|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-1416 |
0e+00 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 2890.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1 METLSRSLSKSLGELLASNSNNHFSRRSGSTIDDhDEEALKWAALEKLPTFARLRTTIIHPHED-----------LVDVT 69
Cdd:PLN03140 9 RRSISRSVSRSSRNMEDVFSGGSQSRRRTSSVDE-DEEALKWAAIEKLPTYSRLRTSIMKSFVEndvygnqllhkEVDVT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 70 KLGVDDRQKFIDSIFKVTEEDNEKFLKKFRNRIDRVRIKLPTVEVRFEKVTIEANCHIGKRALPTLPNAALNIAERGLRL 149
Cdd:PLN03140 88 KLDGNDRQKFIDMVFKVAEEDNEKFLKKFRNRIDRVGIKLPTVEVRFEHLTVEADCYIGSRALPTLPNAARNIAESALGM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 150 LGFNFTKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSLKVTGRVTYNGHGLEEFVPQKTSAYISQN 229
Cdd:PLN03140 168 LGINLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYISQN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 230 DVHVGVMTVQETLDFSARCQGVGTRYDLLSELVRREKDAGILPEPEVDLFMKSIAAGNVKSSLITDYTLRILGLDICKDT 309
Cdd:PLN03140 248 DVHVGVMTVKETLDFSARCQGVGTRYDLLSELARREKDAGIFPEAEVDLFMKATAMEGVKSSLITDYTLKILGLDICKDT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 310 VVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSLLQPAPETFELFDD 389
Cdd:PLN03140 328 IVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 390 IILLSEGQIVYQGPRDHVLTFFETCGFKCPDRKGTADFLQEVTSRKDQEQYWADSKKPYSYISVSEFSKRFRTFHVGANL 469
Cdd:PLN03140 408 IILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKDQEQYWADRNKPYRYISVSEFAERFKSFHVGMQL 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 470 EKDLSVPYDRFKSHPASLVFKKHSVPKSQLFKVCWDRELLLMKRNAFFYITKTVQIIIMALIASTVYLRTEMGTKNESDG 549
Cdd:PLN03140 488 ENELSVPFDKSQSHKAALVFSKYSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTEMHTRNEEDG 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 550 AVYIGALMFSMIVNMFNGFAELALMIQRLPVFYKQRDLLFHPPWTFSLPTFLLGIPISIFESVVWVTITYYMIGFAPELS 629
Cdd:PLN03140 568 ALYIGALLFSMIINMFNGFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 630 RFLKHLLVIFLTQQMAGGIFRFIAATCRSMILANTGGALVILLLFLLGGFIVPRGEIPKWWKWAYWVSPMAYTYDALTVN 709
Cdd:PLN03140 648 RFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPNWWEWAYWVSPLSYGFNALAVN 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 710 EMLAPRWINQPSSDNSTSLGLAVLEIFDIFTDPNWYWIGVGGILGFTVLFNILVTLALTFLNPLEKQQAVVSKENTEE-- 787
Cdd:PLN03140 728 EMFAPRWMNKMASDNSTRLGTAVLNIFDVFTDKNWYWIGVGALLGFTILFNVLFTLALTYLNPLGKKQAIISEETAEEme 807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 788 ----------------------------------NRAENGSKSKSIDVKRGMVLPFTPLTMSFDNVNYYVDMPKEMKEQG 833
Cdd:PLN03140 808 geedsiprslssadgnntrevaiqrmsnpeglskNRDSSLEAANGVAPKRGMVLPFTPLAMSFDDVNYFVDMPAEMKEQG 887
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 834 VSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKRQETFARISGYCEQNDIHSPQ 913
Cdd:PLN03140 888 VTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQ 967
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 914 VTVKESLIYSAFLRLPKEVTKYEKMRFVDEVMELVELESLKDAVVGLPGITGLSTEQRKRLTIAVELVANPSIIFMDEPT 993
Cdd:PLN03140 968 VTVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 994 SGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLLKRGGQVIYAGPLGQNSHKIIEYFQAIHGVPKIKE 1073
Cdd:PLN03140 1048 SGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYSGPLGRNSHKIIEYFEAIPGVPKIKE 1127
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1074 KYNPATWMLEVSSMAAEAKLEIDFAEHYKTSSLYQQNKNLVKELSTPPQGASDLYFSTRFSQSLLGQFKSCLWKQWITYW 1153
Cdd:PLN03140 1128 KYNPATWMLEVSSLAAEVKLGIDFAEHYKSSSLYQRNKALVKELSTPPPGASDLYFATQYSQSTWGQFKSCLWKQWWTYW 1207
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1154 RTPDYNLARFFFTLAAAVMLGSIFWKVGTKRENANDLTKVIGAMYAAVLFVGVNNSSSVQPLIAVERSVFYRERAAEMYS 1233
Cdd:PLN03140 1208 RSPDYNLVRFFFTLAAALMVGTIFWKVGTKRSNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAAGMYS 1287
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1234 ALPYALAQVVCEIPYVLIQTTYYTLIIYAMMCFEWTLAKFFWFYFVSFMSFLYFTYYGMMTVALTPNQQVAAVFAGAFYG 1313
Cdd:PLN03140 1288 ALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAIFAAAFYG 1367
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1314 LFNLFSGFVIPRPRIPKWWIWYYWICPVAWTVYGLIVSQYGDVEDTIKVPGMANDPTIKWYIENHYGYDADFMIPIATVL 1393
Cdd:PLN03140 1368 LFNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYGDVEDTIKVPGGAPDPTIKWYIQDHYGYDPDFMGPVAAVL 1447
|
1450 1460
....*....|....*....|...
gi 18401096 1394 VGFTLFFAFMFAFGIRTLNFQQR 1416
Cdd:PLN03140 1448 VGFTVFFAFIFAFCIRTLNFQTR 1470
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
88-1416 |
0e+00 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 1857.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 88 EEDNEKFLKKFRNRIDRVRIKLP--TVEVRFEKVTIEAnCHIGKRALPTLPNAALNIAERGLRLLgFNFTKTTKVTILRD 165
Cdd:TIGR00956 2 EFNAKAWVKNFRKLIDSDPIYYKpyKLGVAYKNLSAYG-VAADSDYQPTFPNALLKILTRGFRKL-KKFRDTKTFDILKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 166 VSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSLK-VTGRVTYNGHGLEEFVPQKT--SAYISQNDVHVGVMTVQETL 242
Cdd:TIGR00956 80 MDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIgVEGVITYDGITPEEIKKHYRgdVVYNAETDVHFPHLTVGETL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 243 DFSARCQGVGTRYDLLSELVRREKdagilpepevdlfmksiaagnvksslITDYTLRILGLDICKDTVVGDEMIRGISGG 322
Cdd:TIGR00956 160 DFAARCKTPQNRPDGVSREEYAKH--------------------------IADVYMATYGLSHTRNTKVGNDFVRGVSGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 323 QKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSLLQPAPETFELFDDIILLSEGQIVYQG 402
Cdd:TIGR00956 214 ERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 403 PRDHVLTFFETCGFKCPDRKGTADFLQEVTSRKdQEQYWADSKKPySYISVSEFSKRFRTFHVGANLEKDLSVPYDR--- 479
Cdd:TIGR00956 294 PADKAKQYFEKMGFKCPDRQTTADFLTSLTSPA-ERQIKPGYEKK-VPRTPQEFETYWRNSPEYAQLMKEIDEYLDRcse 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 480 -----------FKSHP-ASLVFKKHSVPKSQLFKVCWDRELLLMKRNAFFYITKTVQIIIMALIASTVYLRTEMgtkNES 547
Cdd:TIGR00956 372 sdtkeayreshVAKQSkRTRPSSPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPK---NTS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 548 DGAVYIGALMFSMIVNMFNGFAELALMIQRLPVFYKQRDLLFHPPWTFSLPTFLLGIPISIFESVVWVTITYYMIGFAPE 627
Cdd:TIGR00956 449 DFYSRGGALFFAILFNAFSSLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRT 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 628 LSRFLKHLLVIFLTQQMAGGIFRFIAATCRSMILANTGGALVILLLFLLGGFIVPRGEIPKWWKWAYWVSPMAYTYDALT 707
Cdd:TIGR00956 529 AGRFFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLM 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 708 VNEMLAPRWINQ---PSSDNSTSLG-------LAVLEIFDIFTDPN------------WYWIGVGGILGFTVLFNILVTL 765
Cdd:TIGR00956 609 VNEFHGRRFECSqyvPSGGGYDNLGvtnkvctVVGAEPGQDYVDGDdylklsfqyynsHKWRNFGIIIGFTVFFFFVYIL 688
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 766 ALTFLNPLEKQQAVVSKENTEENRAENG---SKSKSIDVKRGMVLPFTPLTMSFDNVNYYVDMPKEMK-----------E 831
Cdd:TIGR00956 689 LTEFNKGAKQKGEILVFRRGSLKRAKKAgetSASNKNDIEAGEVLGSTDLTDESDDVNDEKDMEKESGedifhwrnltyE 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKRQETFARISGYCEQNDIHS 911
Cdd:TIGR00956 769 VKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHL 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 912 PQVTVKESLIYSAFLRLPKEVTKYEKMRFVDEVMELVELESLKDAVVGLPGItGLSTEQRKRLTIAVELVANP-SIIFMD 990
Cdd:TIGR00956 849 PTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGE-GLNVEQRKRLTIGVELVAKPkLLLFLD 927
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 991 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLLKRGGQVIYAGPLGQNSHKIIEYFQaIHGVPK 1070
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQTVYFGDLGENSHTIINYFE-KHGAPK 1006
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1071 IKEKYNPATWMLEVSSMAAEAKLEIDFAEHYKTSSLYQQNKNLVKELSTPPQGASDLYFST---RFSQSLLGQFKSCLWK 1147
Cdd:TIGR00956 1007 CPEDANPAEWMLEVIGAAPGAHANQDYHEVWRNSSEYQAVKNELDRLEAELSKAEDDNDPDalsKYAASLWYQFKLVLWR 1086
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1148 QWITYWRTPDYNLARFFFTLAAAVMLGSIFWKVGTkreNANDLTKVIGAMYAAVLFVGVNNSSSVQPLIAVERSVFYRER 1227
Cdd:TIGR00956 1087 TFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGT---SLQGLQNQMFAVFMATVLFNPLIQQYLPPFVAQRDLYEVRER 1163
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1228 AAEMYSALPYALAQVVCEIPYVLIQTTYYTLIIYAMMCFEWTLAK-------FFWFYFVSFMSFLYFTYYGMMTVALTPN 1300
Cdd:TIGR00956 1164 PSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGFYWNASKtgqvherGVLFWLLSTMFFLYFSTLGQMVISFNPN 1243
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1301 QQVAAVFAGAFYGLFNLFSGFVIPRPRIPKWWIWYYWICPVAWTVYGLIVSQYGDVEDTIKVP---------GMANDPTI 1371
Cdd:TIGR00956 1244 ADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLADVPVTCKVKelltfnppsGQTCGEYM 1323
|
1370 1380 1390 1400 1410 1420
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18401096 1372 KWYIEN-----------------HYGYDADFMIPIATVLVG----FTLFFAFMFAFGIRTLNFQQR 1416
Cdd:TIGR00956 1324 KPYLENaggyllnpnatdscsfcQYSYTNDFLEPISSKYSGrwrnFGIFIAFIFFNIIATVFFYWL 1389
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
811-1049 |
2.68e-102 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. 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: 213199 [Multi-domain] Cd Length: 192 Bit Score: 323.81 E-value: 2.68e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 811 PLTMSFDNVNYYVDMPKemkeqgvskDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGF 890
Cdd:cd03232 1 GSVLTWKNLNYTVPVKG---------GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEILINGR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 891 PKRqETFARISGYCEQNDIHSPQVTVKESLIYSAFLRlpkevtkyekmrfvdevmelveleslkdavvglpgitGLSTEQ 970
Cdd:cd03232 72 PLD-KNFQRSTGYVEQQDVHSPNLTVREALRFSALLR-------------------------------------GLSVEQ 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 971 RKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLLKRGGQVIYAG 1049
Cdd:cd03232 114 RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRGGKTVYFG 192
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
836-1358 |
3.15e-101 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 337.02 E-value: 3.15e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 836 KDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGY-IEGDIRISGFPKRQETFARISGYCEQNDIHSPQV 914
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 915 TVKESLIYSAFLRLPKEVTKYEKMRFVDEVMELVELESLKDAVVGLPG-ITGLSTEQRKRLTIAVELVANPSIIFMDEPT 993
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGrVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 994 SGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLLKrGGQVIYAGPLGQnshkIIEYFqAIHGVPkIKE 1073
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMA-EGRVAYLGSPDQ----AVPFF-SDLGHP-CPE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1074 KYNPATWMLEVSSMA----AEAKLEID-FAEHYKTSSLYQQNKNLVKELSTPPQG---ASDLYFSTRFSQSLLGQFKSCL 1145
Cdd:TIGR00955 268 NYNPADFYVQVLAVIpgseNESRERIEkICDSFAVSDIGRDMLVNTNLWSGKAGGlvkDSENMEGIGYNASWWTQFYALL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1146 WKQWITYWRTPDYNLARFFFTLAAAVMLGSIFWKVGTKRENANDltkVIGAMYAAVLFVGVNNSSSVQPLIAVERSVFYR 1225
Cdd:TIGR00955 348 KRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQN---INGALFLFLTNMTFQNVFPVINVFTAELPVFLR 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1226 ERAAEMYSALPYALAQVVCEIPYVLIQTTYYTLIIYAMMCFEWTLAKFFWFYFVSFMSFLYFTYYGMMTVALTPNQQVAA 1305
Cdd:TIGR00955 425 ETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMAL 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 18401096 1306 VFAGAFYGLFNLFSGFVIPRPRIPKWWIWYYWIcpvAWTVY---GLIVSQYGDVED 1358
Cdd:TIGR00955 505 TVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYL---SWFRYgneGLLINQWSDVDN 557
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
811-1049 |
2.30e-80 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 262.49 E-value: 2.30e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 811 PLTMSFDNVNYYVDmpkemkeQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGF 890
Cdd:cd03213 1 GVTLSFRNLTVTVK-------SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEVLINGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 891 PKRQETFARISGYCEQNDIHSPQVTVKESLIYSAFLRlpkevtkyekmrfvdevmelveleslkdavvglpgitGLSTEQ 970
Cdd:cd03213 74 PLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGE 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 971 RKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLLKRgGQVIYAG 1049
Cdd:cd03213 117 RKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQ-GRVIYFG 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
161-767 |
3.21e-73 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 257.28 E-value: 3.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSLKVTGRVTYNGHGLEEFVPQKTSAYISQNDVHVGVMTVQE 240
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 241 TLDFSARcqgvgtrydllselvrrekdagilpepevdLFMKSIAAGNVKSsLITDYTLRILGLDICKDTVVGDE-MIRGI 319
Cdd:TIGR00955 119 HLMFQAH------------------------------LRMPRRVTKKEKR-ERVDEVLQALGLRKCANTRIGVPgRVKGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 320 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRfTDATVLMSLLQPAPETFELFDDIILLSEGQIV 399
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQ-KGKTIICTIHQPSSELFELFDKIILMAEGRVA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 400 YQGPRDHVLTFFETCGFKCPDRKGTADFLQEVTSrkdqeqywadsKKPYSYI-SVSEFSKRFRTFHVG-ANLEKDLSVpy 477
Cdd:TIGR00955 247 YLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLA-----------VIPGSENeSRERIEKICDSFAVSdIGRDMLVNT-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 478 dRFKSHPASLVFKKHSVPKSQLFKV-CWDRELLLMKRnAFFYITKT--------VQIIIMALIASTVYLRTEmgtkNESD 548
Cdd:TIGR00955 314 -NLWSGKAGGLVKDSENMEGIGYNAsWWTQFYALLKR-SWLSVLRDplllkvrlIQTMMTAILIGLIYLGQG----LTQK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 549 GAVYIGALMFSMIVNM--FNGFAELALMIQRLPVFYKQrdllfHPPWTFSLPTFLLG-----IPISIFESVVWVTITYYM 621
Cdd:TIGR00955 388 GVQNINGALFLFLTNMtfQNVFPVINVFTAELPVFLRE-----TRSGLYRVSAYFLAktiaeLPLFIILPALFTSITYWM 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 622 IGFAPELSRFLKHLLVIFLTQQMAGGIFRFIAATCRSMILANTGGALVILLLFLLGGFIVPRGEIPKWWKWAYWVSPMAY 701
Cdd:TIGR00955 463 IGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRY 542
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18401096 702 TYDALTVNEMLAPRwiNQPSSDNSTSL-----GLAVLEIFDIFTDPnwYWIGVGGILGFTVLFNILVTLAL 767
Cdd:TIGR00955 543 GNEGLLINQWSDVD--NIECTSANTTGpcpssGEVILETLSFRNAD--LYLDLIGLVILIFFFRLLAYFAL 609
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
156-402 |
7.32e-68 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. 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: 213200 [Multi-domain] Cd Length: 202 Bit Score: 227.15 E-value: 7.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 156 KTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSLKVTGRVTYNGHGLEEF--VPQKTSAYISQNDVHV 233
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYNGIPYKEFaeKYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 234 GVMTVQETLDFSARCQGvgtrydllselvrrekdagilpepevdlfmksiaagnvksslitdytlrilgldickdtvvgD 313
Cdd:cd03233 96 PTLTVRETLDFALRCKG--------------------------------------------------------------N 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 314 EMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSLLQPAPETFELFDDIILL 393
Cdd:cd03233 114 EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDLFDKVLVL 193
|
....*....
gi 18401096 394 SEGQIVYQG 402
Cdd:cd03233 194 YEGRQIYYG 202
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
1144-1351 |
2.26e-58 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 200.19 E-value: 2.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1144 CLWKQWITYWRTPDYNLARFFFTLAAAVMLGSIFWKVGtkreNANDLTKVIGAMYAAVLFVGVNNSSSVQPLIAVERSVF 1223
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG----NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1224 YRERAAEMYSALPYALAQVVCEIPYVLIQTTYYTLIIYAMMCFEWTLAKFFWFYFVSFMSFLYFTYYGMMTVALTPNQQV 1303
Cdd:pfam01061 77 YRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFED 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 18401096 1304 AAVFAGAFYGLFNLFSGFVIPRPRIPKWWIWYYWICPVAWTVYGLIVS 1351
Cdd:pfam01061 157 ASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
811-1364 |
5.47e-57 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 210.51 E-value: 5.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 811 PLTMSFDNVNYYVDMPKEMKEQGVSKDKL----------------QLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG 874
Cdd:PLN03211 37 PITLKFMDVCYRVKFENMKNKGSNIKRILghkpkisdetrqiqerTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 875 RKTGGYIEGDIRISGFPKRQETFARIsGYCEQNDIHSPQVTVKESLIYSAFLRLPKEVTKYEKMRFVDEVMELVELESLK 954
Cdd:PLN03211 117 RIQGNNFTGTILANNRKPTKQILKRT-GFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 955 DAVVGLPGITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFD 1034
Cdd:PLN03211 196 NTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFD 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1035 ELLLLKRGgQVIYAGPLgqnsHKIIEYFQAIHGVPKIKekYNPATWMLEVSS---------------------------M 1087
Cdd:PLN03211 276 SVLVLSEG-RCLFFGKG----SDAMAYFESVGFSPSFP--MNPADFLLDLANgvcqtdgvserekpnvkqslvasyntlL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1088 AAEAKLEIDfaehykTSSLYQQNKNLVKELSTPPQGASD-LYFSTRFSQSllgqfkSCLWKQWITYWRTPDYNLARFFFT 1166
Cdd:PLN03211 349 APKVKAAIE------MSHFPQANARFVGSASTKEHRSSDrISISTWFNQF------SILLQRSLKERKHESFNTLRVFQV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1167 LAAAVMLGSIFWkvgtkRENANDLTKVIGAMYAAVLFVGVNNSSSVQPLIAVERSVFYRERAAEMYSALPYALAQVVCEI 1246
Cdd:PLN03211 417 IAAALLAGLMWW-----HSDFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDL 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1247 PYVLIQTTYYTLIIYAMMCFEWTLAKFFWFYFVSFMSFLYFTYYGMMTVALTPNQQVAAVFAGAFYGLFNLFSGFVIprP 1326
Cdd:PLN03211 492 PMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTVTMLAFVLTGGFYV--H 569
|
570 580 590
....*....|....*....|....*....|....*...
