEELIKEneqELIQVLQEISKIEEVLPSKRSKVDMLRKEVLRLE- 240
Cdd:TIGR01612 1067 NIELLNKEILEEAEINITNFNEIKEK----LKHYNFDDFGKE---ENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKk 1139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 241 -------ETKVEIENSERLLEK--RRGDKRTLEERIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAYLALKEFKNEY 311
Cdd:TIGR01612 1140 ksenyidEIKAQINDLEDVADKaiSNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSY 1219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 312 ---LDKKY--KIEKELTRVEELINEIQK------RIEELNEKESEKEKLENEKKEILNKLAILEKDHQLYEEIKAK-KEN 379
Cdd:TIGR01612 1220 gknLGKLFleKIDEEKKKSEHMIKAMEAyiedldEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKhDEN 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 380 LRQLKEKL-----GDKSPEDIKKLLEELETKKTTIEEERNEITQRIGELKN-----KIGDLKTAIEELKKAKGKCPVCGR 449
Cdd:TIGR01612 1300 ISDIREKSlkiieDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANiynilKLNKIKKIIDEVKEYTKEIEENNK 1379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 450 ELTDE--HREELLSKYHLDLNnskntlakLIDRKSELEREL--RRIDMEIKRLTPLLT--VAEQ------IRSIEEE--- 514
Cdd:TIGR01612 1380 NIKDEldKSEKLIKKIKDDIN--------LEECKSKIESTLddKDIDECIKKIKELKNhiLSEEsnidtyFKNADENnen 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 515 --LNVVNLE----------KIEKN--ATEYEKLLEELRTLEGRIRGLAEDLKKLAPLEKKLAALIhkkQELEKELKELNT 580
Cdd:TIGR01612 1452 vlLLFKNIEmadnksqhilKIKKDnaTNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELF---EQYKKDVTELLN 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 581 KLESFGFK-----SVEDLDSKLRELEEIYKRYlTLLNSKKELEItqREIAKAKETLE-------MSFEELAEVEADIERI 648
Cdd:TIGR01612 1529 KYSALAIKnkfakTKKDSEIIIKEIKDAHKKF-ILEAEKSEQKI--KEIKKEKFRIEddaakndKSNKAAIDIQLSLENF 1605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 649 EKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKKELEKRRD---TIKSTLEKLKAEKENRERVKKEIKDLEKAKDF 725
Cdd:TIGR01612 1606 ENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDTELKENGDnlnSLQEFLESLKDQKKNIEDKKKELDELDSEIEK 1685
|
650
....*....|
gi 499321815 726 TEELIEKVKK 735
Cdd:TIGR01612 1686 IEIDVDQHKK 1695
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
466-656 |
3.37e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.05 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 466 DLNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAeqIRSIEEELNVVNLEKIEKnateYEKLLEELRTLEGRIR 545
Cdd:pfam04012 37 ELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA--LTKGNEELAREALAEKKS----LEKQAEALETQLAQQR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 546 GLAEDLKK-LAPLEKKLAALIHKKQEL---EKELKELNTKLESFGFKSVEDLDSKLRELEEiykryltllnskKELEITQ 621
Cdd:pfam04012 111 SAVEQLRKqLAALETKIQQLKAKKNLLkarLKAAKAQEAVQTSLGSLSTSSATDSFERIEE------------KIEEREA 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 499321815 622 REIAKAKETLEMSF-EELAEVEADIERIEKKLSQLK 656
Cdd:pfam04012 179 RADAAAELASAVDLdAKLEQAGIQMEVSEDVLARLK 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
792-866 |
3.49e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 40.50 E-value: 3.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499321815 792 LSGGERIALGLAFRLAMslylagEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSH-DEELKDAADHV 866
Cdd:PRK13649 146 LSGGQMRRVAIAGILAM------EPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlMDDVANYADFV 215
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
790-857 |
3.61e-03 |
|
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: 40.81 E-value: 3.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499321815 790 TFLSGGERIalglafRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIM----ERYLkkipqVILVSHDE 857
Cdd:TIGR02868 470 ARLSGGERQ------RLALARALLADAPILLLDEPTEHLDAETADELLEDLlaalSGRT-----VVLITHHL 530
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
792-874 |
3.80e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 40.20 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGErialglAFRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQVILVSHD-EELKDAADHVirIS 870
Cdd:PRK13641 146 LSGGQ------MRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDV--LV 217
|
....