gi 18401096 1327 RIPKWWIWYYWICPVAWTVYGLIVSQYGDVEDTIKVPG 1364
Cdd:PLN03211 570 KLPSCMAWIKYISTTFYSYRLLINVQYGEGKRISSLLG 607
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
838-1049 |
7.16e-56 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 193.64 E-value: 7.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 838 KLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYI-EGDIRISGFPKRQETFARISGYCEQNDIHSPQVTV 916
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTtSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 917 KESLIYSAFLRLPKEVTKYEKmRFVDEVMELVELeslKDAVVGLPGITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 996
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIR-KKRVEDVLLRDL---ALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18401096 997 DARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLLKRGGqVIYAG 1049
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGE-IVYSG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
145-402 |
5.19e-48 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 170.04 E-value: 5.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 145 RGLRLLGFNFTKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDqSLKVTGRVTYNGHGLEEFVPQKTSA 224
Cdd:cd03213 7 RNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT-GLGVSGEVLINGRPLDKRSFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 225 YISQNDVHVGVMTVQETLDFSARCqgvgtrydllselvrrekdagilpepevdlfmksiaagnvksslitdytlrilgld 304
Cdd:cd03213 86 YVPQDDILHPTLTVRETLMFAAKL-------------------------------------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 305 ickdtvvgdemiRGISGGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQEIvRFTDATVLMSLLQPAPET 383
Cdd:cd03213 110 ------------RGLSGGERKRVSIAlELVSNPS-LLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPSSEI 175
|
250
....*....|....*....
gi 18401096 384 FELFDDIILLSEGQIVYQG 402
Cdd:cd03213 176 FELFDKLLLLSQGRVIYFG 194
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
503-709 |
3.27e-47 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 167.84 E-value: 3.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 503 CWDRELLLMKRNAFFYITKTVQIIIMALIASTVYLRTemgtKNESDGAVYIGALMFSMIVNMFNGFAELALM-IQRLPVF 581
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNL----GNQQGGLNRPGLLFFSILFNAFSALSGISPVfEKERGVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 582 YKQRDLLFHPPWTFSLPTFLLGIPISIFESVVWVTITYYMIGFAPELSRFLKHLLVIFLTQQMAGGIFRFIAATCRSMIL 661
Cdd:pfam01061 77 YRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFED 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 18401096 662 ANTGGALVILLLFLLGGFIVPRGEIPKWWKWAYWVSPMAYTYDALTVN 709
Cdd:pfam01061 157 ASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
156-402 |
1.75e-42 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 155.12 E-value: 1.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 156 KTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSLKVTGRVTYNGHGLEEFVPQKTSAYISQNDVHVGV 235
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 236 MTVQETLDFSARCQGvgtrydllselvRREKDAGIlPEPEVDlfmksiaagnvksslitdytlrILGLDICKDTVVGDEM 315
Cdd:cd03234 96 LTVRETLTYTAILRL------------PRKSSDAI-RKKRVE----------------------DVLLRDLALTRIGGNL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 316 IRGISGGQKKRVTTG-EMIVGPtKTLFMDEISTGLDSSTTYQIVKCLQEIVRfTDATVLMSLLQPAPETFELFDDIILLS 394
Cdd:cd03234 141 VKGISGGERRRVSIAvQLLWDP-KVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQPRSDLFRLFDRILLLS 218
|
....*...
gi 18401096 395 EGQIVYQG 402
Cdd:cd03234 219 SGEIVYSG 226
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
161-640 |
2.69e-37 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 150.80 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLdQSLKVTGRVTYNGHGLEEFVPQKTsAYISQNDVHVGVMTVQE 240
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRI-QGNNFTGTILANNRKPTKQILKRT-GFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 241 TLDFSARCQgvgtrydLLSELVRREKdagilpepevdlfmksiaagnvksSLITDYTLRILGLDICKDTVVGDEMIRGIS 320
Cdd:PLN03211 160 TLVFCSLLR-------LPKSLTKQEK------------------------ILVAESVISELGLTKCENTIIGNSFIRGIS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 321 GGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQEIVRfTDATVLMSLLQPAPETFELFDDIILLSEGQIV 399
Cdd:PLN03211 209 GGERKRVSIAhEMLINPS-LLILDEPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 400 YQGPRDHVLTFFETCGFKCPDRKGTADFLQEVTSRKDQEQYWADSKKP-------YSYISVseFSKRFRT-FHVGANLEK 471
Cdd:PLN03211 287 FFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANGVCQTDGVSEREKPnvkqslvASYNTL--LAPKVKAaIEMSHFPQA 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 472 DLS-VPYDRFKSHPASLV------FKKHSVPKSQLFKvcwdrelllMKRNAFFYITKTVQIIIMALIASTVYLRTEMgtk 544
Cdd:PLN03211 365 NARfVGSASTKEHRSSDRisistwFNQFSILLQRSLK---------ERKHESFNTLRVFQVIAAALLAGLMWWHSDF--- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 545 neSDGAVYIGALMF-SMIVNMFNGFAELALMIQRLPVFYKQRDLLFHPPWTFSLPTFLLGIPISIFESVVWVTITYYMIG 623
Cdd:PLN03211 433 --RDVQDRLGLLFFiSIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAG 510
|
490
....*....|....*..
gi 18401096 624 FAPELSRFLKHLLVIFL 640
Cdd:PLN03211 511 LKPELGAFLLTLLVLLG 527
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
813-1049 |
8.45e-36 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. 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: 213200 [Multi-domain] Cd Length: 202 Bit Score: 135.08 E-value: 8.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 813 TMSFDNVNYYVdmpkemkeqGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRkTGGY--IEGDIRISGF 890
Cdd:cd03233 3 TLSWRNISFTT---------GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR-TEGNvsVEGDIHYNGI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 891 PKRQ--ETFARISGYCEQNDIHSPQVTVKESLIYSAFLRlpkevtkyekmrfvdevmelveleslKDAVVglpgiTGLST 968
Cdd:cd03233 73 PYKEfaEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCK--------------------------GNEFV-----RGISG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 969 EQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVD-TGRTVVCTIHQPSIDIFEAFDELLLLkRGGQVIY 1047
Cdd:cd03233 122 GERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADvLKTTTFVSLYQASDEIYDLFDKVLVL-YEGRQIY 200
|
..
gi 18401096 1048 AG 1049
Cdd:cd03233 201 YG 202
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
832-1051 |
2.49e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.19 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFP---KRQETFARIsGYC 904
Cdd:COG1131 4 RGLTKryGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGllRPT----SGEVRVLGEDvarDPAEVRRRI-GYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 905 EQNDIHSPQVTVKESLIYSAFLRlpkEVTKYEKMRFVDEVMELVELESLKDAVVGlpgitGLSTEQRKRLTIAVELVANP 984
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVG-----TLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18401096 985 SIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKRgGQVIYAGPL 1051
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLE-EAERLCDRVAIIDK-GRIVADGTP 215
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
155-402 |
1.76e-33 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. 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: 213199 [Multi-domain] Cd Length: 192 Bit Score: 128.13 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 155 TKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSLkVTGRVTYNGHGLEE-FvpQKTSAYISQNDVHV 233
Cdd:cd03232 15 VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGV-ITGEILINGRPLDKnF--QRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 234 GVMTVQETLDFSArcqgvgtrydllselvrrekdagilpepevdlfmksiaagnvksslitdytlrilgldickdtvvgd 313
Cdd:cd03232 92 PNLTVREALRFSA------------------------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 314 eMIRGISGGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQEIVRfTDATVLMSLLQPAPETFELFDDIIL 392
Cdd:cd03232 105 -LLRGLSVEQRKRLTIGvELAAKPS-ILFLDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIHQPSASIFEKFDRLLL 181
|
250
....*....|.
gi 18401096 393 LSE-GQIVYQG 402
Cdd:cd03232 182 LKRgGKTVYFG 192
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
832-1060 |
1.81e-31 |
|
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: 124.20 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKRQETFARIS--GYCEQN 907
Cdd:COG4555 5 ENLSKkyGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD--SGSILIDGEDVRKEPREARRqiGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 908 DIHSPQVTVKESLIYSAFLRlpkEVTKYEKMRFVDEVMELVELESLKDAVVGlpgitGLSTEQRKRLTIAVELVANPSII 987
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELY---GLFDEELKKRIEELIELLGLEEFLDRRVG-----ELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18401096 988 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKRgGQVIYAGPLGQNSHKIIE 1060
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQ-EVEALCDRVVILHK-GKVVAQGSLDELREEIGE 225
|
|
| PDR_assoc |
pfam08370 |
Plant PDR ABC transporter associated; This domain is found on the C-terminus of ABC-2 type ... |
716-780 |
9.13e-30 |
|
Plant PDR ABC transporter associated; This domain is found on the C-terminus of ABC-2 type transporter domains (pfam01061). It seems to be associated with the plant pleiotropic drug resistance (PDR) protein family of ABC transporters. Like in yeast, plant PDR ABC transporters may also play a role in the transport of antifungal agents [also pfam06422]. The PDR family is characterized by a configuration in which the ABC domain is nearer the N-terminus of the protein than the transmembrane domain.
Pssm-ID: 462450 [Multi-domain] Cd Length: 65 Bit Score: 112.97 E-value: 9.13e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18401096 716 WINQPSSDNSTSLGLAVLEIFDIFTDPNWYWIGVGGILGFTVLFNILVTLALTFLNPLEKQQAVV 780
Cdd:pfam08370 1 WMKPTASNGNTTLGVAVLKSRGLFTEAYWYWIGVGALLGFTILFNILFTLALTYLNPLGKSQAII 65
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
833-1049 |
1.11e-29 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 118.06 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 833 GVSK--DKLQLLKEVTGVFRPGVlTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP--KRQETFARISGYCEQND 908
Cdd:cd03264 5 NLTKryGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPS--SGTIRIDGQDvlKQPQKLRRRIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 909 IHSPQVTVKESLIYSAFLrlpKEVTKYEKMRFVDEVMELVELESLKDAVVGlpgitGLSTEQRKRLTIAVELVANPSIIF 988
Cdd:cd03264 82 GVYPNFTVREFLDYIAWL---KGIPSKEVKARVDEVLELVNLGDRAKKKIG-----SLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18401096 989 MDEPTSGLDArAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKrGGQVIYAG 1049
Cdd:cd03264 154 VDEPTAGLDP-EERIRFRNLLSELGEDRIVILSTHIVE-DVESLCNQVAVLN-KGKLVFEG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
849-1049 |
1.09e-28 |
|
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: 115.29 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 849 FRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyiegDIRISGFPKRQETFA--RISGYCEQNDIHSPQVTVKESLIYSA 924
Cdd:cd03263 25 VYKGEIFGLLGHNGAGKTTTLKMLTGelRPTSG----TAYINGYSIRTDRKAarQSLGYCPQFDALFDELTVREHLRFYA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 925 FLR-LPKEVTKYEkmrfVDEVMELVELESLKDAVVGlpgitGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1003
Cdd:cd03263 101 RLKgLPKSEIKEE----VELLLRVLGLTDKANKRAR-----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18401096 1004 VMRTVrNTVDTGRTVVCTIHqpSIDIFEAF-DELLLLKRgGQVIYAG 1049
Cdd:cd03263 172 IWDLI-LEVRKGRSIILTTH--SMDEAEALcDRIAIMSD-GKLRCIG 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
840-1042 |
2.33e-28 |
|
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: 114.10 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 840 QLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKtgGYIEGDIRISGFPKRQET---FARISGYCEQNdihsPQV-- 914
Cdd:cd03225 15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL--GPTSGEVLVDGKDLTKLSlkeLRRKVGLVFQN----PDDqf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 915 ---TVKESLIYSA-FLRLPKEVTKyekmRFVDEVMELVELESLKDAVvglpgITGLSTEQRKRLTIAVELVANPSIIFMD 990
Cdd:cd03225 89 fgpTVEEEVAFGLeNLGLPEEEIE----ERVEEALELVGLEGLRDRS-----PFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18401096 991 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKRG 1042
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDG 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
842-1050 |
1.16e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.26 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKRQETfARIsGYCEQN---DIHSPqVTV 916
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGllPPT----SGTVRLFGKPPRRAR-RRI-GYVPQRaevDWDFP-ITV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 917 KEsLIYS-------AFLRLPKEvtkyEKMRfVDEVMELVELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANPSIIFM 989
Cdd:COG1121 95 RD-VVLMgrygrrgLFRRPSRA----DREA-VDEALERVGLEDLADRPIGE-----LSGGQQQRVLLARALAQDPDLLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18401096 990 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLLKRGgqVIYAGP 1050
Cdd:COG1121 164 DEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRG--LVAHGP 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
828-1042 |
1.76e-27 |
|
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: 109.64 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 828 EMKEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKRQetfarisgyceqn 907
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK--PTSGEILIDGKDIAK------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 908 dihspqvtvkesliysaflrlpkevtkyekmrfvdevmelVELESLKDAVVGLPGitgLSTEQRKRLTIAVELVANPSII 987
Cdd:cd00267 66 ----------------------------------------LPLEELRRRIGYVPQ---LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18401096 988 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKRG 1042
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPE-LAELAADRVIVLKDG 156
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
842-1049 |
1.79e-27 |
|
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: 111.47 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKRQETfARIsGYCEQN---DIHSPqVTV 916
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGllKPT----SGSIRVFGKPLEKER-KRI-GYVPQRrsiDRDFP-ISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 917 KESL---IYSaFLRLPKEVTKYEKMRfVDEVMELVELESLKDAvvglpGITGLSTEQRKRLTIAVELVANPSIIFMDEPT 993
Cdd:cd03235 88 RDVVlmgLYG-HKGLFRRLSKADKAK-VDEALERVGLSELADR-----QIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 18401096 994 SGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLLKRGgqVIYAG 1049
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT--VVASG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
837-1050 |
1.99e-27 |
|
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: 112.04 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 837 DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKRQETFARIS---GYCEQN-D-- 908
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGllKPT----SGEVLVDGKDITKKNLRELRrkvGLVFQNpDdq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 909 IHSPqvTVKESLiysAF----LRLPKEvtkyEKMRFVDEVMELVELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANP 984
Cdd:COG1122 88 LFAP--TVEEDV---AFgpenLGLPRE----EIRERVEEALELVGLEHLADRPPHE-----LSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18401096 985 SIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKRgGQVIYAGP 1050
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLD-LVAELADRVIVLDD-GRIVADGT 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
834-1050 |
1.09e-26 |
|
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: 110.52 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 834 VSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKRQetFARISGYCEQNDIH 910
Cdd:COG1120 9 VGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGllKPSSGEVLlDGRDLASLSRRE--LARRIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 911 SPQVTVKESLI-----YSAFLRLPKEvtkyEKMRFVDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVANPS 985
Cdd:COG1120 87 PFGLTVRELVAlgrypHLGLFGRPSA----EDREAVEEALERTGLEHLADRPV-----DELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 986 IIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIdifeAF---DELLLLKrGGQVIYAGP 1050
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHDLNL----AAryaDRLVLLK-DGRIVAQGP 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
833-1025 |
1.57e-23 |
|
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: 99.86 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 833 GVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKRQ--ETFARISGYCEQND 908
Cdd:COG4133 9 SCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGllPPS----AGEVLWNGEPIRDarEDYRRRLAYLGHAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 909 IHSPQVTVKESL-IYSAFLRLPKEVTKyekmrfVDEVMELVELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANPSII 987
Cdd:COG4133 85 GLKPELTVRENLrFWAALYGLRADREA------IDEALEAVGLAGLADLPVRQ-----LSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 18401096 988 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQP 1025
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
842-994 |
2.24e-23 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 97.72 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISG--FPKRQETFARIS-GYCEQNDIHSPQVTVKE 918
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS--PTEGTILLDGqdLTDDERKSLRKEiGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18401096 919 SLIYSAFLRLPKevTKYEKMRfVDEVMELVELESLKDAVVGLPGITgLSTEQRKRLTIAVELVANPSIIFMDEPTS 994
Cdd:pfam00005 79 NLRLGLLLKGLS--KREKDAR-AEEALEKLGLGDLADRPVGERPGT-LSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
833-1049 |
1.19e-22 |
|
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: 96.74 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 833 GVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG-RKTGGyieGDIRISGFP----KRQEtFARISGYCEQn 907
Cdd:cd03214 6 SVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGlLKPSS---GEILLDGKDlaslSPKE-LARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 908 dihspqvtvkesliysaflrlpkevtkyekmrfvdeVMELVELESLKDAvvglpGITGLSTEQRKRLTIAVELVANPSII 987
Cdd:cd03214 81 ------------------------------------ALELLGLAHLADR-----PFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18401096 988 FMDEPTSGLDARAAAIVMRTVRNTVD-TGRTVVCTIHQPSIdIFEAFDELLLLKrGGQVIYAG 1049
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNL-AARYADRVILLK-DGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
832-1042 |
1.30e-22 |
|
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: 96.31 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFP--KRQETFARISGYCE 905
Cdd:cd03230 4 RNLSKryGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGllKPD----SGEIKVLGKDikKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 906 QNDIHSPQVTVKESLIYSaflrlpkevtkyekmrfvdevmelveleslkdavvglpgiTGlsteQRKRLTIAVELVANPS 985
Cdd:cd03230 80 EEPSLYENLTVRENLKLS----------------------------------------GG----MKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 18401096 986 IIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKRG 1042
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNG 171
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
828-1051 |
2.46e-22 |
|
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: 97.85 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 828 EMKEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGyieGDIRISGFPKRQETF----ARIs 901
Cdd:COG1119 5 ELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpPTYG---NDVRLFGERRGGEDVwelrKRI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 902 GYCeQNDIH---SPQVTVKESLIySAF---LRLPKEVTKYEKMRfVDEVMELVELESLKDAVVGlpgitGLSTEQRKRLT 975
Cdd:COG1119 81 GLV-SPALQlrfPRDETVLDVVL-SGFfdsIGLYREPTDEQRER-ARELLELLGLAHLADRPFG-----TLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 976 IAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTvvcTI----HQPSiDIFEAFDELLLLKRgGQVIYAGPL 1051
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAP---TLvlvtHHVE-EIPPGITHVLLLKD-GRVVAAGPK 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
836-1045 |
4.32e-22 |
|
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: 95.79 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 836 KDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISGFPKRQETfariSGYCEQN-DIHSP 912
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGliKESSGSILLNGKPIKAKERRKS----IGYVMQDvDYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 913 QVTVKESLIYSAfLRLPKEVTKyekmrfVDEVMELVELESLKDAvvgLPgiTGLSTEQRKRLTIAVELVANPSIIFMDEP 992
Cdd:cd03226 86 TDSVREELLLGL-KELDAGNEQ------AETVLKDLDLYALKER---HP--LSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18401096 993 TSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLLKRGGQV 1045
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHDYEF-LAKVCDRVLLLANGAIV 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
832-1042 |
7.48e-22 |
|
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: 95.63 E-value: 7.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK------DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKRQETFAR--- 899
Cdd:cd03255 4 KNLSKtyggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldRPTSGEVRvDGTDISKLSEKELAAFRrrh 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 900 IsGYCEQNdiHS--PQVTVKESLIYSAFLRlpkEVTKYEKMRFVDEVMELVELESLKDAVVGlpgitGLSTEQRKRLTIA 977
Cdd:cd03255 84 I-GFVFQS--FNllPDLTALENVELPLLLA---GVPKKERRERAEELLERVGLGDRLNHYPS-----ELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18401096 978 VELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHQPsiDIFEAFDELLLLKRG 1042
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDP--ELAEYADRIIELRDG 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
829-1042 |
1.41e-21 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 94.51 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 829 MKEQGVSKD--KLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKRQetfaRISGY 903
Cdd:cd03259 1 LELKGLSKTygSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPDSGEILiDGRDVTGVPPER----RNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 904 CEQNDIHSPQVTVKESLiysAF-LRLpKEVTKYEKMRFVDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVA 982
Cdd:cd03259 77 VFQDYALFPHLTVAENI---AFgLKL-RGVPKAEIRARVRELLELVGLEGLLNRYP-----HELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18401096 983 NPSIIFMDEPTSGLDARAAAIVMRTVRNT-VDTGRTVVCTIHqpsiDIFEAF---DELLLLKRG 1042
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTH----DQEEALalaDRIAVMNEG 207
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
832-1047 |
3.71e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. 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: 213236 [Multi-domain] Cd Length: 210 Bit Score: 93.11 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSKD--KLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGrktggyI----EGDIRISGFPKRQETFARIsGYCE 905
Cdd:cd03269 4 ENVTKRfgRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILG------IilpdSGEVLFDGKPLDIAARNRI-GYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 906 QNDIHSPQVTVKESLIYSAFLrlpKEVTKYEKMRFVDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVANPS 985
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQL---KGLKKEEARRRIDEWLERLELSEYANKRV-----EELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18401096 986 IIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAF-DELLLLKRGGQVIY 1047
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQ--MELVEELcDRVLLLNKGRAVLY 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
745-1050 |
4.72e-21 |
|
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: 99.91 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 745 YWIGVGGILG--FT----VLFNILVTLaltFLNPLEK--------QQAVVSKE------NTEENRaENGSKSKSIDVKRG 804
Cdd:COG2274 397 LWLGAYLVIDgqLTlgqlIAFNILSGR---FLAPVAQligllqrfQDAKIALErlddilDLPPER-EEGRSKLSLPRLKG 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 805 MVlpftpltmSFDNVNYyvdmpkemkeqGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGrktgGYI--E 882
Cdd:COG2274 473 DI--------ELENVSF-----------RYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG----LYEptS 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 883 GDIRISGFPKRQ---ETFARISGYCEQND-IHSPqvTVKESLIYSAflrlpKEVTKyekmrfvDEVMELVELESLKDAVV 958
Cdd:COG2274 530 GRILIDGIDLRQidpASLRRQIGVVLQDVfLFSG--TIRENITLGD-----PDATD-------EEIIEAARLAGLHDFIE 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 959 GLP-GI--------TGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSidI 1029
Cdd:COG2274 596 ALPmGYdtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLR-RLLKGRTVIIIAHRLS--T 672
|
330 340
....*....|....*....|.
gi 18401096 1030 FEAFDELLLLKRgGQVIYAGP 1050
Cdd:COG2274 673 IRLADRIIVLDK-GRIVEDGT 692
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
153-408 |
2.14e-20 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 91.66 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 153 NFTKT-TKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEE----------FVPQK 221
Cdd:COG1131 5 GLTKRyGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT---SGEVRVLGEDVARdpaevrrrigYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 222 TSAYisqndvhvGVMTVQETLDFSARCQGvgtrydlLSELVRREKdagilpepevdlfmksiaagnvkssliTDYTLRIL 301
Cdd:COG1131 82 PALY--------PDLTVRENLRFFARLYG-------LPRKEARER---------------------------IDELLELF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 302 GLDICKDTvvgdeMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRfTDATVLMS--LLqp 379
Cdd:COG1131 120 GLTDAADR-----KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSthYL-- 191
|
250 260
....*....|....*....|....*....
gi 18401096 380 aPETFELFDDIILLSEGQIVYQGPRDHVL 408
Cdd:COG1131 192 -EEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
829-1042 |
4.31e-20 |
|
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: 89.17 E-value: 4.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 829 MKEQGVSKD--KLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKRQETFARISGY 903
Cdd:cd03229 1 LELKNVSKRygQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGleEPDSGSILiDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 904 CEQNDIHSPQVTVKESLIYsaflrlpkevtkyekmrfvdevmelveleslkdavvglpgitGLSTEQRKRLTIAVELVAN 983
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL------------------------------------------GLSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18401096 984 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHqpsiDIFEAF---DELLLLKRG 1042
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTH----DLDEAArlaDRVVVLRDG 177
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
832-1050 |
2.31e-19 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 88.78 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK---DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKRQETFARI-SGYC 904
Cdd:cd03256 4 ENLSKtypNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlvEPTSGSVLiDGTDINKLKGKALRQLRRqIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 905 EQNDIHSPQVTVKE-----SLIYSAFLR-LPKEVTKYEKMRFVdEVMELVELESLKDAVVGLpgitgLSTEQRKRLTIAV 978
Cdd:cd03256 84 FQQFNLIERLSVLEnvlsgRLGRRSTWRsLFGLFPKEEKQRAL-AALERVGLLDKAYQRADQ-----LSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18401096 979 ELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSIdIFEAFDELLLLKRgGQVIYAGP 1050
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDL-AREYADRIVGLKD-GRIVFDGP 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
156-406 |
2.55e-19 |
|
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: 88.33 E-value: 2.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 156 KTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLeefVPQKTSA-----YISQND 230
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT---SGTAYINGYSI---RTDRKAArqslgYCPQFD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 231 VHVGVMTVQETLDFSARCQGVgtrydllselvrREKDAgilpepevdlfmksiaagnvksSLITDYTLRILGLDICKDTV 310
Cdd:cd03263 85 ALFDELTVREHLRFYARLKGL------------PKSEI----------------------KEEVELLLRVLGLTDKANKR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 311 VGDemirgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRftDATVLMSLLQPApETFELFDDI 390
Cdd:cd03263 131 ART-----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMD-EAEALCDRI 202
|
250
....*....|....*.
gi 18401096 391 ILLSEGQIVYQGPRDH 406
Cdd:cd03263 203 AIMSDGKLRCIGSPQE 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
836-1049 |
2.68e-19 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 88.19 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 836 KDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGD-IRISGFPkrQETFARIsGYCEQNDIHSP 912
Cdd:cd03266 15 KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGllEPDAGFATVDgFDVVKEP--AEARRRL-GFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 913 QVTVKESLIYsaFLRL----PKEVTKYekmrfVDEVMELVELESLKDAVVGlpgitGLSTEQRKRLTIAVELVANPSIIF 988
Cdd:cd03266 92 RLTARENLEY--FAGLyglkGDELTAR-----LEELADRLGMEELLDRRVG-----GFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18401096 989 MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKRgGQVIYAG 1049
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHR-GRVVYEG 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
832-1053 |
5.16e-19 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 87.94 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEGDIRISGFPKRQETFARISGYCE 905
Cdd:cd03261 4 RGLTKsfGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGllRPDSGevLIDGEDISGLSEAELYRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 906 Q-----NDIhspqvTVKESLiysAF-LRlpkevtkyEKMRFVDEVMElvELESLKDAVVGLPGI-----TGLSTEQRKRL 974
Cdd:cd03261 84 QsgalfDSL-----TVFENV---AFpLR--------EHTRLSEEEIR--EIVLEKLEAVGLRGAedlypAELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 975 TIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHQPSiDIFEAFDELLLLKRgGQVIYAGPLGQ 1053
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLD-TAFAIADRIAVLYD-GKIVAEGTPEE 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
832-1019 |
7.05e-19 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 87.49 E-value: 7.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEGDiRISGFPKRQ-------ETFa 898
Cdd:cd03219 4 RGLTKrfGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGflRPTSGsvLFDGE-DITGLPPHEiarlgigRTF- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 899 risgyceQNdihsPQV----TVKESLIYSAFLRLP------KEVTKYEKMR-FVDEVMELVELESLKDAVVGLpgitgLS 967
Cdd:cd03219 82 -------QI----PRLfpelTVLENVMVAAQARTGsglllaRARREEREAReRAEELLERVGLADLADRPAGE-----LS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18401096 968 TEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVV 1019
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVL 197
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
837-1023 |
1.43e-18 |
|
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: 85.17 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 837 DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISGFPKRQETFARIS-GYCEQN---DIH 910
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGllRPQSGAVLIDGEPLDYSRKGLLERRQRvGLVFQDpddQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 911 SPqvTVKESLIYSAF-LRLPKEvtkyEKMRFVDEVMELVELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANPSIIFM 989
Cdd:TIGR01166 83 AA--DVDQDVAFGPLnLGLSEA----EVERRVREALTAVGASGLRERPTHC-----LSGGEKKRVAIAGAVAMRPDVLLL 151
|
170 180 190
....*....|....*....|....*....|....
gi 18401096 990 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1023
Cdd:TIGR01166 152 DEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
841-1050 |
1.52e-18 |
|
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: 91.37 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 841 LLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGrktggYIE---GDIRISGFPKRQ---ETFARISGYCEQNdihsPQV 914
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR-----FLDpqsGSITLGGVDLRDldeDDLRRRIAVVPQR----PHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 915 ---TVKESLiysaflRLPK-EVTKyEKMRfvdEVMELVEL----ESLK---DAVVGlPGITGLSTEQRKRLTIAVELVAN 983
Cdd:COG4987 421 fdtTLRENL------RLARpDATD-EELW---AALERVGLgdwlAALPdglDTWLG-EGGRRLSGGERRRLALARALLRD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18401096 984 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPSidIFEAFDELLLLKRgGQVIYAGP 1050
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLA--GLERMDRILVLED-GRIVEQGT 552
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
832-1042 |
3.45e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 85.10 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSKD------KLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKRQETFAR--- 899
Cdd:COG1136 8 RNLTKSygtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGldRPTSGEVLiDGQDISSLSERELARLRrrh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 900 IsGYCEQnDIH-SPQVTVKESLIYSAFLRlpkEVTKYEKMRFVDEVMELVELESLKDAvvgLPGItgLSTEQRKRLTIAV 978
Cdd:COG1136 88 I-GFVFQ-FFNlLPELTALENVALPLLLA---GVSRKERRERARELLERVGLGDRLDH---RPSQ--LSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18401096 979 ELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHQPsiDIFEAFDELLLLKRG 1042
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDP--ELAARADRVIRLRDG 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
851-1049 |
4.69e-18 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 84.27 E-value: 4.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 851 PGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISgFPKRQETF----ARISGYCEQNDIHSPQVTVKESLIYSA 924
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGleKPDGGTIVLNGTVL-FDSRKKINlppqQRKIGLVFQQYALFPHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 925 flrlpKEVTKYEKMRFVDEVMELVELESLKDAvvglpGITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1004
Cdd:cd03297 101 -----KRKRNREDRISVDELLDLLGLDHLLNR-----YPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18401096 1005 MRTVRNTV-DTGRTVVCTIHQPSidifEAF---DELLLLkRGGQVIYAG 1049
Cdd:cd03297 171 LPELKQIKkNLNIPVIFVTHDLS----EAEylaDRIVVM-EDGRLQYIG 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
832-1092 |
6.13e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.93 E-value: 6.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGrktggyI----EGDIRISGFPKRQETFARIsGYC- 904
Cdd:COG4152 5 KGLTKrfGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILG------IlapdSGEVLWDGEPLDPEDRRRI-GYLp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 905 EQNDIHsPQVTVKESLIYsaFLRLpKEVTKYEKMRFVDEVMELVELESLKDAVVGlpgitGLS-TEQRKrLTIAVELVAN 983
Cdd:COG4152 78 EERGLY-PKMKVGEQLVY--LARL-KGLSKAEAKRRADEWLERLGLGDRANKKVE-----ELSkGNQQK-VQLIAALLHD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 984 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAF-DELLLLKRgGQVIYAGPLGQnshkiieyf 1062
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ--MELVEELcDRIVIINK-GRKVLSGSVDE--------- 215
|
250 260 270
....*....|....*....|....*....|
gi 18401096 1063 qaihgvpkIKEKYNPATWMLEVSSMAAEAK 1092
Cdd:COG4152 216 --------IRRQFGRNTLRLEADGDAGWLR 237
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
832-1024 |
6.52e-18 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 83.81 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSKD--KLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEgdIRISGFPKRQETFARISGYCEQN 907
Cdd:cd03268 4 NDLTKTygKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGliKPDSGEIT--FDGKSYQKNIEALRRIGALIEAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 908 DIHsPQVTVKESLIYSA-FLRLPKEVtkyekmrfVDEVMELVELESLKDAVVGlpgitGLSTEQRKRLTIAVELVANPSI 986
Cdd:cd03268 82 GFY-PNLTARENLRLLArLLGIRKKR--------IDEVLDVVGLKDSAKKKVK-----GFSLGMKQRLGIALALLGNPDL 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 18401096 987 IFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1024
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHL 185
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
842-1023 |
1.29e-17 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. 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: 213232 [Multi-domain] Cd Length: 220 Bit Score: 83.19 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyiegDIRISGFPKRQETF---ARIsGYCEQNDIHSPQVTV 916
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTllKPTSG----RATVAGHDVVREPRevrRRI-GIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 917 KESL-IYSAFLRLPKEVTKyekmRFVDEVMELVELESLKDAVVGlpgitGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 995
Cdd:cd03265 91 WENLyIHARLYGVPGAERR----ERIDELLDFVGLLEAADRLVK-----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180
....*....|....*....|....*....
gi 18401096 996 LDARAAAIVMRTVRNTVDT-GRTVVCTIH 1023
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEEfGMTILLTTH 190
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
850-1023 |
2.04e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 850 RPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP-KRQETFARIS-GYCEQNDIHSPQVTVKESL-IYSAFL 926
Cdd:PRK13537 31 QRGECFGLLGPNGAGKTTTLRMLLGLTHPD--AGSISLCGEPvPSRARHARQRvGVVPQFDNLDPDFTVRENLlVFGRYF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 927 RLPKEVTKyekmRFVDEVMELVELESLKDAVVGlpgitGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMR 1006
Cdd:PRK13537 109 GLSAAAAR----ALVPPLLEFAKLENKADAKVG-----ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
170
....*....|....*..
gi 18401096 1007 TVRNTVDTGRTVVCTIH 1023
Cdd:PRK13537 180 RLRSLLARGKTILLTTH 196
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
810-1049 |
2.46e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 87.51 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 810 TPLTMSFDNVNYyvdmpkemkeqgVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISG 889
Cdd:COG4988 333 GPPSIELEDVSF------------SYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP--YSGSILING 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 890 FPKRQETFARIS---GYCEQNDiHSPQVTVKESliysafLRLPK-EVTKyekmrfvDEVMELVELESLKDAVVGLPGitG 965
Cdd:COG4988 399 VDLSDLDPASWRrqiAWVPQNP-YLFAGTIREN------LRLGRpDASD-------EELEAALEAAGLDEFVAALPD--G 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 966 LSTE-----------QRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQPSIDifEAFD 1034
Cdd:COG4988 463 LDTPlgeggrglsggQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR-LAKGRTVILITHRLALL--AQAD 539
|
250
....*....|....*
gi 18401096 1035 ELLLLkRGGQVIYAG 1049
Cdd:COG4988 540 RILVL-DDGRIVEQG 553
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
159-408 |
2.64e-17 |
|
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: 82.98 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 159 KVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEE----------FVPQKTSAYisq 228
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD---SGSILIDGEDVRKeprearrqigVLPDERGLY--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 229 ndvhvGVMTVQETLDFSARcqgvgtrydlLSELVRREKDAGIlpepevdlfmksiaagnvksslitDYTLRILGLDICKD 308
Cdd:COG4555 87 -----DRLTVRENIRYFAE----------LYGLFDEELKKRI------------------------EELIELLGLEEFLD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 309 TVVGdemirGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIvRFTDATVLMS--LLQpapETFEL 386
Cdd:COG4555 128 RRVG-----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSshIMQ---EVEAL 198
|
250 260
....*....|....*....|..
gi 18401096 387 FDDIILLSEGQIVYQGPRDHVL 408
Cdd:COG4555 199 CDRVVILHKGKVVAQGSLDELR 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
147-409 |
3.31e-17 |
|
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: 86.50 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 147 LRLLGFNFTKTTkVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSLKVTGRVTYNGH---GLEEFVPQKTS 223
Cdd:COG1123 7 VRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRdllELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 224 AYISQN-DVHVGVMTVQETLDFSARCQGVGTRydllsELVRREKDAgilpepevdlfmksiaagnvksslitdytLRILG 302
Cdd:COG1123 86 GMVFQDpMTQLNPVTVGDQIAEALENLGLSRA-----EARARVLEL-----------------------------LEAVG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 303 LDickdtVVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSLLQPApE 382
Cdd:COG1123 132 LE-----RRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLG-V 205
|
250 260
....*....|....*....|....*..
gi 18401096 383 TFELFDDIILLSEGQIVYQGPRDHVLT 409
Cdd:COG1123 206 VAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
850-1023 |
3.38e-17 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 83.98 E-value: 3.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 850 RPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYiegdirisgfpkrqetfARISGYceqnDIHSPQVTVKESL-----IY 922
Cdd:TIGR01188 17 REGEVFGFLGPNGAGKTTTIRMLTTllRPTSGT-----------------ARVAGY----DVVREPRKVRRSIgivpqYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 923 SAFLRLPKE-----------VTKYEKMRFVDEVMELVELESLKDAVVGlpgitGLSTEQRKRLTIAVELVANPSIIFMDE 991
Cdd:TIGR01188 76 SVDEDLTGRenlemmgrlygLPKDEAEERAEELLELFELGEAADRPVG-----TYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190
....*....|....*....|....*....|..
gi 18401096 992 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1023
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRALKEEGVTILLTTH 182
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
163-344 |
5.37e-17 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 79.23 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 163 LRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDqslKVTGRVTYNGHGL---EEFVPQKTSAYISQNDVHVGVMTVQ 239
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS---PTEGTILLDGQDLtddERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 240 ETLDFSARCQGVGtrydllselvRREKDAgilpepEVDLFMKSiaagnvksslitdytlriLGLDICKDTVVGDEMiRGI 319
Cdd:pfam00005 78 ENLRLGLLLKGLS----------KREKDA------RAEEALEK------------------LGLGDLADRPVGERP-GTL 122
|
170 180
....*....|....*....|....*
gi 18401096 320 SGGQKKRVTTGEMIVGPTKTLFMDE 344
Cdd:pfam00005 123 SGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
852-1027 |
8.51e-17 |
|
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: 80.91 E-value: 8.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAGRK--TGGYIE-GDIRISGFPKRQETFARIS-GYCEQNDIHSPQVTVKESLIYSafLR 927
Cdd:cd03292 27 GEFVFLVGPSGAGKSTLLKLIYKEElpTSGTIRvNGQDVSDLRGRAIPYLRRKiGVVFQDFRLLPDRNVYENVAFA--LE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 928 L----PKEVTKYekmrfVDEVMELVELESLKDAvvgLPgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1003
Cdd:cd03292 105 VtgvpPREIRKR-----VPAALELVGLSHKHRA---LP--AELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180
....*....|....*....|....
gi 18401096 1004 VMRTVRNTVDTGRTVVCTIHQPSI 1027
Cdd:cd03292 175 IMNLLKKINKAGTTVVVATHAKEL 198
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
842-1096 |
9.15e-17 |
|
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: 85.34 E-value: 9.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGR-KTGGYIEGDIRISGFPKRQETFARIS---GYCEQNDIHS--PqVT 915
Cdd:COG1123 22 VDGVSLTIAPGETVALVGESGSGKSTLALALMGLlPHGGRISGEVLLDGRDLLELSEALRGrriGMVFQDPMTQlnP-VT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 916 VKESLiysAFLRLPKEVTKYEKMRFVDEVMELVELESLKDAvvglpGITGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 995
Cdd:COG1123 101 VGDQI---AEALENLGLSRAEARARVLELLEAVGLERRLDR-----YPHQLSGGQRQRVAIAMALALDPDLLIADEPTTA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 996 LDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSiDIFEAFDELLLLKRgGQVIYAGPLGQnshkIIEYFQAIHGVPkikeK 1074
Cdd:COG1123 173 LDVTTQAEILDLLRElQRERGTTVLLITHDLG-VVAEIADRVVVMDD-GRIVEDGPPEE----ILAAPQALAAVP----R 242
|
250 260
....*....|....*....|..
gi 18401096 1075 YNPATWMLEVSSMAAEAKLEID 1096
Cdd:COG1123 243 LGAARGRAAPAAAAAEPLLEVR 264
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
842-1025 |
9.30e-17 |
|
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: 85.49 E-value: 9.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPkrQETFARISGYCEQnDIHSPQVTVKE 918
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlldPLQGEVTLDGVPVSSLD--QDEVRRRVSVCAQ-DAHLFDTTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 919 SLIYSAflrlpKEVTKyekmrfvDEVMELVELESLKDAVVGLPGitGLSTE-----------QRKRLTIAVELVANPSII 987
Cdd:TIGR02868 428 NLRLAR-----PDATD-------EELWAALERVGLADWLRALPD--GLDTVlgeggarlsggERQRLALARALLADAPIL 493
|
170 180 190
....*....|....*....|....*....|....*...
gi 18401096 988 FMDEPTSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQP 1025
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
835-1019 |
1.24e-16 |
|
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: 84.95 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 835 SKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKRQ-ETFARISGYCEQNDIH 910
Cdd:COG1123 274 GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGllRPTSGSILfDGKDLTKLSRRSlRELRRRVQMVFQDPYS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 911 S--PQVTVKESLIYSafLRLPKEVTKYEKMRFVDEVMELVEL-ESLKDAvvgLPGitGLSTEQRKRLTIAVELVANPSII 987
Cdd:COG1123 354 SlnPRMTVGDIIAEP--LRLHGLLSRAERRERVAELLERVGLpPDLADR---YPH--ELSGGQRQRVAIARALALEPKLL 426
|
170 180 190
....*....|....*....|....*....|...
gi 18401096 988 FMDEPTSGLDARAAAIVMRTVRNTVD-TGRTVV 1019
Cdd:COG1123 427 ILDEPTSALDVSVQAQILNLLRDLQReLGLTYL 459
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
814-1042 |
2.03e-16 |
|
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: 78.19 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 814 MSFDNVNY-YVDMPKemkeqgvskdklQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGF 890
Cdd:cd03228 1 IEFKNVSFsYPGRPK------------PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRlyDPT----SGEILIDGV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 891 PKRQ---ETFARISGYCEQndihspqvtvkESLIYSAflrlpkevtkyekmrfvdevmelveleSLKDAVvglpgitgLS 967
Cdd:cd03228 65 DLRDldlESLRKNIAYVPQ-----------DPFLFSG---------------------------TIRENI--------LS 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18401096 968 TEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQPSidIFEAFDELLLLKRG 1042
Cdd:cd03228 99 GGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRA-LAKGKTVIVIAHRLS--TIRDADRIIVLDDG 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
816-1045 |
2.07e-16 |
|
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: 79.94 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 816 FDNVNYYVDmpkEMKEQGVSKDKLQllkevtgvFRPGVLTALMGVSGAGKTTLMDVLAGRktggYI--EGDIRISGFPKR 893
Cdd:cd03245 5 FRNVSFSYP---NQEIPALDNVSLT--------IRAGEKVAIIGRVGSGKSTLLKLLAGL----YKptSGSVLLDGTDIR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 894 Q----ETFARIsGYCEQnDIHSPQVTVKESLIYSAflrlpkevtkyekmRFVD--EVMELVELESLKDAVVGLP------ 961
Cdd:cd03245 70 QldpaDLRRNI-GYVPQ-DVTLFYGTLRDNITLGA--------------PLADdeRILRAAELAGVTDFVNKHPngldlq 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 962 ---GITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVdTGRTVVCTIHQPSIDifEAFDELLL 1038
Cdd:cd03245 134 igeRGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLL--DLVDRIIV 210
|
....*..