gi 499321815 871 LENG 874
Cdd:PRK13641 218 LEHG 221
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-44 |
3.88e-03 |
|
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: 39.97 E-value: 3.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 499321815 1 MKLERVTVKNFRSHSD-TVVE-FKEGINLIIGQNGSGKSSLLDAIL 44
Cdd:cd03273 1 MHIKEIILDGFKSYATrTVISgFDPQFNAITGLNGSGKSNILDAIC 46
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
792-870 |
3.91e-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: 39.06 E-value: 3.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499321815 792 LSGGERIALGLAfRLamsLYLagEISLLILDEPTPYLDEERRRKLITIMERYLKKIpqvILVSHDEELKDAADHVIRIS 870
Cdd:cd03223 92 LSGGEQQRLAFA-RL---LLH--KPKFVFLDEATSALDEESEDRLYQLLKELGITV---ISVGHRPSLWKFHDRVLDLD 161
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
393-658 |
4.27e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.04 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 393 EDIKKLLEEletkKTTIEEERNEITQRIGELKNKIgdlKTAieelkkAKGKCPVcgrELTDEHREELLSKYHLDLNNSKN 472
Cdd:PLN02939 156 EDLEKILTE----KEALQGKINILEMRLSETDARI---KLA------AQEKIHV---EILEEQLEKLRNELLIRGATEGL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 473 TLAKLIDRKSELERE--LRRIDMEIKRltplltvAEQIRSIEEELNVVNLEKieknatEYEKLLEELRTLEGRIRGLAED 550
Cdd:PLN02939 220 CVHSLSKELDVLKEEnmLLKDDIQFLK-------AELIEVAETEERVFKLEK------ERSLLDASLRELESKFIVAQED 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 551 LKKLAPLekKLAALIHKKQELEKELKELNTKLESFG--FKSVEDLDSKLRELEEIYKRYLTLLNSKKELEITQREIAKAK 628
Cdd:PLN02939 287 VSKLSPL--QYDCWWEKVENLQDLLDRATNQVEKAAlvLDQNQDLRDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLE 364
|
250 260 270
....*....|....*....|....*....|....
gi 499321815 629 ETLEMSFEELAE----VEADIERIEKKLSQLKQK 658
Cdd:PLN02939 365 ERLQASDHEIHSyiqlYQESIKEFQDTLSKLKEE 398
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
792-869 |
4.49e-03 |
|
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: 39.80 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGE--RIALGLAfrlamslyLAGEISLLILDEPTPYLDEERRRKLITIMERyLKKIPQ--VILVSHDEEL-KDAADHV 866
Cdd:cd03257 146 LSGGQrqRVAIARA--------LALNPKLLIADEPTSALDVSVQAQILDLLKK-LQEELGltLLFITHDLGVvAKIADRV 216
|
...
gi 499321815 867 IRI 869
Cdd:cd03257 217 AVM 219
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
569-750 |
4.75e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 569 QELEKELKELNTKLESfGFKSVEDLDSKLRELEEiykrylTLLNSKKELEITQREIAKAKEtlemsfeELAEVEADIERI 648
Cdd:COG1579 13 QELDSELDRLEHRLKE-LPAELAELEDELAALEA------RLEAAKTELEDLEKEIKRLEL-------EIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 649 EKKLSQLKqkyNEEEYKKKREEKEELEKELARLEAQKKELEKRRDTIKSTLEKLKAE-KENRERVKKEIKDLEKAKDFTE 727
Cdd:COG1579 79 EEQLGNVR---NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAElAELEAELEEKKAELDEELAELE 155
|
170 180
....*....|....*....|...
gi 499321815 728 ELIEKVKKykalAREAALSKIGE 750
Cdd:COG1579 156 AELEELEA----EREELAAKIPP 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
392-632 |
4.97e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 392 PEDIKKLLE--ELETKKTTIEEERNEITQRIGELKNKIGDLKTAIEELKKAKgkcpvcgreltdehreellskyhldlnn 469
Cdd:COG1579 3 PEDLRALLDlqELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL---------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 470 skntlaklidrkSELERELRRIDMEIKrltpllTVAEQIRSIEEELNVVnlekieKNATEYEKLLEELRTLEGRIRGlae 549
Cdd:COG1579 55 ------------EDLEKEIKRLELEIE------EVEARIKKYEEQLGNV------RNNKEYEALQKEIESLKRRISD--- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 550 dlkklapLEKKLAALIHKKQELEKELKELNTKLEsfgfKSVEDLDSKLRELEEIYKRyltllnSKKELEITQREIAKAKE 629
Cdd:COG1579 108 -------LEDEILELMERIEELEEELAELEAELA----ELEAELEEKKAELDEELAE------LEAELEELEAEREELAA 170
|
...