gi 18401096 1039 LKRGGQV 1045
Cdd:cd03245 211 MDSGRIV 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
832-1004 |
3.35e-16 |
|
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: 79.53 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKRQETFARIS----- 901
Cdd:cd03260 4 RDLNVyyGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndLIPGAPDEGEVLLDGKDIYDLDVDVLElrrrv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 902 GYCEQndihSPQV---TVKESLIYSafLRLPKEVTKYEKMRFVDEVMELVEL-ESLKDAVVGLpgitGLSTEQRKRLTIA 977
Cdd:cd03260 84 GMVFQ----KPNPfpgSIYDNVAYG--LRLHGIKLKEELDERVEEALRKAALwDEVKDRLHAL----GLSGGQQQRLCLA 153
|
170 180
....*....|....*....|....*..
gi 18401096 978 VELVANPSIIFMDEPTSGLDARAAAIV 1004
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKI 180
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
832-1050 |
3.41e-16 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 79.64 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFP--KRQETFARIsGYC 904
Cdd:COG1127 9 RNLTKsfGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGllRPDSGEILvDGQDITGLSekELYELRRRI-GML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 905 EQN-----DIhspqvTVKESLiysAF-LR----LPKEvtkyEKMRFVDEVMELVELESLKDAvvgLPGitGLSTEQRKRL 974
Cdd:COG1127 88 FQGgalfdSL-----TVFENV---AFpLRehtdLSEA----EIRELVLEKLELVGLPGAADK---MPS--ELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 975 TIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHqpsiDIFEAF---DELLLLKRgGQVIYAGP 1050
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTH----DLDSAFaiaDRVAVLAD-GKIIAEGT 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
842-1027 |
4.01e-16 |
|
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: 83.49 E-value: 4.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKRQETFA---RISGYCEQNDiHSPQVTVKE 918
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT--EGSIAVNGVPLADADADswrDQIAWVPQHP-FLFAGTIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 919 SLiysaflRLpkevtkYEKMRFVDEVMELVELESLKDAVVGLP-GI--------TGLSTEQRKRLTIAVELVANPSIIFM 989
Cdd:TIGR02857 415 NI------RL------ARPDASDAEIREALERAGLDEFVAALPqGLdtpigeggAGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190
....*....|....*....|....*....|....*...
gi 18401096 990 DEPTSGLDARAAAIVMRTVRNtVDTGRTVVCTIHQPSI 1027
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRA-LAQGRTVLLVTHRLAL 519
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
852-1049 |
5.48e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 78.91 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGF-P-KRQETF-ARISGYCEQNDIHSPQVTVKESLiysafl 926
Cdd:cd03267 47 GEIVGFIGPNGAGKTTTLKILSGllQPT----SGEVRVAGLvPwKRRKKFlRRIGVVFGQKTQLWWDLPVIDSF------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 927 RLPKEVTKYEKMRF---VDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1003
Cdd:cd03267 117 YLLAAIYDLPPARFkkrLDELSELLDLEELLDTPV-----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18401096 1004 VMRTVRNTV-DTGRTVVCTIHQPSiDIfEAFDELLLLKRGGQVIYAG 1049
Cdd:cd03267 192 IRNFLKEYNrERGTTVLLTSHYMK-DI-EALARRVLVIDKGRLLYDG 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
842-1042 |
6.90e-16 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. 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: 213221 [Multi-domain] Cd Length: 229 Bit Score: 78.42 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLagrkTGGYI--EGDIRISGFPKRQETFARIS---GYCEQnDIHSPQVTV 916
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLL----MRFYDpqKGQILIDGIDIRDISRKSLRsmiGVVLQ-DTFLFSGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 917 KESLIYSAFLRLPKEVTKYEK-MRFVDEVMELvelESLKDAVVGlPGITGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 995
Cdd:cd03254 94 MENIRLGRPNATDEEVIEAAKeAGAHDFIMKL---PNGYDTVLG-ENGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18401096 996 LDARAAAIVMRTVRNTVDtGRTVVCTIHQPSIdIFEAfDELLLLKRG 1042
Cdd:cd03254 170 IDTETEKLIQEALEKLMK-GRTSIIIAHRLST-IKNA-DKILVLDDG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
850-1046 |
1.12e-15 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. 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: 213260 [Multi-domain] Cd Length: 220 Bit Score: 77.51 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 850 RPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKRQETFARisGYCEQNDIHSPQVTVKESLIYSafLR 927
Cdd:cd03293 28 EEGEFVALVGPSGCGKSTLLRIIAGleRPT----SGEVLVDGEPVTGPGPDR--GYVFQQDALLPWLTVLDNVALG--LE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 928 LpKEVTKYEKMRFVDEVMELVELESLKDAvvgLPGitGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT 1007
Cdd:cd03293 100 L-QGVPKAEARERAEELLELVGLSGFENA---YPH--QLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18401096 1008 VRNTV-DTGRTVVCTIHqpsiDIFEAF---DELLLL-KRGGQVI 1046
Cdd:cd03293 174 LLDIWrETGKTVLLVTH----DIDEAVflaDRVVVLsARPGRIV 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
150-409 |
1.36e-15 |
|
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: 77.76 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 150 LGFNFTKTTKVtiLRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGkLdqsLKVT-GRVTYNGHGLEEfvpqKTSAYISQ 228
Cdd:COG1122 6 LSFSYPGGTPA--LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG-L---LKPTsGEVLVDGKDITK----KNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 229 ndvHVGVM-----------TVQETLDFSARCQGvgtrydllselvrrekdagiLPEPEVDLfmksiaagnvksslITDYT 297
Cdd:COG1122 76 ---KVGLVfqnpddqlfapTVEEDVAFGPENLG--------------------LPREEIRE--------------RVEEA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 298 LRILGLDICKDTVVGDemirgISGGQKKRVT-TGEMIVGPtKTLFMDEISTGLDSSTTYQIVKCLQEIVRfTDATVLMS- 375
Cdd:COG1122 119 LELVGLEHLADRPPHE-----LSGGQKQRVAiAGVLAMEP-EVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVt 191
|
250 260 270
....*....|....*....|....*....|....*...
gi 18401096 376 ----LLQpapetfELFDDIILLSEGQIVYQGPRDHVLT 409
Cdd:COG1122 192 hdldLVA------ELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
159-409 |
1.76e-15 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 77.82 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 159 KVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDqslKVTGRVTYNGHGLEE------FVPQKTSAyisqnDVH 232
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP---PTSGTVRLFGKPPRRarrrigYVPQRAEV-----DWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 233 VgVMTVQETLDfSARCQGVGtrydLLSELVRREKDAgilpepevdlfmksiaagnVKSSL----ITDYtlrilgldickd 308
Cdd:COG1121 90 F-PITVRDVVL-MGRYGRRG----LFRRPSRADREA-------------------VDEALervgLEDL------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 309 tvvGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRfTDATVLMSL--LQPAPetfEL 386
Cdd:COG1121 133 ---ADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVThdLGAVR---EY 205
|
250 260
....*....|....*....|...
gi 18401096 387 FDDIILLSeGQIVYQGPRDHVLT 409
Cdd:COG1121 206 FDRVLLLN-RGLVAHGPPEEVLT 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
148-397 |
2.07e-15 |
|
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: 76.74 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 148 RLLGFNFT-KTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLdqsLKVTGRVTYNGHGLEEFVPQ---KTS 223
Cdd:cd03225 1 ELKNLSFSyPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL---GPTSGEVLVDGKDLTKLSLKelrRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 224 AYISQNDVHVGVM-TVQETLDFSARCQGvgtrydllselvrrekdagiLPEPEVDLfmksiaagnvksslITDYTLRILG 302
Cdd:cd03225 78 GLVFQNPDDQFFGpTVEEEVAFGLENLG--------------------LPEEEIEE--------------RVEEALELVG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 303 LDICKDTVvgdemIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRfTDATVLMS-----LL 377
Cdd:cd03225 124 LEGLRDRS-----PFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVthdldLL 197
|
250 260
....*....|....*....|
gi 18401096 378 qpapetFELFDDIILLSEGQ 397
Cdd:cd03225 198 ------LELADRVIVLEDGK 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
851-1023 |
2.14e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.10 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 851 PGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP-KRQETFARIS-GYCEQNDIHSPQVTVKESLI-YSAFLR 927
Cdd:PRK13536 66 SGECFGLLGPNGAGKSTIARMILGMTSPD--AGKITVLGVPvPARARLARARiGVVPQFDNLDLEFTVRENLLvFGRYFG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 928 LpkevtkyeKMRFVDEVM----ELVELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1003
Cdd:PRK13536 144 M--------STREIEAVIpsllEFARLESKADARVSD-----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180
....*....|....*....|
gi 18401096 1004 VMRTVRNTVDTGRTVVCTIH 1023
Cdd:PRK13536 211 IWERLRSLLARGKTILLTTH 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
832-1042 |
2.62e-15 |
|
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: 76.99 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKRQetfaRISGYCEQ 906
Cdd:cd03296 6 RNVSKrfGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGleRPDSGTILfGGEDATDVPVQE----RNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 907 NDIHSPQVTVKESLiysAF-LRLPKEVT---KYEKMRFVDEVMELVELESLKDAvvgLPgiTGLSTEQRKRLTIAVELVA 982
Cdd:cd03296 82 HYALFRHMTVFDNV---AFgLRVKPRSErppEAEIRAKVHELLKLVQLDWLADR---YP--AQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18401096 983 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVD-TGRTVVCTIHQPSiDIFEAFDELLLLKRG 1042
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDeLHVTTVFVTHDQE-EALEVADRVVVMNKG 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
832-1075 |
3.06e-15 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 76.81 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSKD--KLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFP--KRqetfARIS-GY 903
Cdd:cd03218 4 ENLSKRygKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlvKPDSGKILlDGQDITKLPmhKR----ARLGiGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 904 CEQNDIHSPQVTVKESLIysAFLRLPKeVTKYEKMRFVDEVMELVELESLKDAvvglPGITgLSTEQRKRLTIAVELVAN 983
Cdd:cd03218 80 LPQEASIFRKLTVEENIL--AVLEIRG-LSKKEREEKLEELLEEFHITHLRKS----KASS-LSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 984 PSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLkRGGQVIYAGplgqNSHKIIEYfq 1063
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVR-ETLSITDRAYII-YEGKVLAEG----TPEEIAAN-- 223
|
250
....*....|..
gi 18401096 1064 aihgvPKIKEKY 1075
Cdd:cd03218 224 -----ELVRKVY 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
161-409 |
6.74e-15 |
|
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: 76.24 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEFVPQ---KTSAYISQNDVHVGVMT 237
Cdd:COG1120 15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS---SGEVLLDGRDLASLSRRelaRRIAYVPQEPPAPFGLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 238 VQETLdfsarcqGVGtRYDLLSELVR-REKDAgilpepevdlfmksiaagnvkssLITDYTLRILGLDICKDTVVGDemi 316
Cdd:COG1120 92 VRELV-------ALG-RYPHLGLFGRpSAEDR-----------------------EAVEEALERTGLEHLADRPVDE--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 317 rgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSL--LQPApetFELFDDIILLS 394
Cdd:COG1120 138 --LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLhdLNLA---ARYADRLVLLK 212
|
250
....*....|....*
gi 18401096 395 EGQIVYQGPRDHVLT 409
Cdd:COG1120 213 DGRIVAQGPPEEVLT 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
153-402 |
1.20e-14 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 74.48 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 153 NFTKT-TKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAG--KLDQslkvtGRVTYNGHGLEEFVPQKTS-AYISQ 228
Cdd:cd03259 5 GLSKTyGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGleRPDS-----GEILIDGRDVTGVPPERRNiGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 229 NDV---HvgvMTVQETLDFSARCQGVGTRydllsELVRREKDAgilpepevdlfmksiaagnvksslitdytLRILGLDI 305
Cdd:cd03259 80 DYAlfpH---LTVAENIAFGLKLRGVPKA-----EIRARVREL-----------------------------LELVGLEG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 306 ckdtvVGDEMIRGISGGQKKRVTTGE-MIVGPtKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSLLQPApETF 384
Cdd:cd03259 123 -----LLNRYPHELSGGQQQRVALARaLAREP-SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQE-EAL 195
|
250
....*....|....*...
gi 18401096 385 ELFDDIILLSEGQIVYQG 402
Cdd:cd03259 196 ALADRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
850-1010 |
1.57e-14 |
|
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: 74.46 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 850 RPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEGDIRISGFPKRQETFARISGYCEQNDIHS--PQVTVKESlIYS 923
Cdd:cd03257 29 KKGETLGLVGESGSGKSTLARAILGllKPTSGsiIFDGKDLLKLSRRLRKIRRKEIQMVFQDPMSSlnPRMTIGEQ-IAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 924 AFLRLPKEVTKYEKMRFVDEVMELVEL-ESLKDAvvgLPGitGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1002
Cdd:cd03257 108 PLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNR---YPH--ELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQA 182
|
....*...
gi 18401096 1003 IVMRTVRN 1010
Cdd:cd03257 183 QILDLLKK 190
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
161-366 |
2.58e-14 |
|
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: 73.28 E-value: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGkldQSLKVTGRVTYNGHGLEEFVPQ--KTSAYISQNDVHVGVMTV 238
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG---LLPPSAGEVLWNGEPIRDAREDyrRRLAYLGHADGLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 239 QETLDFSARCQGVGTRYDLLSELvrrekdagilpepevdlfmksiaagnvksslitdytLRILGLDICkdtvvGDEMIRG 318
Cdd:COG4133 93 RENLRFWAALYGLRADREAIDEA------------------------------------LEAVGLAGL-----ADLPVRQ 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 18401096 319 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTtyqiVKCLQEIVR 366
Cdd:COG4133 132 LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG----VALLAELIA 175
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
841-1044 |
3.19e-14 |
|
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: 72.25 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 841 LLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKRQ---ETFARISGYCEQNDihspqvt 915
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGllRPT----SGRVRLDGADISQwdpNELGDHVGYLPQDD------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 916 vkesliysaflrlpkevtkyekmrfvdevmELVElESLKDAVvglpgitgLSTEQRKRLTIAVELVANPSIIFMDEPTSG 995
Cdd:cd03246 86 ------------------------------ELFS-GSIAENI--------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18401096 996 LDARAAAIVMRTVRNTVDTGRTVVCTIHQPSidIFEAFDELLLLKRGGQ 1044
Cdd:cd03246 127 LDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
840-1053 |
4.69e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.27 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 840 QLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISGFPKR-----QETFARISGYCEQNDIHsp 912
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGllRPQKGAVLWQGKPLDYSKRgllalRQQVATVFQDPEQQIFY-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 913 qvTVKESLIysAFLRLPKEVTKYEKMRFVDEVMELVELESLKDAvvglPgITGLSTEQRKRLTIAVELVANPSIIFMDEP 992
Cdd:PRK13638 93 --TDIDSDI--AFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQ----P-IQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18401096 993 TSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSID-IFEAFDELLLLKRgGQVIYAGPLGQ 1053
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSH--DIDlIYEISDAVYVLRQ-GQILTHGAPGE 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
832-1050 |
5.65e-14 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. 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, 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: 213262 [Multi-domain] Cd Length: 242 Bit Score: 73.10 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK---DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMdvlagRKTGGYIE---GDIRISGFPKRQET---FARISG 902
Cdd:cd03295 4 ENVTKrygGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTM-----KMINRLIEptsGEIFIDGEDIREQDpveLRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 903 YCEQNDIHSPQVTVKESLIYsaflrLPKeVTKYEKMRFVDEVMELVELeslkdavVGLPGIT-------GLSTEQRKRLT 975
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIAL-----VPK-LLKWPKEKIRERADELLAL-------VGLDPAEfadryphELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 976 IAVELVANPSIIFMDEPTSGLDAraaaiVMRT------VRNTVDTGRTVVCTIHqpsiDIFEAF---DELLLLKRGGQVI 1046
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDP-----ITRDqlqeefKRLQQELGKTIVFVTH----DIDEAFrlaDRIAIMKNGEIVQ 216
|
....
gi 18401096 1047 YAGP 1050
Cdd:cd03295 217 VGTP 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
852-1049 |
1.33e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 72.74 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAGRKTG------------------GYIEGDIRISgfpkRQETfarisGYCEQNDIHSPQ 913
Cdd:PRK09984 30 GEMVALLGPSGSGKSTLLRHLSGLITGdksagshiellgrtvqreGRLARDIRKS----RANT-----GYIFQQFNLVNR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 914 VTVKESLIYSAFLRLPKEVTKYEKMRFVDEVMELVELESLKDAVVGLPGITGLSTEQRKRLTIAVELVANPSIIFMDEPT 993
Cdd:PRK09984 101 LSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 18401096 994 SGLDARAAAIVMRTVRNTVDT-GRTVVCTIHQpsIDIFEAFDELLLLKRGGQVIYAG 1049
Cdd:PRK09984 181 ASLDPESARIVMDTLRDINQNdGITVVVTLHQ--VDYALRYCERIVALRQGHVFYDG 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
850-1023 |
1.34e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.21 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 850 RPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpkrQETFARIS------GYCEQNDIHSPQVTVKESLIYS 923
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTGDTT--VTSGDATVAG----KSILTNISdvhqnmGYCPQFDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 924 AFLR-LPKEvtkyEKMRFVDEVMELVELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1002
Cdd:TIGR01257 2037 ARLRgVPAE----EIEKVANWSIQSLGLSLYADRLAGT-----YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180
....*....|....*....|.
gi 18401096 1003 IVMRTVRNTVDTGRTVVCTIH 1023
Cdd:TIGR01257 2108 MLWNTIVSIIREGRAVVLTSH 2128
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
851-1049 |
1.69e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.97 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 851 PGVLTALMGVSGAGKTTLMDVLAgR----KTGGYIEGDIRISGFPKRQetFARISGYCEQndIH-SPQ-VTVKESLIY-- 922
Cdd:PRK11231 27 TGKITALIGPNGCGKSTLLKCFA-RlltpQSGTVFLGDKPISMLSSRQ--LARRLALLPQ--HHlTPEgITVRELVAYgr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 923 SAFLRLPKEVTKYEKMRfVDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1002
Cdd:PRK11231 102 SPWLSLWGRLSAEDNAR-VNQAMEQTRINHLADRRL-----TDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18401096 1003 IVMRTVRNTVDTGRTVVCTIHqpsiDIFEA---FDELLLLKrGGQVIYAG 1049
Cdd:PRK11231 176 ELMRLMRELNTQGKTVVTVLH----DLNQAsryCDHLVVLA-NGHVMAQG 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
815-1049 |
2.13e-13 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 71.49 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 815 SFDNVNYyvdmpkemkeqGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGFPKRQ 894
Cdd:cd03251 2 EFKNVTF-----------RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIP--RFYDVDSGRILIDGHDVRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 895 ETFA---RISGYCEQnDIHSPQVTVKESLIYSAFLRLPKEVTKYEKMRFVDEVMElvELESLKDAVVGLPGITgLSTEQR 971
Cdd:cd03251 69 YTLAslrRQIGLVSQ-DVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIM--ELPEGYDTVIGERGVK-LSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18401096 972 KRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPSIdIFEAfDELLLLKRgGQVIYAG 1049
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLST-IENA-DRIVVLED-GKIVERG 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
851-1032 |
2.39e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 851 PGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISGFPKRQETFARISgycEQNDIHsPQVTVKESLIY-SAFLR 927
Cdd:PRK13539 27 AGEALVLTGPNGSGKTTLLRLIAGllPPAAGTIKLDGGDIDDPDVAEACHYLG---HRNAMK-PALTVAENLEFwAAFLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 928 lpkevtkyEKMRFVDEVMELVELeslkDAVVGLPGiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT 1007
Cdd:PRK13539 103 --------GEELDIAAALEAVGL----APLAHLPF-GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAEL 169
|
170 180
....*....|....*....|....*
gi 18401096 1008 VRNTVDTGRTVVCTIHQPsIDIFEA 1032
Cdd:PRK13539 170 IRAHLAQGGIVIAATHIP-LGLPGA 193
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
828-1025 |
5.16e-13 |
|
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: 69.31 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 828 EMKEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISgfPKRQETFARISGYCE 905
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGllRPDSGEVRWNGTPL--AEQRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 906 QNDIHSPQVTVKESL-IYSAFLRlpkevtkYEKmRFVDEVMELVELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANP 984
Cdd:TIGR01189 80 HLPGLKPELSALENLhFWAAIHG-------GAQ-RTIEDALAAVGLTGFEDLPAAQ-----LSAGQQRRLALARLWLSRR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18401096 985 SIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQP 1025
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQD 187
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
838-1019 |
5.35e-13 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 69.77 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 838 KLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPkrqeTFARIS---GYCEQNDIHS 911
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGllPPRSGSIRfDGRDITGLP----PHERARagiGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 912 PQVTVKESLIYSAFLRLPKEVTkyekmRFVDEVMELV-ELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANPSIIFMD 990
Cdd:cd03224 88 PELTVEENLLLGAYARRRAKRK-----ARLERVYELFpRLKERRKQLAGT-----LSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180
....*....|....*....|....*....
gi 18401096 991 EPTSGLDARAAAIVMRTVRNTVDTGRTVV 1019
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTIL 186
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
833-1042 |
7.11e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.60 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 833 GVSKDKLQ--LLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGdirisgfpkrqetfarisgyceQNDIH 910
Cdd:COG2401 35 GVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAG----------------------CVDVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 911 SPQVTVKESLIYSAFLRLPkevtkyekmrfVDEVMELVELESLKDAVVGLPGITGLSTEQRKRLTIAVELVANPSIIFMD 990
Cdd:COG2401 93 DNQFGREASLIDAIGRKGD-----------FKDAVELLNAVGLSDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18401096 991 EPTSGLDARAAAIVMRTVRNTVDTGRT--VVCTIH-------QPSIDIFEAFDELLLLKRG 1042
Cdd:COG2401 162 EFCSHLDRQTAKRVARNLQKLARRAGItlVVATHHydviddlQPDLLIFVGYGGVPEEKRR 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
856-1049 |
8.85e-13 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 69.67 E-value: 8.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 856 ALMGVSGAGKTTLMDVLAG--RKTGGYI--EGDiRISGFPKRQETFarisGYCEQNDIHSPQVTVKESLIYSafLRLpKE 931
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGfiKPDSGKIllNGK-DITNLPPEKRDI----SYVPQNYALFPHMTVYKNIAYG--LKK-RK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 932 VTKYEKMRFVDEVMELVELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNT 1011
Cdd:cd03299 101 VDKKEIERKVLEIAEMLGIDHLLNRKPET-----LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKI 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 18401096 1012 VDTGRTVVCTIHQPSIDIFEAFDELLLLkRGGQVIYAG 1049
Cdd:cd03299 176 RKEFGVTVLHVTHDFEEAWALADKVAIM-LNGKLIQVG 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
842-1042 |
8.87e-13 |
|
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: 67.45 E-value: 8.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGfpkrqetfarisgycEQNDIHSPqvtvKES 919
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGlyKPD----SGEILVDG---------------KEVSFASP----RDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 920 LiysaflrlpkevtkyekmrfvdevmelveleslkDAVVGLpgITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 999
Cdd:cd03216 73 R----------------------------------RAGIAM--VYQLSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18401096 1000 AAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKRG 1042
Cdd:cd03216 117 EVERLFKVIRRLRAQGVAVIFISHRLD-EVFEIADRVTVLRDG 158
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
840-1031 |
9.30e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.54 E-value: 9.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 840 QLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKRQETFARIsGYCEQNDIHSPQVTV 916
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivpRDAGNIIIDDEDISLLPLHARARRGI-GYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 917 KESLIysAFLRLPKEVTKYEKMRFVDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 996
Cdd:PRK10895 96 YDNLM--AVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG-----QSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 18401096 997 DARAAAIVMRTVRNTVDTGRTVVCTIH--QPSIDIFE 1031
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSGLGVLITDHnvRETLAVCE 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
825-1050 |
9.65e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 9.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 825 MPKEMKEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKRQETFARISgyc 904
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT--AGTVLVAGDDVEALSARAAS--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 905 eQNDIHSPQVTvkeSLIYSAFLRLPKEV------TKYEKM-----RFVDEVMELVELESLKDAvvglpGITGLSTEQRKR 973
Cdd:PRK09536 77 -RRVASVPQDT---SLSFEFDVRQVVEMgrtphrSRFDTWtetdrAAVERAMERTGVAQFADR-----PVTSLSGGERQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18401096 974 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAF-DELLLLKRGGqVIYAGP 1050
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIH--DLDLAARYcDELVLLADGR-VRAAGP 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
159-397 |
1.02e-12 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 67.27 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 159 KVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEFVPQKTSAYISqndvhvgvmtv 238
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT---SGEILIDGKDIAKLPLEELRRRIG----------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 239 qetldfsarcqgvgtrydllselvrrekdagilpepevdlfmksiaagnvksslitdytlrilgldickdtvvgdeMIRG 318
Cdd:cd00267 77 ----------------------------------------------------------------------------YVPQ 80
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 319 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRfTDATVLMSLLQPaPETFELFDDIILLSEGQ 397
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDP-ELAELAADRVIVLKDGK 157
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
834-1027 |
1.04e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.33 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 834 VSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKtgGY--IEGDIR-----ISGFP--KRqetfAR--IsG 902
Cdd:COG0396 8 VSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHP--KYevTSGSILldgedILELSpdER----ARagI-F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 903 YCEQNDIHSPQVTVKESLIYSAFLRLPKEVTKYEKMRFVDEVMELVELES--LKDAV-VGLPGitGlsteQRKRLTIAVE 979
Cdd:COG0396 81 LAFQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEdfLDRYVnEGFSG--G----EKKRNEILQM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 18401096 980 LVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1027
Cdd:COG0396 155 LLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQRI 202
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
162-408 |
1.15e-12 |
|
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: 72.56 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 162 ILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEfvpqktsayISQNDV--HVGVMTvQ 239
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT---SGRILIDGIDLRQ---------IDPASLrrQIGVVL-Q 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 240 ETLDFSarcqgvGTRYDLLSelvrrekdagiLPEPEVDLFmKSIAAgnvksslitdytLRILGLD--ICK-----DTVVG 312
Cdd:COG2274 557 DVFLFS------GTIRENIT-----------LGDPDATDE-EIIEA------------ARLAGLHdfIEAlpmgyDTVVG 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 313 dEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRftDATVLMSllqpA--PETFELFDDI 390
Cdd:COG2274 607 -EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIII----AhrLSTIRLADRI 679
|
250
....*....|....*...
gi 18401096 391 ILLSEGQIVYQGPRDHVL 408
Cdd:COG2274 680 IVLDKGRIVEDGTHEELL 697
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
842-1019 |
1.68e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.59 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISG----FPKRQEtfARISG----YCEQNDIhs 911
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGvyQPD----SGEILLDGepvrFRSPRD--AQAAGiaiiHQELNLV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 912 PQVTVKESLiysaFL-RLPKevtkyeKMRFVD---------EVMELVELE-SLkDAVVGlpgitGLSTEQRKRLTIAVEL 980
Cdd:COG1129 92 PNLSVAENI----FLgREPR------RGGLIDwramrrrarELLARLGLDiDP-DTPVG-----DLSVAQQQLVEIARAL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 18401096 981 VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVV 1019
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAII 194
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
832-999 |
1.74e-12 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. 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: 213267 [Multi-domain] Cd Length: 232 Bit Score: 68.42 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFP--KRQetfariSGYC 904
Cdd:cd03300 4 ENVSKfyGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfeTPTSGEILlDGKDITNLPphKRP------VNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 905 EQNDIHSPQVTVKESLiysAF-LRLpKEVTKYEKMRFVDEVMELVELESLKDAVvglpgITGLSTEQRKRLTIAVELVAN 983
Cdd:cd03300 78 FQNYALFPHLTVFENI---AFgLRL-KKLPKAEIKERVAEALDLVQLEGYANRK-----PSQLSGGQQQRVAIARALVNE 148
|
170
....*....|....*.
gi 18401096 984 PSIIFMDEPTSGLDAR 999
Cdd:cd03300 149 PKVLLLDEPLGALDLK 164
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
840-1004 |
2.08e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 68.91 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 840 QLLKEVTGVFRPGVLTALMGVSGAGKTTLM-------DVLAGRKtggyIEGDIRISGfpkrqetfarisgyceqNDIHSP 912
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGAR----VEGEILLDG-----------------EDIYDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 913 QVTVKEsliysafLR------------LPKEVtkYE---------KMRFVDEVMELVElESLKDAvvGL----------P 961
Cdd:COG1117 84 DVDVVE-------LRrrvgmvfqkpnpFPKSI--YDnvayglrlhGIKSKSELDEIVE-ESLRKA--ALwdevkdrlkkS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18401096 962 GiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1004
Cdd:COG1117 152 A-LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI 193
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
161-402 |
2.23e-12 |
|
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: 67.94 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEE------FVPQKTSAY----ISQND 230
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPT---SGSIRVFGKPLEKerkrigYVPQRRSIDrdfpISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 231 VhvgVMTvqetldfsarcqGVGTRYDLLSELVRREKDAGilpepevdlfmksiaagnvksslitDYTLRILGLdickdTV 310
Cdd:cd03235 90 V---VLM------------GLYGHKGLFRRLSKADKAKV-------------------------DEALERVGL-----SE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 311 VGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEiVRFTDATVLMSL--LQPAPetfELFD 388
Cdd:cd03235 125 LADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRE-LRREGMTILVVThdLGLVL---EYFD 200
|
250
....*....|....
gi 18401096 389 DIILLsEGQIVYQG 402
Cdd:cd03235 201 RVLLL-NRTVVASG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
152-409 |
2.53e-12 |
|
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: 71.09 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 152 FNFTKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEFVPQKTSAYISqndv 231
Cdd:COG1123 270 YPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT---SGSILFDGKDLTKLSRRSLRELRR---- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 232 HVGV------------MTVQETLDFSARCQGVGTRYDllselvRREKdagilpepevdlfmksiaagnvkssliTDYTLR 299
Cdd:COG1123 343 RVQMvfqdpysslnprMTVGDIIAEPLRLHGLLSRAE------RRER---------------------------VAELLE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 300 ILGLDickdTVVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVL-----M 374
Cdd:COG1123 390 RVGLP----PDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLfishdL 465
|
250 260 270
....*....|....*....|....*....|....*
gi 18401096 375 SLLQpapetfELFDDIILLSEGQIVYQGPRDHVLT 409
Cdd:COG1123 466 AVVR------YIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
832-1042 |
3.51e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 69.41 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGrktggyIE----GDIRISGfpkrQETFARIS---- 901
Cdd:COG1118 6 RNISKrfGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAG------LEtpdsGRIVLNG----RDLFTNLPprer 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 902 --GYCEQNDIHSPQVTVKESLiysAF----LRLPKEVTKyEKmrfVDEVMELVELESLKDAvvgLPgiTGLSTEQRKRLT 975
Cdd:COG1118 76 rvGFVFQHYALFPHMTVAENI---AFglrvRPPSKAEIR-AR---VEELLELVQLEGLADR---YP--SQLSGGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18401096 976 IAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVD-TGRTVVCTIHqpsiDIFEAF---DELLLLKRG 1042
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDeLGGTTVFVTH----DQEEALelaDRVVVMNQG 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
841-1000 |
3.90e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 841 LLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRIsgfPKRqetfARIsGYCEQNDIHSPQVTVKESL 920
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELE--PDSGEVSI---PKG----LRI-GYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 921 IySAFLRLPKEVTKYE----KMRFVDEVME-LVELESLKDAV---------------VGLPG------ITGLSTEQRKRL 974
Cdd:COG0488 83 L-DGDAELRALEAELEeleaKLAEPDEDLErLAELQEEFEALggweaearaeeilsgLGFPEedldrpVSELSGGWRRRV 161
|
170 180
....*....|....*....|....*.
gi 18401096 975 TIAVELVANPSIIFMDEPTSGLDARA 1000
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
155-402 |
5.24e-12 |
|
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: 67.15 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 155 TKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDQslKVTGRVTYNGHGLEEFVPQ------KTSAYISQ 228
Cdd:cd03257 13 TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILG-LLK--PTSGSIIFDGKDLLKLSRRlrkirrKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 229 NDVHV--GVMTVQETLDFSARCQGVGTRYDLLSELVRREKDAGILPEpevdlfmksiaagnvksslitdytlRILgldic 306
Cdd:cd03257 90 DPMSSlnPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPE-------------------------EVL----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 307 kdtvvgDEMIRGISGGQKKRVttgeMI-----VGPtKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLM-----SL 376
Cdd:cd03257 140 ------NRYPHELSGGQRQRV----AIaralaLNP-KLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFithdlGV 208
|
250 260
....*....|....*....|....*.
gi 18401096 377 LQpapetfELFDDIILLSEGQIVYQG 402
Cdd:cd03257 209 VA------KIADRVAVMYAGKIVEEG 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
161-402 |
5.87e-12 |
|
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: 65.92 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEFVPQKTS---AYISQndvhvgVMT 237
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS---SGEILLDGKDLASLSPKELArkiAYVPQ------ALE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 238 VQETLDFSARcqgvgtrydLLSELvrrekdagilpepevdlfmksiaagnvksslitdytlrilgldickdtvvgdemir 317
Cdd:cd03214 84 LLGLAHLADR---------PFNEL-------------------------------------------------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 318 giSGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSL--LQPApetFELFDDIILLSE 395
Cdd:cd03214 99 --SGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLhdLNLA---ARYADRVILLKD 173
|
....*..
gi 18401096 396 GQIVYQG 402
Cdd:cd03214 174 GRIVAQG 180
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
852-1050 |
7.80e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKRQETFARISGYCEQN---DIHSPqVTVKESLI-----YS 923
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLA--SGKISILGQPTRQALQKNLVAYVPQSeevDWSFP-VLVEDVVMmgrygHM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 924 AFLRLPKEvtkyEKMRFVDEVMELVELESLKDAVVGlpgitGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1003
Cdd:PRK15056 110 GWLRRAKK----RDRQIVTAALARVDMVEFRHRQIG-----ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18401096 1004 VMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKrgGQVIYAGP 1050
Cdd:PRK15056 181 IISLLRELRDEGKTMLVSTHNLG-SVTEFCDYTVMVK--GTVLASGP 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
158-398 |
1.03e-11 |
|
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: 65.97 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 158 TKVTILRDVSGIIKPSRMTLLLGPPSSGKTTlLLALAGKLDQSlkVTGRVTYNGHGLEEFVPQKTSAYISQndvHVGVmt 237
Cdd:cd03255 15 EKVQALKGVSLSIEKGEFVAIVGPSGSGKST-LLNILGGLDRP--TSGEVRVDGTDISKLSEKELAAFRRR---HIGF-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 238 vqetldfsarcqgVGTRYDLLSELVRREKdagilpepeVDLFMksIAAGNVKSSLITDYT--LRILGLDICKDTVVGdEM 315
Cdd:cd03255 87 -------------VFQSFNLLPDLTALEN---------VELPL--LLAGVPKKERRERAEelLERVGLGDRLNHYPS-EL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 316 irgiSGGQKKRVTTGEMIVGPTKTLFMDEiSTG-LDSSTTYQIVKCLQEIVRFTDATVLMSLLQpaPETFELFDDIILLS 394
Cdd:cd03255 142 ----SGGQQQRVAIARALANDPKIILADE-PTGnLDSETGKEVMELLRELNKEAGTTIVVVTHD--PELAEYADRIIELR 214
|
....
gi 18401096 395 EGQI 398
Cdd:cd03255 215 DGKI 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
842-1045 |
1.13e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.17 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKR-QETFARI-SG----YCEqndIH-SPQV 914
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD--AGSILIDGQEMRfASTTAALaAGvaiiYQE---LHlVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 915 TVKESLiysaFL-RLPkevtkyEKMRFVD------EVMElvELESLKDAVVGLPGITGLSTEQRKRLTIAVELVANPSII 987
Cdd:PRK11288 95 TVAENL----YLgQLP------HKGGIVNrrllnyEARE--QLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 18401096 988 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKRGGQV 1045
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME-EIFALCDAITVFKDGRYV 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
840-1042 |
1.13e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 66.72 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 840 QLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAgrktgGYIE---GDIRISGFPKRQ---ETFARISGYCEQndiHSPQ 913
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS-----GELSpdsGEVRLNGRPLADwspAELARRRAVLPQ---HSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 914 V---TVKESLiysAFLRLPKEVTKYEKMRFVDEVMELVELESLKDAVvglpgITGLSTEQRKRLTIAVELV------ANP 984
Cdd:PRK13548 88 SfpfTVEEVV---AMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRD-----YPQLSGGEQQRVQLARVLAqlwepdGPP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18401096 985 SIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHqpsiDIFEAF---DELLLLKRG 1042
Cdd:PRK13548 160 RWLLLDEPTSALDLAHQHHVLRLARQlAHERGLAVIVVLH----DLNLAAryaDRIVLLHQG 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
836-1079 |
1.25e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.68 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 836 KDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKRQETFARISG-----YCEQNDih 910
Cdd:PRK13647 15 KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQ--RGRVKVMGREVNAENEKWVRSkvglvFQDPDD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 911 spQV---TVKESLiysAFLRLPKEVTKYEKMRFVDEVMELVELESLKDAVvglPgiTGLSTEQRKRLTIAVELVANPSII 987
Cdd:PRK13647 91 --QVfssTVWDDV---AFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKP---P--YHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 988 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDI-FEAFDELLLLKRGGQVIYAGP--------LGQNSHKI 1058
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATH--DVDLaAEWADQVIVLKEGRVLAEGDKslltdediVEQAGLRL 238
|
250 260
....*....|....*....|.
gi 18401096 1059 IEYFQAIHGVPKIKEKYNPAT 1079
Cdd:PRK13647 239 PLVAQIFEDLPELGQSKLPLT 259
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
828-1025 |
1.32e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 65.21 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 828 EMKEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPkrqetfarisgyce 905
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlsPPL----AGRVLLNGGP-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 906 qndIHSPQVTVKESLIYSAFLRLPKEV-TKYEKMRF---------VDEVMELVELESLKDAVVGlpgitGLSTEQRKRLT 975
Cdd:cd03231 64 ---LDFQRDSIARGLLYLGHAPGIKTTlSVLENLRFwhadhsdeqVEEALARVGLNGFEDRPVA-----QLSAGQQRRVA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18401096 976 IAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQP 1025
Cdd:cd03231 136 LARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
841-1069 |
1.36e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.73 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 841 LLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLaGRKTGGYiEGDIRISGFPKRQ---ETFARISGYCEQNDIHSPQVTVK 917
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPS-EGEILLDAQPLESwssKAFARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 918 ESLiysAFLRLP--KEVTKY--EKMRFVDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVANPSIIFMDEPT 993
Cdd:PRK10575 104 ELV---AIGRYPwhGALGRFgaADREKVEEAISLVGLKPLAHRLV-----DSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 994 SGLDARAAAIVMRTV-RNTVDTGRTVVCTIHqpSIDIFEAFDELLLLKRGGQVIYAGP---LGQNshkiiEYFQAIHGVP 1069
Cdd:PRK10575 176 SALDIAHQVDVLALVhRLSQERGLTVIAVLH--DINMAARYCDYLVALRGGEMIAQGTpaeLMRG-----ETLEQIYGIP 248
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
850-1070 |
1.42e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.07 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 850 RPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKRQET--FARISGYCEQndihSPQVTVKESLIYSA 924
Cdd:PRK13643 30 KKGSYTALIGHTGSGKSTLLQHLNGllQPTEGKVTvGDIVVSSTSKQKEIkpVRKKVGVVFQ----FPESQLFEETVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 925 FLRLPKE--VTKYEKMRFVDEVMELVELEslKDAVVGLPgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1002
Cdd:PRK13643 106 VAFGPQNfgIPKEKAEKIAAEKLEMVGLA--DEFWEKSP--FELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 1003 IVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKRGGQVIYAGPlgQNSHKIIEYFQAIH-GVPK 1070
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVLVTHLMD-DVADYADYVYLLEKGHIISCGTP--SDVFQEVDFLKAHElGVPK 247
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
832-1007 |
1.88e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 67.41 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFP--KRqetfaRIsGYC 904
Cdd:COG3839 7 ENVSKsyGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGleDPTSGEILiGGRDVTDLPpkDR-----NI-AMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 905 EQNDIHSPQVTVKESLiysAF-LRLPKeVTKYEKMRFVDEVMELVELESLKDAvvgLPGitGLSTEQRKRLTIAVELVAN 983
Cdd:COG3839 81 FQSYALYPHMTVYENI---AFpLKLRK-VPKAEIDRRVREAAELLGLEDLLDR---KPK--QLSGGQRQRVALGRALVRE 151
|
170 180
....*....|....*....|....*.