gi 499321815 630 TLE 632
Cdd:COG1579 171 KIP 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
792-856 |
5.17e-03 |
|
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: 39.47 E-value: 5.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499321815 792 LSGGERIALGLAFRLAMslylagEISLLILDEPTPYLDEERRRKLITIMERyLKKIPQVILVSHD 856
Cdd:cd03260 142 LSGGQQQRLCLARALAN------EPEVLLLDEPTSALDPISTAKIEELIAE-LKKEYTIVIVTHN 199
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
157-660 |
5.51e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 157 VREVLNLDKFETAYKKLSELKKTINNRiKEYRDILARTENIEELIKENEQELIQVLQEISKIEEVLPSKRSKVDMLRKEV 236
Cdd:COG5022 783 LRRLVDYELKWRLFIKLQPLLSLLGSR-KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRF 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 237 LRLEETKVEIENSERLLEKRRgdkrtleeRIKNTEEYLEKLKEKEKELEEQVKEITSIKKDVDAYLALK-EFKNEyldkk 315
Cdd:COG5022 862 SLLKKETIYLQSAQRVELAER--------QLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENlEFKTE----- 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 316 ykiekELTRVEELINEIQ------KRIEELNEKESEKEKLENEKKEILNKLAILEKDHQLYEEIKAKKENLRQLKEKLGD 389
Cdd:COG5022 929 -----LIARLKKLLNNIDleegpsIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAE 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 390 KSpedikKLLEELETKKTTIEEERNEITqrigELKNKIGDLKTAIEELKKAKGKCPVCGRELTD--EHREELLS-KYHLD 466
Cdd:COG5022 1004 LS-----KQYGALQESTKQLKELPVEVA----ELQSASKIISSESTELSILKPLQKLKGLLLLEnnQLQARYKAlKLRRE 1074
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 467 LNNSKNTLAKLIDRKSELERELRRIDMEIKRLTPLLTVAEQIRSIEEELNVVNLEKIEKNATEYEKLLEELRTLEGRIRG 546
Cdd:COG5022 1075 NSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQL 1154
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 547 LAEDLKKLAPLEKKLA--ALIHKKQELEKELKELNTKLESfgfkSVEDLDSKLRELEEIYKRYLTLLNSKKELEITQREI 624
Cdd:COG5022 1155 ELDGLFWEANLEALPSppPFAALSEKRLYQSALYDEKSKL----SSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEG 1230
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 499321815 625 AKAKETL----EMSFEELAEVEADIERIEKKLSQLKQKYN 660
Cdd:COG5022 1231 WVPTEYStslkGFNNLNKKFDTPASMSNEKLLSLLNSIDN 1270
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
719-866 |
6.44e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 39.40 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 719 LEKAKDFTEELIEKVKKYKALAREAALSKIGELASE---IFAEFTEGKYSEVVVRAEENKVRLFVVWEGKERPLTFLSGG 795
Cdd:PRK13652 62 LIRGEPITKENIREVRKFVGLVFQNPDDQIFSPTVEqdiAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGG 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499321815 796 ERIALGLAFRLAMslylagEISLLILDEPTPYLDEERRRKLITIMERYLKKIP-QVILVSHDEEL-KDAADHV 866
Cdd:PRK13652 142 EKKRVAIAGVIAM------EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGmTVIFSTHQLDLvPEMADYI 208
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
362-485 |
6.70e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.62 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 362 ILEKDHQLYEEIKAKKENLRQLKEKLGDKSPEDIKKLLEELETKKTTIEEERN----------EITQRIGELKNKIGDLK 431
Cdd:smart00787 173 IKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKkleeleeelqELESKIEDLTNKKSELN 252
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 499321815 432 TAIEELKKAKGKCPVCGR----ELTDEHRE-ELLSKYHLdLNNSKNTLAKLIDRKSELE 485
Cdd:smart00787 253 TEIAEAEKKLEQCRGFTFkeieKLKEQLKLlQSLTGWKI-TKLSGNTLSMTYDREINLV 310
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
792-870 |
6.82e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 40.18 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 792 LSGGE--RIALGlafRLamslyLAGEISLLILDEPTPYLDEERRRKLITIMERYLKKIpQVILVSHDEELKDAADHVIRI 869
Cdd:COG4178 486 LSLGEqqRLAFA---RL-----LLHKPDWLFLDEATSALDEENEAALYQLLREELPGT-TVISVGHRSTLAAFHDRVLEL 556
|
.