gi 18401096 984 PSIIFMDEPTSGLDA--RAAaivMRT 1007
Cdd:COG3839 152 PKVFLLDEPLSNLDAklRVE---MRA 174
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
837-1049 |
2.44e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 65.87 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 837 DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKRQETFARIS-----GYCEQN-- 907
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGilKPT----SGEVLIKGEPIKYDKKSLLEvrktvGIVFQNpd 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 908 -DIHSPqvTVKESLIYSAF-LRLPKEvtkyekmrfvdEVMELVElESLKDavVGLPGITG-----LSTEQRKRLTIAVEL 980
Cdd:PRK13639 89 dQLFAP--TVEEDVAFGPLnLGLSKE-----------EVEKRVK-EALKA--VGMEGFENkpphhLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 981 VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLLKRGGQVIYAG 1049
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYADKVYVMSDGKIIKEG 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
832-1046 |
2.48e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 65.88 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK------DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPkRQETFARIsGY 903
Cdd:COG1116 11 RGVSKrfptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGleKPT----SGEVLVDGKP-VTGPGPDR-GV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 904 CEQNDihS--PQVTVKESLIYSafLRLpKEVTKYEKMRFVDEVMELVELESLKDAvvgLPGItgLSTEQRKRLTIAVELV 981
Cdd:COG1116 85 VFQEP--AllPWLTVLDNVALG--LEL-RGVPKAERRERARELLELVGLAGFEDA---YPHQ--LSGGMRQRVAIARALA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 982 ANPSIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHqpsiDIFEAF---DELLLL-KRGGQVI 1046
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLWqETGKTVLFVTH----DVDEAVflaDRVVVLsARPGRIV 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
850-1026 |
2.63e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 850 RPGVLTALMGVSGAGKTTLMDV--LAGRKTGGYIE-GDIRISG---FPKRQETFARIS---GYCEQNDIHSPQVTVKESL 920
Cdd:PRK11264 27 KPGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTIRvGDITIDTarsLSQQKGLIRQLRqhvGFVFQNFNLFPHRTVLENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 921 IYSaflrlPKEVTKYEKMRFVDEVMELVeleslkdAVVGLPGITG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSG 995
Cdd:PRK11264 107 IEG-----PVIVKGEPKEEATARARELL-------AKVGLAGKETsyprrLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190
....*....|....*....|....*....|.
gi 18401096 996 LDARAAAIVMRTVRNTVDTGRTVVCTIHQPS 1026
Cdd:PRK11264 175 LDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
162-402 |
2.84e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 64.52 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 162 ILRDVSGIIkPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEE----------FVPQKTSAYISqndv 231
Cdd:cd03264 15 ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPS---SGTIRIDGQDVLKqpqklrrrigYLPQEFGVYPN---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 232 hvgvMTVQETLDFSARcqgvgtrydllselvrrekdagilpepevdlfMKSIAAGNVKSSLitDYTLRILGLdickdTVV 311
Cdd:cd03264 87 ----FTVREFLDYIAW--------------------------------LKGIPSKEVKARV--DEVLELVNL-----GDR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 312 GDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSsttyqivkclQEIVRF--------TDATVLMS--LLqpap 381
Cdd:cd03264 124 AKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP----------EERIRFrnllselgEDRIVILSthIV---- 189
|
250 260
....*....|....*....|..
gi 18401096 382 ETFELF-DDIILLSEGQIVYQG 402
Cdd:cd03264 190 EDVESLcNQVAVLNKGKLVFEG 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
828-1045 |
3.63e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 828 EMKEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIegDIRISGFPKRQETFARISG--- 902
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGihEPTKGTI--TINNINYNKLDHKLAAQLGigi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 903 -YCEQNDIHspQVTVKESLIYSaflRLPKE------VTKYEKMRFVDEVMEL-VELESLKDAVVGlpgitGLSTEQRKRL 974
Cdd:PRK09700 85 iYQELSVID--ELTVLENLYIG---RHLTKkvcgvnIIDWREMRVRAAMMLLrVGLKVDLDEKVA-----NLSISHKQML 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18401096 975 TIAVELVANPSIIFMDEPTSGLDARAAA---IVMRTVRNtvdTGRTVVCTIHQPSiDIFEAFDELLLLKRGGQV 1045
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDylfLIMNQLRK---EGTAIVYISHKLA-EIRRICDRYTVMKDGSSV 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
851-1053 |
4.63e-11 |
|
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: 66.28 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 851 PGVlTALMGVSGAGKTTLMDVLAG--RKTGGYiegdIRISG---FPKRQETFA-----RIsGYCEQNDIHSPQVTVKESL 920
Cdd:COG4148 25 RGV-TALFGPSGSGKTTLLRAIAGleRPDSGR----IRLGGevlQDSARGIFLpphrrRI-GYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 921 IYsAFLRLPKEVTKYEkmrfVDEVMELVELESLKDAvvglpGITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD-AR 999
Cdd:COG4148 99 LY-GRKRAPRAERRIS----FDEVVELLGIGHLLDR-----RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDlAR 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18401096 1000 AAAI--VMRTVRNTVDTgrtvvctihqP----SIDIFEAF---DELLLLKrGGQVIYAGPLGQ 1053
Cdd:COG4148 169 KAEIlpYLERLRDELDI----------PilyvSHSLDEVArlaDHVVLLE-QGRVVASGPLAE 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
837-1026 |
5.15e-11 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 64.43 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 837 DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRktggYI--EGDIRISGFP---KRQETFARISGYCEQndihs 911
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF----YVpeNGRVLVDGHDlalADPAWLRRQVGVVLQ----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 912 pqvtvkESLIYSAFLRlpkevtkyEKMRFVDEVM---ELVELESLKDA-------------VVGLPGItGLSTEQRKRLT 975
Cdd:cd03252 84 ------ENVLFNRSIR--------DNIALADPGMsmeRVIEAAKLAGAhdfiselpegydtIVGEQGA-GLSGGQRQRIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18401096 976 IAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPS 1026
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLS 198
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
747-1019 |
5.79e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.11 E-value: 5.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 747 IGVGGILGFtvlfnilVTLALTFLNPLEK--------QQAVVSKEN-----TEENRAENGSKSKSIDVKRGMVlpftplt 813
Cdd:COG1132 275 LTVGDLVAF-------ILYLLRLFGPLRQlanvlnqlQRALASAERifellDEPPEIPDPPGAVPLPPVRGEI------- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 814 mSFDNVNY-YvdmpkemkeqgvsKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRktggY--IEGDIRISGF 890
Cdd:COG1132 341 -EFENVSFsY-------------PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF----YdpTSGRILIDGV 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 891 PKRQETFA----RIsGYCEQNdihsPQV---TVKESLIYSAflrlpKEVTKYEkmrfVDEVMELVEL----ESLK---DA 956
Cdd:COG1132 403 DIRDLTLEslrrQI-GVVPQD----TFLfsgTIRENIRYGR-----PDATDEE----VEEAAKAAQAhefiEALPdgyDT 468
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18401096 957 VVGLPGITgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtVDTGRTVV 1019
Cdd:COG1132 469 VVGERGVN-LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALER-LMKGRTTI 529
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
830-1024 |
6.32e-11 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. 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: 213225 [Multi-domain] Cd Length: 233 Bit Score: 64.14 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 830 KEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGF------PKRQETFARISGY 903
Cdd:cd03258 9 KVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLER--PTSGSVLVDGTdltllsGKELRKARRRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 904 CEQ--NDIHSPqvTVKESLIYsaflrlPKEVTKYEKM---RFVDEVMELVELESLKDAVvglpgITGLSTEQRKRLTIAV 978
Cdd:cd03258 87 IFQhfNLLSSR--TVFENVAL------PLEIAGVPKAeieERVLELLELVGLEDKADAY-----PAQLSGGQKQRVGIAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18401096 979 ELVANPSIIFMDEPTSGLDARAAAIVMRTVRNT-VDTGRTVVCTIHQ 1024
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHE 200
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
850-1049 |
6.59e-11 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK 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 complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 64.47 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 850 RPGVLTALMGVSGAGKTTLMDVLAGRKT--GGYIEGDIRISGF--------PKRQETFARISGYCEQNDIHSPQVTVKES 919
Cdd:TIGR02323 27 YPGEVLGIVGESGSGKSTLLGCLAGRLApdHGTATYIMRSGAElelyqlseAERRRLMRTEWGFVHQNPRDGLRMRVSAG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 920 LIYSAFLrLPKEVTKYEKMR-FVDEVMELVELEslKDAVVGLPgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 998
Cdd:TIGR02323 107 ANIGERL-MAIGARHYGNIRaTAQDWLEEVEID--PTRIDDLP--RAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDV 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18401096 999 RAAAIVMRTVRNTV-DTGRTVVCTIHQPSIDIFEAfDELLLLKRgGQVIYAG 1049
Cdd:TIGR02323 182 SVQARLLDLLRGLVrDLGLAVIIVTHDLGVARLLA-QRLLVMQQ-GRVVESG 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
159-405 |
7.55e-11 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 63.61 E-value: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 159 KVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEFVPQKTS----AYISQNDVHVG 234
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR---SGSIRFDGRDITGLPPHERAragiGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 235 VMTVQETLdfsarcqgvgtrydLLSELVRREKDAGILPEPEVDLF-----MKSIAAGnvksslitdyTLrilgldickdt 309
Cdd:cd03224 89 ELTVEENL--------------LLGAYARRRAKRKARLERVYELFprlkeRRKQLAG----------TL----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 310 vvgdemirgiSGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIvRFTDATVLMSlLQPAPETFELFDD 389
Cdd:cd03224 134 ----------SGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLV-EQNARFALEIADR 201
|
250
....*....|....*.
gi 18401096 390 IILLSEGQIVYQGPRD 405
Cdd:cd03224 202 AYVLERGRVVLEGTAA 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
837-1049 |
8.75e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 64.48 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 837 DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISGFPKRQETFARIS-GYCEQNDIHSP- 912
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGilKPSSGRILFDGKPIDYSRKGLMKLRESvGMVFQDPDNQLf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 913 QVTVKESLIYSAF-LRLPKEvtkyEKMRFVDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVANPSIIFMDE 991
Cdd:PRK13636 97 SASVYQDVSFGAVnLKLPED----EVRKRVDNALKRTGIEHLKDKPT-----HCLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 992 PTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHqpSIDIFEAFDELLLLKRGGQVIYAG 1049
Cdd:PRK13636 168 PTAGLDPMGVSEIMKLLVEMQkELGLTIIIATH--DIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
825-999 |
8.76e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 65.12 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 825 MPKEMKE-QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFP--KRqet 896
Cdd:COG3842 1 MAMPALElENVSKryGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfeTPDSGRILlDGRDVTGLPpeKR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 897 faRIsGYCEQNDIHSPQVTVKESLiysAF-LRLpKEVTKYEKMRFVDEVMELVELESLKDAvvgLPGitGLSTEQRKRLT 975
Cdd:COG3842 78 --NV-GMVFQDYALFPHLTVAENV---AFgLRM-RGVPKAEIRARVAELLELVGLEGLADR---YPH--QLSGGQQQRVA 145
|
170 180
....*....|....*....|....
gi 18401096 976 IAVELVANPSIIFMDEPTSGLDAR 999
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAK 169
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
851-1046 |
9.44e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.95 E-value: 9.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 851 PGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKRQETFARisGYCEQNDIHSPQVTVKESLiysAF-LRLp 929
Cdd:PRK11248 26 SGELLVVLGPSGCGKTTLLNLIAGFVP--YQHGSITLDGKPVEGPGAER--GVVFQNEGLLPWRNVQDNV---AFgLQL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 930 KEVTKYEKMRFVDEVMELVELESlkdavVGLPGITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA--RAAaivMRT 1007
Cdd:PRK11248 98 AGVEKMQRLEIAHQMLKKVGLEG-----AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAftREQ---MQT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18401096 1008 VRNTV--DTGRTVVCTIHqpsiDIFEAF---DELLLLKRG-GQVI 1046
Cdd:PRK11248 170 LLLKLwqETGKQVLLITH----DIEEAVfmaTELVLLSPGpGRVV 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
835-1023 |
1.38e-10 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 62.94 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 835 SKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAgRKtggY--IEGDIRISGFPKRQ---ETFARISGYCEQNdi 909
Cdd:cd03249 12 SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLE-RF---YdpTSGEILLDGVDIRDlnlRWLRSQIGLVSQE-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 910 hsPQV---TVKESLIYSAFLRLPKEVTKYEKMRFVDEVmeLVELESLKDAVVGlPGITGLSTEQRKRLTIAVELVANPSI 986
Cdd:cd03249 86 --PVLfdgTIAENIRYGKPDATDEEVEEAAKKANIHDF--IMSLPDGYDTLVG-ERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 18401096 987 IFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIH 1023
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAH 196
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
161-409 |
1.57e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.25 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEFVPQKTSAyisqndvHVGVMTVQE 240
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD---SGEVRLNGRPLADWSPAELAR-------RRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 241 TLDFSARcqgvgtrydlLSELVRrekdAGILPEPEvdlfmksiaaGNVKSSLITDYTLRILGLdickdTVVGDEMIRGIS 320
Cdd:PRK13548 86 SLSFPFT----------VEEVVA----MGRAPHGL----------SRAEDDALVAAALAQVDL-----AHLAGRDYPQLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 321 GGQKKRV------TTGEMIVGPTKTLFMDEISTGLDSSttYQIvKCLQEIVRFTDAT------VLMSLLQPApetfeLF- 387
Cdd:PRK13548 137 GGEQQRVqlarvlAQLWEPDGPPRWLLLDEPTSALDLA--HQH-HVLRLARQLAHERglavivVLHDLNLAA-----RYa 208
|
250 260
....*....|....*....|..
gi 18401096 388 DDIILLSEGQIVYQGPRDHVLT 409
Cdd:PRK13548 209 DRIVLLHQGRLVADGTPAEVLT 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
163-402 |
1.91e-10 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. 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: 213232 [Multi-domain] Cd Length: 220 Bit Score: 62.39 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 163 LRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLdqslKVT-GRVTYNGHGL--EEFVPQKTSAYISQNDVHVGVMTVQ 239
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLL----KPTsGRATVAGHDVvrEPREVRRRIGIVFQDLSVDDELTGW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 240 ETLDFSARCQGVGTRydllselVRREKdagilpepevdlfmksiaagnvkssliTDYTLRILGLdickdTVVGDEMIRGI 319
Cdd:cd03265 92 ENLYIHARLYGVPGA-------ERRER---------------------------IDELLDFVGL-----LEAADRLVKTY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 320 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSlLQPAPETFELFDDIILLSEGQIV 399
Cdd:cd03265 133 SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLT-THYMEEAEQLCDRVAIIDHGRII 211
|
...
gi 18401096 400 YQG 402
Cdd:cd03265 212 AEG 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
830-997 |
2.24e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.10 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 830 KEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP-------KRQETFARISG 902
Cdd:PRK10584 14 KSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS--SGEVSLVGQPlhqmdeeARAKLRAKHVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 903 YCEQNDIHSPQVTVKESLIYSAFLRLPKEVTKYEKMRfvdevmELVELESLKDAVVGLPGitGLSTEQRKRLTIAVELVA 982
Cdd:PRK10584 92 FVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAK------ALLEQLGLGKRLDHLPA--QLSGGEQQRVALARAFNG 163
|
170
....*....|....*
gi 18401096 983 NPSIIFMDEPTSGLD 997
Cdd:PRK10584 164 RPDVLFADEPTGNLD 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
832-1024 |
2.66e-10 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 61.78 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGF----PKRQETFARIS-GYC 904
Cdd:cd03262 4 KNLHKsfGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEE--PDSGTIIIDGLkltdDKKNINELRQKvGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 905 EQNDIHSPQVTVKESLIYSaflrlPKEVTKYEKMRFVDEVMELVELESLKDAVVGLPGitGLSTEQRKRLTIAVELVANP 984
Cdd:cd03262 82 FQQFNLFPHLTVLENITLA-----PIKVKGMSKAEAEERALELLEKVGLADKADAYPA--QLSGGQQQRVAIARALAMNP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 18401096 985 SIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1024
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
162-397 |
6.22e-10 |
|
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: 60.56 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 162 ILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDqslKVTGRVTYNGHglEEFVPQktSAYIsQNDvhvgvmTVQET 241
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE---KLSGSVSVPGS--IAYVSQ--EPWI-QNG------TIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 242 LDFsarcqgvGTRYDllSELVRrekdagilpepevdlfmKSIAAgnvkSSLITDytLRIL-GLDickDTVVGDemiRGI- 319
Cdd:cd03250 86 ILF-------GKPFD--EERYE-----------------KVIKA----CALEPD--LEILpDGD---LTEIGE---KGIn 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 320 -SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIV-KCLQEIVRFTDATVL----MSLLQPApetfelfDDIILL 393
Cdd:cd03250 128 lSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILvthqLQLLPHA-------DQIVVL 200
|
....
gi 18401096 394 SEGQ 397
Cdd:cd03250 201 DNGR 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
148-350 |
6.72e-10 |
|
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: 60.35 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 148 RLLGFNFTKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEFVPQKTSAYIS 227
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES---SGSILLNGKPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 228 QNdvhvgvmtvqetldfsarcqgvgTRYDLLSELVRREkdagilpepeVDLFMKSIAAGNVKSSLItdytLRILGLDICK 307
Cdd:cd03226 78 QD-----------------------VDYQLFTDSVREE----------LLLGLKELDAGNEQAETV----LKDLDLYALK 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18401096 308 DtvvgdEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLD 350
Cdd:cd03226 121 E-----RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
857-999 |
7.21e-10 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 60.35 E-value: 7.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 857 LMGVSGAGKTTLMDVLAG--RKTGG--YIeGDIRISGFPKRQETFARISgyceQNDIHSPQVTVKESLiysAF-LRLPKe 931
Cdd:cd03301 31 LLGPSGCGKTTTLRMIAGleEPTSGriYI-GGRDVTDLPPKDRDIAMVF----QNYALYPHMTVYDNI---AFgLKLRK- 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18401096 932 VTKYEKMRFVDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 999
Cdd:cd03301 102 VPKDEIDERVREVAELLQIEHLLDRKP-----KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK 164
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
834-1027 |
8.44e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.85 E-value: 8.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 834 VSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGfpkrqetfarisgyceqNDIHSPQ 913
Cdd:cd03217 8 VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTEGEILFKG-----------------EDITDLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 914 VTVKESL-IYSAFLRLPK--EVTKYEKMRFVDEvmelveleslkdavvglpgitGLSTEQRKRLTIAVELVANPSIIFMD 990
Cdd:cd03217 71 PEERARLgIFLAFQYPPEipGVKNADFLRYVNE---------------------GFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 18401096 991 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1027
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRL 166
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
841-1042 |
1.54e-09 |
|
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: 59.41 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 841 LLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGfpkrqetfaRISgYCEQ-----NDihspq 913
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGelEKL----SGSVSVPG---------SIA-YVSQepwiqNG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 914 vTVKESLIYSAflrlpkevtKYEKMRFvDEVME----LVELESLKDA---VVGLPGITgLSTEQRKRLTIAVELVANPSI 986
Cdd:cd03250 81 -TIRENILFGK---------PFDEERY-EKVIKacalEPDLEILPDGdltEIGEKGIN-LSGGQKQRISLARAVYSDADI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 18401096 987 IFMDEPTSGLDAR-AAAIVMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLLKRG 1042
Cdd:cd03250 149 YLLDDPLSAVDAHvGRHIFENCILGLLLNNKTRILVTHQ--LQLLPHADQIVVLDNG 203
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
850-1019 |
2.07e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 59.61 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 850 RPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPkrqeTFARIS---GYCEQN-DIHsPQVTVKESLIY 922
Cdd:COG0410 27 EEGEIVALLGRNGAGKTTLLKAISGllPPRSGSIRfDGEDITGLP----PHRIARlgiGYVPEGrRIF-PSLTVEENLLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 923 SAFLRLPKEVTKYEkmrfVDEVMELV-ELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1001
Cdd:COG0410 102 GAYARRDRAEVRAD----LERVYELFpRLKERRRQRAGT-----LSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIV 172
|
170
....*....|....*...
gi 18401096 1002 AIVMRTVRNTVDTGRTVV 1019
Cdd:COG0410 173 EEIFEIIRRLNREGVTIL 190
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
161-409 |
2.09e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.23 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQS-----LKVTGRVTYNGHGLEEFVPQKTS---AYISQndvh 232
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgARVTGDVTLNGEPLAAIDAPRLArlrAVLPQ---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 233 vgvmTVQETLDFSARcqgvgtrydllsELVRrekdAGILPEpevdlfMKSIAAGNVKSSLITDYTLRILGldicKDTVVG 312
Cdd:PRK13547 91 ----AAQPAFAFSAR------------EIVL----LGRYPH------ARRAGALTHRDGEIAWQALALAG----ATALVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 313 DEmIRGISGGQKKRVTTGEMI---------VGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSLLQPAPET 383
Cdd:PRK13547 141 RD-VTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAA 219
|
250 260
....*....|....*....|....*.
gi 18401096 384 fELFDDIILLSEGQIVYQGPRDHVLT 409
Cdd:PRK13547 220 -RHADRIAMLADGAIVAHGAPADVLT 244
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
147-407 |
2.26e-09 |
|
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: 59.12 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 147 LRLLGFNFTKTTKvTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAG--KLDQSLKVTGRVTYNGHGLeefvpqktsa 224
Cdd:cd03260 1 IELRDLNVYYGDK-HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlnDLIPGAPDEGEVLLDGKDI---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 225 YISQNDV-----HVGV---------MTVQETLDFSARCQGVGTRyDLLSELVRRekdagilpepevdlfmksiaagnvks 290
Cdd:cd03260 70 YDLDVDVlelrrRVGMvfqkpnpfpGSIYDNVAYGLRLHGIKLK-EELDERVEE-------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 291 slitdyTLRILGLDickDTVVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRftDA 370
Cdd:cd03260 123 ------ALRKAALW---DEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EY 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 18401096 371 TVLM---SLLQPApetfELFDDIILLSEGQIVYQGPRDHV 407
Cdd:cd03260 192 TIVIvthNMQQAA----RVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
154-408 |
2.28e-09 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 59.55 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 154 FTKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEfvpqktsayISQNDV-- 231
Cdd:cd03253 8 FAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS---SGSILIDGQDIRE---------VTLDSLrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 232 HVGVMTvQETLDFSarcqgvgtryDLLSELVRREK-DAGilpEPEVdlfmksIAAgnVKSSLITDytlRILGLDICKDTV 310
Cdd:cd03253 76 AIGVVP-QDTVLFN----------DTIGYNIRYGRpDAT---DEEV------IEA--AKAAQIHD---KIMRFPDGYDTI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 311 VGDemiRG--ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIvrFTDATVLM-----SLLQPApet 383
Cdd:cd03253 131 VGE---RGlkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIViahrlSTIVNA--- 202
|
250 260
....*....|....*....|....*
gi 18401096 384 felfDDIILLSEGQIVYQGPRDHVL 408
Cdd:cd03253 203 ----DKIIVLKDGRIVERGTHEELL 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
835-1042 |
2.31e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.05 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 835 SKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGgyieGDIRISGFPKRQetfarisgyCEQNDIHS- 911
Cdd:TIGR00958 490 NRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlyQPTG----GQVLLDGVPLVQ---------YDHHYLHRq 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 912 -------PQV---TVKESLIYSAFLRLPKEVTKYEKMRFVDEVmeLVELESLKDAVVGLPGiTGLSTEQRKRLTIAVELV 981
Cdd:TIGR00958 557 valvgqePVLfsgSVRENIAYGLTDTPDEEIMAAAKAANAHDF--IMEFPNGYDTEVGEKG-SQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18401096 982 ANPSIIFMDEPTSGLDARaaaiVMRTVRNTVDT-GRTVVCTIHQPSidIFEAFDELLLLKRG 1042
Cdd:TIGR00958 634 RKPRVLILDEATSALDAE----CEQLLQESRSRaSRTVLLIAHRLS--TVERADQILVLKKG 689
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
162-408 |
2.38e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 59.42 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 162 ILRDVSGIIKPSRMTLLLGPPSSGKTTLllalaGKLDQSLKV--TGRVTYNGHGLEEFVPqktsAYISQndvHVGVMtVQ 239
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTL-----TKLIQRFYVpeNGRVLVDGHDLALADP----AWLRR---QVGVV-LQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 240 ETLDFSarcqgvgtrydllselvRREKDAGILPEPEVDLfMKSIAAGNVKSSliTDYtlrILGLDICKDTVVGDEMIrGI 319
Cdd:cd03252 84 ENVLFN-----------------RSIRDNIALADPGMSM-ERVIEAAKLAGA--HDF---ISELPEGYDTIVGEQGA-GL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 320 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSLLQpapeTFELFDDIILLSEGQIV 399
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLS----TVKNADRIIVMEKGRIV 215
|
....*....
gi 18401096 400 YQGPRDHVL 408
Cdd:cd03252 216 EQGSHDELL 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
160-409 |
2.76e-09 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 58.99 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 160 VTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEFVPQKTSAY-IS---QNDVHVGV 235
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT---SGSVLFDGEDITGLPPHEIARLgIGrtfQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 236 MTVQETLDFSARCQgvgTRYDLLSELVRREKDAgiLPEpevdlfmksiAAGNVksslitdytLRILGLDickdtVVGDEM 315
Cdd:cd03219 90 LTVLENVMVAAQAR---TGSGLLLARARREERE--ARE----------RAEEL---------LERVGLA-----DLADRP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 316 IRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFtDATVL-----MSLLqpapetFELFDDI 390
Cdd:cd03219 141 AGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLlvehdMDVV------MSLADRV 213
|
250
....*....|....*....
gi 18401096 391 ILLSEGQIVYQGPRDHVLT 409
Cdd:cd03219 214 TVLDQGRVIAEGTPDEVRN 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
837-1042 |
2.76e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 61.36 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 837 DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDI--RIS-----GFPKRQETFARISGYC----- 904
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIiyHVAlcekcGYVERPSKVGEPCPVCggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 905 -EQNDIHSPQVTVKESLIYSAFLRLPKEVTKYEKMRFVDEVMELVE------LESLKDAV-----VGLPG-IT----GLS 967
Cdd:TIGR03269 91 pEEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEeigyegKEAVGRAVdliemVQLSHrIThiarDLS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18401096 968 TEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHQPSIdIFEAFDELLLLKRG 1042
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEV-IEDLSDKAIWLENG 245
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
857-1050 |
2.86e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 857 LMGVSGAGKTTLMDVLAGRKTGGYieGDIRISgfpkrqetfarisgyceqnDIHSPQvtvKESLIYSAFLRLPKEVTKYE 936
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKY--GTIQVG-------------------DIYIGD---KKNNHELITNPYSKKIKNFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 937 KMR-FVDEVMELVELESLKDAV----------VGLPGIT------------------------GLSTEQRKRLTIAVELV 981
Cdd:PRK13631 113 ELRrRVSMVFQFPEYQLFKDTIekdimfgpvaLGVKKSEakklakfylnkmglddsylerspfGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 982 ANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKRGGQVIYAGP 1050
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME-HVLEVADEVIVMDKGKILKTGTP 260
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
840-1042 |
2.99e-09 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 59.02 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 840 QLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDirisGFPkrqetfarISGYcEQNDIHS------ 911
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfyQPQGGQVLLD----GKP--------ISQY-EHKYLHSkvslvg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 912 --PQV---TVKESLIYS----AFLRLPKEVTKYEKMRFVDEvmelveLESLKDAVVGLPGiTGLSTEQRKRLTIAVELVA 982
Cdd:cd03248 95 qePVLfarSLQDNIAYGlqscSFECVKEAAQKAHAHSFISE------LASGYDTEVGEKG-SQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 983 NPSIIFMDEPTSGLDARAAAIVMRTVRNTvDTGRTVVCTIHQpsIDIFEAFDELLLLKRG 1042
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDW-PERRTVLVIAHR--LSTVERADQILVLDGG 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
848-1027 |
3.38e-09 |
|
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: 59.30 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 848 VFRPGVLTALMGVSGAGKTTLMDVLAGR------KTGGYIEGDIRISGF--PKRQETFARISGYcEQNDIHSPQVTVkes 919
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKlkpnlgKFDDPPDWDEILDEFrgSELQNYFTKLLEG-DVKVIVKPQYVD--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 920 liysaflRLPKEV--------TKYEKMRFVDEVMELVELESLKDAvvglpGITGLSTEQRKRLTIAVELVANPSIIFMDE 991
Cdd:cd03236 98 -------LIPKAVkgkvgellKKKDERGKLDELVDQLELRHVLDR-----NIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 18401096 992 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1027
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAV 201
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
851-1051 |
3.83e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.10 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 851 PGVLTALMGVSGAGKTTLMDVLAGrktggyI----EGDIRISGF-P-KRQETFAR-IS---GyceqndihspQ------- 913
Cdd:COG4586 47 PGEIVGFIGPNGAGKSTTIKMLTG------IlvptSGEVRVLGYvPfKRRKEFARrIGvvfG----------Qrsqlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 914 VTVKESL-----IYsaflRLPKEvtKYEKmrFVDEVMELVELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANPSIIF 988
Cdd:COG4586 111 LPAIDSFrllkaIY----RIPDA--EYKK--RLDELVELLDLGELLDTPVRQ-----LSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18401096 989 MDEPTSGLDaraaAIVMRTVRNTV-----DTGRTVVCTIHQPSiDIFEAFDELLLLKRgGQVIYAGPL 1051
Cdd:COG4586 178 LDEPTIGLD----VVSKEAIREFLkeynrERGTTILLTSHDMD-DIEALCDRVIVIDH-GRIIYDGSL 239
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
834-1042 |
4.09e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.01 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 834 VSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGrktggYI--EGDIRISGFPKRQ---ETFARISGYCEQND 908
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-----FLpyQGSLKINGIELREldpESWRKHLSWVGQNP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 909 iHSPQVTVKESLIYSAflrlpKEVTKyekmrfvDEVMELVELESLKDAVVGLP---------GITGLSTEQRKRLTIAVE 979
Cdd:PRK11174 433 -QLPHGTLRDNVLLGN-----PDASD-------EQLQQALENAWVSEFLPLLPqgldtpigdQAAGLSVGQAQRLALARA 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18401096 980 LVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQpsIDIFEAFDELLLLKRG 1042
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQAL-NAASRRQTTLMVTHQ--LEDLAQWDQIWVMQDG 559
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
128-361 |
4.28e-09 |
|
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: 60.84 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 128 GKRALPTLPNAALNIAER-GLRLLGFNFTKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGR 206
Cdd:TIGR02868 315 GPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL---QGE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 207 VTYNGHGLEEFVPQKTSAYIS--QNDVHVGVMTVQETLDFSArcqGVGTRYDLLSEL--VRREKDAGILPEpevdlfmks 282
Cdd:TIGR02868 392 VTLDGVPVSSLDQDEVRRRVSvcAQDAHLFDTTVRENLRLAR---PDATDEELWAALerVGLADWLRALPD--------- 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 283 iaagnvksslitdytlrilGLdickDTVVGdEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCL 361
Cdd:TIGR02868 460 -------------------GL----DTVLG-EGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL 514
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
842-1042 |
4.30e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.26 E-value: 4.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKRQETFARIS---GYCEQN-DIHSPQVT 915
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGllLPE----AGTITVGGMVLSEETVWDVRrqvGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 916 VKESLiysAFLRLPKEVTKYEKMRFVDEVMELVELESLKDAVvglPgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 995
Cdd:PRK13635 99 VQDDV---AFGLENIGVPREEMVERVDQALRQVGMEDFLNRE---P--HRLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18401096 996 LDARAAAIVMRTVRNTVDTGR-TVVCTIHqpsiDIFEAF--DELLLLKRG 1042
Cdd:PRK13635 171 LDPRGRREVLETVRQLKEQKGiTVLSITH----DLDEAAqaDRVIVMNKG 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
851-1049 |
5.41e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.78 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 851 PGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKRQETFARIS------------GYCEQN--DIHSPQVT- 915
Cdd:PRK11701 31 PGEVLGIVGESGSGKTTLLNALSARLAPD--AGEVHYRMRDGQLRDLYALSeaerrrllrtewGFVHQHprDGLRMQVSa 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 916 ---VKESLIYSAflrlpkeVTKYEKMRFV-DEVMELVELESlkDAVVGLPgiTGLSTEQRKRLTIAVELVANPSIIFMDE 991
Cdd:PRK11701 109 ggnIGERLMAVG-------ARHYGDIRATaGDWLERVEIDA--ARIDDLP--TTFSGGMQQRLQIARNLVTHPRLVFMDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18401096 992 PTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHqpsiDIfeAFDELL----LLKRGGQVIYAG 1049
Cdd:PRK11701 178 PTGGLDVSVQARLLDLLRGLVrELGLAVVIVTH----DL--AVARLLahrlLVMKQGRVVESG 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
161-409 |
5.73e-09 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 58.28 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEFVPQ------KTSAYISQNDVHVG 234
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD---SGEVLIDGEDISGLSEAelyrlrRRMGMLFQSGALFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 235 VMTVQETLDFsarcqgvgtrydLLselvrREKdaGILPEPEVDlfmkSIAAgnvksslitdYTLRILGLdicKDTVvgDE 314
Cdd:cd03261 91 SLTVFENVAF------------PL-----REH--TRLSEEEIR----EIVL----------EKLEAVGL---RGAE--DL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 315 MIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLM---SLlqpaPETFELFDDII 391
Cdd:cd03261 133 YPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMvthDL----DTAFAIADRIA 208
|
250
....*....|....*...
gi 18401096 392 LLSEGQIVYQGPRDHVLT 409
Cdd:cd03261 209 VLYDGKIVAEGTPEELRA 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
828-1050 |
8.09e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.00 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 828 EMKEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLaGRKTGGY----IEGDIRISG----------FPKR 893
Cdd:PRK14247 5 EIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF-NRLIELYpearVSGEVYLDGqdifkmdvieLRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 894 QETFARISgyceqNDIhsPQVTVKESLIYSAFL-RLPKevTKYEKMRFVDEVMELVEL-ESLKDAVVGLPGitGLSTEQR 971
Cdd:PRK14247 84 VQMVFQIP-----NPI--PNLSIFENVALGLKLnRLVK--SKKELQERVRWALEKAQLwDEVKDRLDAPAG--KLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 972 KRLTIAVELVANPSIIFMDEPTSGLD----ARAAAIVMRTVRNTvdtgrTVVCTIHQPS----IDIFEAFdellllKRGG 1043
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDpentAKIESLFLELKKDM-----TIVLVTHFPQqaarISDYVAF------LYKG 221
|
....*..
gi 18401096 1044 QVIYAGP 1050
Cdd:PRK14247 222 QIVEWGP 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
148-409 |
8.17e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.46 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 148 RLLGFNFT-KTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDqslKVTGRVTYNGHGLEEFVPQKTSAYI 226
Cdd:PRK10253 7 RLRGEQLTlGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT---PAHGHVWLDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 227 ---SQNDVHVGVMTVQETLdfsARC----QGVGTRYdllselvRREKDAGIlpepevdlfmksiaAGNVKSSLITDytlr 299
Cdd:PRK10253 84 gllAQNATTPGDITVQELV---ARGryphQPLFTRW-------RKEDEEAV--------------TKAMQATGITH---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 300 ilgldickdtvVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVR---FTDATVLMSL 376
Cdd:PRK10253 136 -----------LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRekgYTLAAVLHDL 204
|
250 260 270
....*....|....*....|....*....|...
gi 18401096 377 LQPAPETFELfddiILLSEGQIVYQGPRDHVLT 409
Cdd:PRK10253 205 NQACRYASHL----IALREGKIVAQGAPKEIVT 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
827-1050 |
9.70e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.82 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 827 KEMKEQGVSKDKlQLLKEVTGV---FRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE---GDIRISGFPKRQETFA 898
Cdd:TIGR03269 283 RNVSKRYISVDR-GVVKAVDNVsleVKEGEIFGIVGTSGAGKTTLSKIIAGvlEPTSGEVNvrvGDEWVDMTKPGPDGRG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 899 RISGYC----EQNDIHsPQVTVKESLIYSAFLRLPKEvtkYEKMRFVdEVMELVELESlKDAVVGLPGITG-LSTEQRKR 973
Cdd:TIGR03269 362 RAKRYIgilhQEYDLY-PHRTVLDNLTEAIGLELPDE---LARMKAV-ITLKMVGFDE-EKAEEILDKYPDeLSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 974 LTIAVELVANPSIIFMDEPTSGLDaraaAIVMRTVRNTV-----DTGRTVVCTIHqpSIDIFEAFDELLLLKRGGQVIYA 1048
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMD----PITKVDVTHSIlkareEMEQTFIIVSH--DMDFVLDVCDRAALMRDGKIVKI 509
|
..
gi 18401096 1049 GP 1050
Cdd:TIGR03269 510 GD 511
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
161-409 |
1.44e-08 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 56.91 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGkLdqsLKVT-GRVTYNGHGLEEFVPQKTSAYISQndvhVGV---- 235
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG-L---LRPDsGEILVDGQDITGLSEKELYELRRR----IGMlfqg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 236 ------MTVQETLDFSarcqgvgtrydllseLVRREKdagiLPEPEvdlfMKSIAagnvksslitDYTLRILGLDickdt 309
Cdd:COG1127 91 galfdsLTVFENVAFP---------------LREHTD----LSEAE----IRELV----------LEKLELVGLP----- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 310 VVGDEMIRGISGGQKKRV----TtgeMIVGPtKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLM---SLlqpaPE 382
Cdd:COG1127 133 GAADKMPSELSGGMRKRValarA---LALDP-EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVvthDL----DS 204
|
250 260
....*....|....*....|....*..
gi 18401096 383 TFELFDDIILLSEGQIVYQGPRDHVLT 409
Cdd:COG1127 205 AFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
856-1050 |
1.75e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.51 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 856 ALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKRQETFARIS---GYCEQN---DIHSPqvTVKESLIYSAF-LRL 928
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPT--SGSVLIRGEPITKENIREVRkfvGLVFQNpddQIFSP--TVEQDIAFGPInLGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 929 PKEVTKYEkmrfVDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1008
Cdd:PRK13652 110 DEETVAHR----VSSALHMLGLEELRDRVP-----HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18401096 1009 RNTVDT-GRTVVCTIHQPSIdIFEAFDELLLLKRGGQVIYAGP 1050
Cdd:PRK13652 181 NDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTV 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
130-393 |
1.89e-08 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 58.84 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 130 RALPTLPNAALNIAE-RGLRLLGFNFTKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVT 208
Cdd:TIGR02857 304 APRPLAGKAPVTAAPaSSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT---EGSIA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 209 YNGHGLEEFVP---QKTSAYISQNDvHVGVMTVQETLDFsarcqgvGTRYDLLSELVRREKDAGILPepevdlFMKSIAA 285
Cdd:TIGR02857 381 VNGVPLADADAdswRDQIAWVPQHP-FLFAGTIAENIRL-------ARPDASDAEIREALERAGLDE------FVAALPQ 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 286 GnvksslitdytlrilgldicKDTVVGDEMiRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIv 365
Cdd:TIGR02857 447 G--------------------LDTPIGEGG-AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL- 504
|
250 260
....*....|....*....|....*...
gi 18401096 366 rFTDATVLmsLLQPAPETFELFDDIILL 393
Cdd:TIGR02857 505 -AQGRTVL--LVTHRLALAALADRIVVL 529
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
857-997 |
1.94e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.58 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 857 LMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFP--KRqetfAR--IsGYCEQNdihsPQV----TVKESLIysAF 925
Cdd:COG1137 34 LLGPNGAGKTTTFYMIVGlvKPDSGRIFlDGEDITHLPmhKR----ARlgI-GYLPQE----ASIfrklTVEDNIL--AV 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18401096 926 LRLpKEVTKYEKMRFVDEVMELVELESLKDAvvglPGITgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 997
Cdd:COG1137 103 LEL-RKLSKKEREERLEELLEEFGITHLRKS----KAYS-LSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
828-1010 |
2.24e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 828 EMKEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKRqetFARISGyCEQN 907
Cdd:PRK13549 7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIFEGEELQ---ASNIRD-TERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 908 D---IHS-----PQVTVKESLiysaFLR---LPKEVTKYEKM-RFVDEVMELVELeslkDAVVGLPgITGLSTEQRKRLT 975
Cdd:PRK13549 83 GiaiIHQelalvKELSVLENI----FLGneiTPGGIMDYDAMyLRAQKLLAQLKL----DINPATP-VGNLGLGQQQLVE 153
|
170 180 190
....*....|....*....|....*....|....*
gi 18401096 976 IAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1010
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLTESETAVLLDIIRD 188
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
841-1057 |
2.33e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 56.84 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 841 LLKEVTGVFRPGVLTALMGVSGAGKTTL-------MDVLAGRKTggyIEGdIRISGFPkRQETFARISgyceqndihspq 913
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslaffrmVDIFDGKIV---IDG-IDISKLP-LHTLRSRLS------------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 914 VTVKESLIYSAFLRLPKEVtkyEKMRFVDEVMELVELESLKDAVVGLPG-----IT----GLSTEQRKRLTIAVELVANP 984
Cdd:cd03288 99 IILQDPILFSGSIRFNLDP---ECKCTDDRLWEALEIAQLKNMVKSLPGgldavVTeggeNFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18401096 985 SIIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQPSiDIFEAfDELLLLKRGGQVIYAGPLGQNSHK 1057
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVM-TAFADRTVVTIAHRVS-TILDA-DLVLVLSRGILVECDTPENLLAQE 245
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
172-402 |
2.36e-08 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 56.15 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 172 PSRMTLLLGPPSSGKTTLLLALAG--KLDQSLKVTGRVTYNGHGLEEFVP--QKTSAYISQNDVHVGVMTVQETLDFSAR 247
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGleKPDGGTIVLNGTVLFDSRKKINLPpqQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 248 CQGVGTRYDLLSELVRRekdagilpepevdlfmksiaagnvksslitdytlriLGLDickdtVVGDEMIRGISGGQKKRV 327
Cdd:cd03297 102 RKRNREDRISVDELLDL------------------------------------LGLD-----HLLNRYPAQLSGGEKQRV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18401096 328 TTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIV-RFTDATVLMSllQPAPETFELFDDIILLSEGQIVYQG 402
Cdd:cd03297 141 ALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKkNLNIPVIFVT--HDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
153-402 |
2.39e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. 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: 213236 [Multi-domain] Cd Length: 210 Bit Score: 55.75 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 153 NFTKTTK-VTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLdqsLKVTGRVTYNGHGLeEFVPQKTSAYISQNDV 231
Cdd:cd03269 5 NVTKRFGrVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII---LPDSGEVLFDGKPL-DIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 232 HVGVMTVQETLDFSARCQGVGTRYdllselvrrekdagilpepevdlfmksiAAGNVksslitDYTLRILGLDICKDTVV 311
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEE----------------------------ARRRI------DEWLERLELSEYANKRV 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 312 gDEMirgiSGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRfTDATVLMSLLQPApETFELFDDII 391
Cdd:cd03269 127 -EEL----SKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQME-LVEELCDRVL 199
|
250
....*....|.