gi 499321815 870 S 870
Cdd:COG4178 557 T 557
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
19-44 |
7.12e-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: 38.60 E-value: 7.12e-03
10 20
....*....|....*....|....*..
gi 499321815 19 VEFKEG-INLIIGQNGSGKSSLLDAIL 44
Cdd:cd03250 26 LEVPKGeLVAIVGPVGSGKSSLLSALL 52
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
636-781 |
7.30e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 636 EELAEVEADIERIEKKLSQLKQKYNEEEYKKKREEKEELEKELARLEAQKKELEKRRDTIKSTLEKLKAEKENRERVKKE 715
Cdd:PRK05771 43 ERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQE 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499321815 716 IKDLEKAKDFTEELIekvkkyKALAREAALSKIGELASEIFAEF--TEGKYSEVVVRAEENKVRLFVV 781
Cdd:PRK05771 123 IERLEPWGNFDLDLS------LLLGFKYVSVFVGTVPEDKLEELklESDVENVEYISTDKGYVYVVVV 184
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
792-842 |
7.49e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.44 E-value: 7.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 499321815 792 LSGGER-----IALGLAFRLAMSLYLAGE--ISLLILDEPTPYLDEERRRKLITIMER 842
Cdd:pfam13558 33 LSGGEKqllayLPLAAALAAQYGSAEGRPpaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
792-867 |
7.93e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 39.23 E-value: 7.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499321815 792 LSGGERIALGLAFRLAMslylagEISLLILDEPTPYLDEERRRKLITIMERYLKKIPQ-VILVSHD-EELKDAADHVI 867
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAM------EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLtTVLVTHSmEDAARYADQIV 217
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
434-659 |
8.68e-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: 39.66 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 434 IEELKKAKGKCPVCGRELTDEHREELLSKYHLDLNNSKNTLAKLIDRKselereLRRIDMEIKRLTPLLTVAEQIRSIEE 513
Cdd:pfam13166 248 LELHKAHLDTCPFCGQPLPAERKAALEAHFDDEFTEFQNRLQKLIEKV------ESAISSLLAQLPAVSDLASLLSAFEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 514 elnvvNLEKIEKNATEYEKLLEEL-RTLEGRIRGLA---------EDLKKLAPLEKKLAALIHKKQE----LEKELKELN 579
Cdd:pfam13166 322 -----DVEDIESEAEVLNSQLDGLrRALEAKRKDPFksieldsvdAKIESINDLVASINELIAKHNEitdnFEEEKNKAK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 580 TKLESFgfkSVEDLDSKLRELEEIYKRyltLLNSKKELEITQREIAKAKETLEMSFEELAEVEADIERIEKKLSQLKQKY 659
Cdd:pfam13166 397 KKLRLH---LVEEFKSEIDEYKDKYAG---LEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKLLKAF 470
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
786-856 |
9.15e-03 |
|
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: 39.77 E-value: 9.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499321815 786 ERPLTFLSGGERIalglafRLAMSLYLAGEISLLILDEPTPYLDEERRRKLITIMERYL-KKIPQVILVSHD 856
Cdd:COG1245 450 DKNVKDLSGGELQ------RVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAeNRGKTAMVVDHD 515
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
483-742 |
9.22e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.72 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 483 ELERELRRIDMEIKRLTplltvAEQIRsiEEELnVVNLEKIEknatEYEKLLEELRTLEGRIRGLAEDLKKLAPLEKkla 562
Cdd:pfam17380 345 ERERELERIRQEERKRE-----LERIR--QEEI-AMEISRMR----ELERLQMERQQKNERVRQELEAARKVKILEE--- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 563 alihkkqELEKELKELNTKLESFGFKSVEDLDSKLRELEEIYKRYLTLLNsKKELE-------ITQREIAKAKETLEMSF 635
Cdd:pfam17380 410 -------ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVR-LEEQErqqqverLRQQEEERKRKKLELEK 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499321815 636 EELAEVEADIER---IEKKLSQLKQKYNEEEYKKKREekeelekelarleaqKKELEKRRDTIKSTLEKLKAEKENRErv 712
Cdd:pfam17380 482 EKRDRKRAEEQRrkiLEKELEERKQAMIEEERKRKLL---------------EKEMEERQKAIYEEERRREAEEERRK-- 544
|
250 260 270
....*....|....*....|....*....|
gi 499321815 713 KKEIKDLEKAKDFTEELIEKVKKYKALARE 742
Cdd:pfam17380 545 QQEMEERRRIQEQMRKATEERSRLEAMERE 574
|
|
| |