gi 18401096 392 LLSEGQIVYQG 402
Cdd:cd03269 200 LLNKGRAVLYG 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
838-1026 |
2.67e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.32 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 838 KLQLLKEVTGVFRPGVLTALMGVSGAGKTTL------MDVLAGRKTggyIEGDIRISG---FPKRQET--FARISGYCEQ 906
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsinrMNDLNPEVT---ITGSIVYNGhniYSPRTDTvdLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 907 NDIHSPqVTVKESLIYSafLRLPKEVTKyekmRFVDEVMElvelESLKDAVVG-------LPGITGLSTEQRKRLTIAVE 979
Cdd:PRK14239 94 QPNPFP-MSIYENVVYG--LRLKGIKDK----QVLDEAVE----KSLKGASIWdevkdrlHDSALGLSGGQQQRVCIARV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18401096 980 LVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVD--TGRTVVCTIHQPS 1026
Cdd:PRK14239 163 LATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQAS 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
155-399 |
3.15e-08 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. 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: 213260 [Multi-domain] Cd Length: 220 Bit Score: 55.56 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 155 TKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEfvPQKTSAYISQNDVHVG 234
Cdd:cd03293 12 GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT---SGEVLVDGEPVTG--PGPDRGYVFQQDALLP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 235 VMTVQETLDFSARCQGVGTRydllsELVRREKDAgilpepevdlfmksiaagnvksslitdytLRILGLDickdtvvG-- 312
Cdd:cd03293 87 WLTVLDNVALGLELQGVPKA-----EARERAEEL-----------------------------LELVGLS-------Gfe 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 313 DEMIRGISGGQKKRV----TtgeMIVGPtKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLM---SLLqpapETFE 385
Cdd:cd03293 126 NAYPHQLSGGMRQRValarA---LAVDP-DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLvthDID----EAVF 197
|
250
....*....|....*.
gi 18401096 386 LFDDIILLSE--GQIV 399
Cdd:cd03293 198 LADRVVVLSArpGRIV 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
827-1001 |
3.25e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.98 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 827 KEMKEQGVSKDklqLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFP-------KRQETFAR 899
Cdd:PRK11629 13 KRYQEGSVQTD---VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP--TSGDVIFNGQPmsklssaAKAELRNQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 900 ISGYCEQNDIHSPQVTVKESLIysaflrLPKEVTKYEKMRFVDEVMELVeleslkdAVVGLPG-----ITGLSTEQRKRL 974
Cdd:PRK11629 88 KLGFIYQFHHLLPDFTALENVA------MPLLIGKKKPAEINSRALEML-------AAVGLEHranhrPSELSGGERQRV 154
|
170 180
....*....|....*....|....*..
gi 18401096 975 TIAVELVANPSIIFMDEPTSGLDARAA 1001
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNA 181
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
842-1042 |
3.32e-08 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 55.58 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLmdVLAGRKTGGYIEGDIRISGFP----KRQETFARISGyceqndIhsPQvtvk 917
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSL--LLALFRLVELSSGSILIDGVDiskiGLHDLRSRISI------I--PQ---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 918 ESLIYSAFLRL---PKEvtKYEKmrfvDEVMELVELESLKDAVVGLPGI---------TGLSTEQRKRLTIAVELVANPS 985
Cdd:cd03244 86 DPVLFSGTIRSnldPFG--EYSD----EELWQALERVGLKEFVESLPGGldtvveeggENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 18401096 986 IIFMDEPTSGLDARAAAIVMRTVRnTVDTGRTVVCTIHQpsIDIFEAFDELLLLKRG 1042
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIR-EAFKDCTVLTIAHR--LDTIIDSDRILVLDKG 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
852-1042 |
3.55e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 57.04 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGfpkrqETFARISgyCEQNDI----HS----PQVTVKESLIYS 923
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAGLEKP--TEGQIFIDG-----EDVTHRS--IQQRDIcmvfQSyalfPHMSLGENVGYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 924 afLRLPKeVTKYEKMRFVDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARaaai 1003
Cdd:PRK11432 103 --LKMLG-VPKEERKQRVKEALELVDLAGFEDRYV-----DQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN---- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18401096 1004 VMRTVRNTV-----DTGRTVVCTIHQPSidifEAF---DELLLLKRG 1042
Cdd:PRK11432 171 LRRSMREKIrelqqQFNITSLYVTHDQS----EAFavsDTVIVMNKG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
153-405 |
3.92e-08 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 55.65 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 153 NFTKT--TKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEFVPQKT------SA 224
Cdd:cd03256 5 NLSKTypNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGSVLIDGTDINKLKGKALrqlrrqIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 225 YISQNDVHVGVMTVQETLdFSARcqgVGTRyDLLSELVRREKDAGILpepevdlfmKSIAAGNvKSSLITDYTLRIlgld 304
Cdd:cd03256 82 MIFQQFNLIERLSVLENV-LSGR---LGRR-STWRSLFGLFPKEEKQ---------RALAALE-RVGLLDKAYQRA---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 305 ickdtvvgDEMirgiSGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSLLQPapetf 384
Cdd:cd03256 143 --------DQL----SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQV----- 205
|
250 260
....*....|....*....|....*
gi 18401096 385 EL----FDDIILLSEGQIVYQGPRD 405
Cdd:cd03256 206 DLareyADRIVGLKDGRIVFDGPPA 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
163-378 |
3.93e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 55.94 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 163 LRDVSGIIKPSRMTLLLGPPSSGKTTLLLAL--AGKLDQSLKVTGRVTYNGHGLeeFVPQKTSAYISQndvHVGV----- 235
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNI--YSPRTDTVDLRK---EIGMvfqqp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 236 ----MTVQETLDFSARCQGVGTRyDLLSELVRRE-KDAGILPEpevdlfmksiaagnVKsslitdytlrilglDICKDTV 310
Cdd:PRK14239 96 npfpMSIYENVVYGLRLKGIKDK-QVLDEAVEKSlKGASIWDE--------------VK--------------DRLHDSA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 311 VgdemirGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIV-RFTDATVLMSLLQ 378
Cdd:PRK14239 147 L------GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKdDYTMLLVTRSMQQ 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
153-398 |
4.07e-08 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 54.33 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 153 NFTKT-TKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGL---EEFVPQKTsAYISQ 228
Cdd:cd03230 5 NLSKRyGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD---SGEIKVLGKDIkkePEEVKRRI-GYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 229 NDVHVGVMTVQETLDFsarcqgvgtrydllselvrrekdagilpepevdlfmksiaagnvksslitdytlrilgldickd 308
Cdd:cd03230 81 EPSLYENLTVRENLKL---------------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 309 tvvgdemirgiSGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRfTDATVLMS--LLQpapETFEL 386
Cdd:cd03230 97 -----------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSshILE---EAERL 161
|
250
....*....|..
gi 18401096 387 FDDIILLSEGQI 398
Cdd:cd03230 162 CDRVAILNNGRI 173
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
839-997 |
4.36e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 56.23 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 839 LQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGgyieGDIRISGFP------KRQETFARISGYCEQNDIH 910
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGleSPSQ----GNVSWRGEPlaklnrAQRKAFRRDIQMVFQDSIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 911 S--PQVTVKESLiySAFLRLPKEVTKYEKMRFVDEVMELVEL-ESLKDAvvgLPGitGLSTEQRKRLTIAVELVANPSII 987
Cdd:PRK10419 101 AvnPRKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLdDSVLDK---RPP--QLSGGQLQRVCLARALAVEPKLL 173
|
170
....*....|
gi 18401096 988 FMDEPTSGLD 997
Cdd:PRK10419 174 ILDEAVSNLD 183
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
147-402 |
4.60e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.39 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 147 LRLLGFNFTKTTKVtiLRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGhgleefvpqktsayi 226
Cdd:PRK13636 8 VEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPS---SGRILFDG--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 227 sqndvhvgvmtvqETLDFSARCqgvgtrydlLSELvrREKDAGILPEPEVDLFmksiaagnvKSSLITDYTLRILGLDIC 306
Cdd:PRK13636 68 -------------KPIDYSRKG---------LMKL--RESVGMVFQDPDNQLF---------SASVYQDVSFGAVNLKLP 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 307 KDTV---VGDEMIR-GI-----------SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDAT 371
Cdd:PRK13636 115 EDEVrkrVDNALKRtGIehlkdkpthclSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLT 194
|
250 260 270
....*....|....*....|....*....|..
gi 18401096 372 VLMSLLQpaPETFELF-DDIILLSEGQIVYQG 402
Cdd:PRK13636 195 IIIATHD--IDIVPLYcDNVFVMKEGRVILQG 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
158-399 |
4.62e-08 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 55.43 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 158 TKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDqslKVT-GRVTYNGHGLEEFVPQKTSA-------YISQN 229
Cdd:COG1136 19 GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG-LD---RPTsGEVLIDGQDISSLSERELARlrrrhigFVFQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 230 dvH--VGVMTVQETLDFSARCQGVGTRydllselvRREKDAGILpepevdlfmksiaagnvksslitdytLRILGLDICK 307
Cdd:COG1136 95 --FnlLPELTALENVALPLLLAGVSRK--------ERRERAREL--------------------------LERVGLGDRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 308 DTVVGDemirgISGGQKKRVTTGEMIVGPTKTLFMDEIsTG-LDSSTTYQIVKCLQEIVRFTDATVLMsllqpA---PET 383
Cdd:COG1136 139 DHRPSQ-----LSGGQQQRVAIARALVNRPKLILADEP-TGnLDSKTGEEVLELLRELNRELGTTIVM-----VthdPEL 207
|
250
....*....|....*.
gi 18401096 384 FELFDDIILLSEGQIV 399
Cdd:COG1136 208 AARADRVIRLRDGRIV 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
161-250 |
4.95e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.88 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLdqsLKVTGRVTYNGHGLEEFVPQKTSAYISQNDVHVGVMTVQE 240
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLL---PPAAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAE 92
|
90
....*....|
gi 18401096 241 TLDFSARCQG 250
Cdd:PRK13539 93 NLEFWAAFLG 102
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
816-1049 |
4.96e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.66 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 816 FDNVNYYVDMpkemKEQGVSkdklqllkEVTGVFRPGVLTALMGVSGAGKTTLMDVL--AGRKTGGYIegdiRISGFPKR 893
Cdd:PRK13657 337 FDDVSFSYDN----SRQGVE--------DVSFEAKPGQTVAIVGPTGAGKSTLINLLqrVFDPQSGRI----LIDGTDIR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 894 QETFARISgyceqndiHSPQVTVKESLIY----SAFLRLPKEVTKYEKMRFVDE---VMELVELESLK-DAVVGLPGiTG 965
Cdd:PRK13657 401 TVTRASLR--------RNIAVVFQDAGLFnrsiEDNIRVGRPDATDEEMRAAAEraqAHDFIERKPDGyDTVVGERG-RQ 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 966 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSIdIFEAfDELLLLKRgGQV 1045
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL-DELMKGRTTFIIAHRLST-VRNA-DRILVFDN-GRV 547
|
....
gi 18401096 1046 IYAG 1049
Cdd:PRK13657 548 VESG 551
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
153-397 |
5.62e-08 |
|
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: 54.12 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 153 NFTKT-TKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDQslKVTGRVTYNGHGLeefvpQKTSAYISQNDV 231
Cdd:cd03229 5 NVSKRyGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAG-LEE--PDSGSILIDGEDL-----TDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 232 HVGvMTVQEtldfsarcqgvgtrYDLLSELVRREkdagilpepevdlfmksiaagNVksslitdytlrILGLdickdtvv 311
Cdd:cd03229 77 RIG-MVFQD--------------FALFPHLTVLE---------------------NI-----------ALGL-------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 312 gdemirgiSGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSLLQPApETFELFDDII 391
Cdd:cd03229 102 --------SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLD-EAARLADRVV 172
|
....*.
gi 18401096 392 LLSEGQ 397
Cdd:cd03229 173 VLRDGK 178
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
835-1060 |
6.29e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.77 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 835 SKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKRQETFARIS---GYCEQN-D 908
Cdd:PRK13632 18 PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGllKPQ----SGEIKIDGITISKENLKEIRkkiGIIFQNpD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 909 IHSPQVTVKESLiysAFLRLPKEVTKYEKMRFVDEVMELVELESLKDAVvglPgiTGLSTEQRKRLTIAVELVANPSIIF 988
Cdd:PRK13632 94 NQFIGATVEDDI---AFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKE---P--QNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 989 MDEPTSGLDARAAAIV---MRTVRNTVDtgRTVVCTIHqpsiDIFEAF--DELLLLKrGGQVIYAG-PLG-QNSHKIIE 1060
Cdd:PRK13632 166 FDESTSMLDPKGKREIkkiMVDLRKTRK--KTLISITH----DMDEAIlaDKVIVFS-EGKLIAQGkPKEiLNNKEILE 237
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
859-1006 |
7.54e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.19 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 859 GVSGAGKTTLMDVLAGRK--TGG--YIeGDIRISGFPKRQetfaRISGYCEQNDIHSPQVTVKESLiysAF-LRLPKeVT 933
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEdiTSGdlFI-GEKRMNDVPPAE----RGVGMVFQSYALYPHLSVAENM---SFgLKLAG-AK 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18401096 934 KYEKMRFVDEVMELVELESLKDAvvgLPgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDArAAAIVMR 1006
Cdd:PRK11000 107 KEEINQRVNQVAEVLQLAHLLDR---KP--KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA-ALRVQMR 173
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
828-1046 |
8.80e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.37 E-value: 8.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 828 EMKeqGVSKD--KLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKR----QETFARIS 901
Cdd:TIGR02633 3 EMK--GIVKTfgGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKasniRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 902 GYCEQNDIHSPQVTVKESLIYSAFLRLPKEVTKYEKMrfVDEVMELVELESLKDAVVGLPgITGLSTEQRKRLTIAVELV 981
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAM--YLRAKNLLRELQLDADNVTRP-VGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18401096 982 ANPSIIFMDEPTSGLDARAAAIVMRTVRNTvdTGRTVVCTIHQPSIDIFEAFDELLLLKRGGQVI 1046
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDL--KAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
812-1050 |
9.42e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.22 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 812 LTMSFDNVNYYVDMPKEMKEQGVSKDKLQLLKevtgvfrpGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEgdirisg 889
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMEKKGLDNISFELEE--------GSFVALVGHTGSGKSTLMQHFNAllKPSSGTIT------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 890 fpkrqetfarISGYceqndihspQVTVKESliYSAFLRLPKEVTKY----EKMRFVDEVMELVEL----------ESLKD 955
Cdd:PRK13641 66 ----------IAGY---------HITPETG--NKNLKKLRKKVSLVfqfpEAQLFENTVLKDVEFgpknfgfsedEAKEK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 956 AV-----VGLP------GITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1024
Cdd:PRK13641 125 ALkwlkkVGLSedliskSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHN 204
|
250 260
....*....|....*....|....*.
gi 18401096 1025 PSiDIFEAFDELLLLKRGGQVIYAGP 1050
Cdd:PRK13641 205 MD-DVAEYADDVLVLEHGKLIKHASP 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
832-1024 |
1.11e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 54.33 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSKD--KLQLLKEVTGVFRPGVLTALMGVSGAGKTTLM---DVLAGRKTGGYIEGDIRISGfPKRQETFARI-SGYCE 905
Cdd:PRK09493 5 KNVSKHfgPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLEEITSGDLIVDGLKVND-PKVDERLIRQeAGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 906 QNDIHSPQVTVKESLIYSaflrlPKEVTKYEKMRFVDEVMELVeleslkdAVVGLPGITG-----LSTEQRKRLTIAVEL 980
Cdd:PRK09493 84 QQFYLFPHLTALENVMFG-----PLRVRGASKEEAEKQARELL-------AKVGLAERAHhypseLSGGQQQRVAIARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18401096 981 VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1024
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
854-999 |
1.20e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 55.72 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 854 LTaLMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpkrqETFARISGycEQNDIHS--------PQVTVKESLiysAF 925
Cdd:PRK09452 43 LT-LLGPSGCGKTTVLRLIAGFETPD--SGRIMLDG-----QDITHVPA--ENRHVNTvfqsyalfPHMTVFENV---AF 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18401096 926 -LRLPKeVTKYEKMRFVDEVMELVELESLKDAvvglpGITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 999
Cdd:PRK09452 110 gLRMQK-TPAAEITPRVMEALRMVQLEEFAQR-----KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
837-1027 |
1.53e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.89 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 837 DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLagrktgGYIE----GDIRISG-----------FPKRQETFaris 901
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL------GCLDkptsGTYRVAGqdvatldadalAQLRREHF---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 902 GYCEQNDIHSPQVTVKESLiysaflRLPKEVTKYEKMRFVDEVMELVELESLKDAVVGLPGitGLSTEQRKRLTIAVELV 981
Cdd:PRK10535 89 GFIFQRYHLLSHLTAAQNV------EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPS--QLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18401096 982 ANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1027
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQV 206
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
814-1042 |
2.21e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 55.41 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 814 MSFDNVNYYVDmpkemkeqgvSKDKLQLlKEVTGVFRPGVLTALMGVSGAGKTTLMDVLagrkTGGY--IEGDIRISGFP 891
Cdd:PRK11176 342 IEFRNVTFTYP----------GKEVPAL-RNINFKIPAGKTVALVGRSGSGKSTIANLL----TRFYdiDEGEILLDGHD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 892 KRQETFARISGYC---EQNdIHSPQVTVKESLIYSA---FLRlpKEVTKYEKMRFVdevMELVE-LESLKDAVVGLPGIT 964
Cdd:PRK11176 407 LRDYTLASLRNQValvSQN-VHLFNDTIANNIAYARteqYSR--EQIEEAARMAYA---MDFINkMDNGLDTVIGENGVL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 965 gLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAaivmRTVRNTVDT---GRTVVCTIHQPSidIFEAFDELLLLKR 1041
Cdd:PRK11176 481 -LSGGQRQRIAIARALLRDSPILILDEATSALDTESE----RAIQAALDElqkNRTSLVIAHRLS--TIEKADEILVVED 553
|
.
gi 18401096 1042 G 1042
Cdd:PRK11176 554 G 554
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
163-428 |
2.22e-07 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 53.49 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 163 LRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAG--KLDqslkvTGRVTYNGHGLEEFVPQKTS-AYISQNDVHVGVMTVQ 239
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGfiKPD-----SGKILLNGKDITNLPPEKRDiSYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 240 ETLDFSARcqgvgtrydllseLVRREKdagilpePEVDLFMKSIAagnvksslitdytlRILGLDickdtVVGDEMIRGI 319
Cdd:cd03299 90 KNIAYGLK-------------KRKVDK-------KEIERKVLEIA--------------EMLGID-----HLLNRKPETL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 320 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLmSLLQPAPETFELFDDIILLSEGQIV 399
Cdd:cd03299 131 SGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVL-HVTHDFEEAWALADKVAIMLNGKLI 209
|
250 260
....*....|....*....|....*....
gi 18401096 400 YQGPRDHVltffetcgFKCPDRKGTADFL 428
Cdd:cd03299 210 QVGKPEEV--------FKKPKNEFVAEFL 230
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
810-999 |
2.28e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.22 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 810 TPLTMSFDNVNY-YVDMPkemkeqgvskdkLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLagrkTGGY--IEGDIR 886
Cdd:PRK11160 335 DQVSLTLNNVSFtYPDQP------------QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL----TRAWdpQQGEIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 887 ISGFPkrqetfarISGYCEQNDIHSPQVTVKESLIYSAFLR----LPKEVTKYEKMRfvdEVMELVELESLKDAVVGLPG 962
Cdd:PRK11160 399 LNGQP--------IADYSEAALRQAISVVSQRVHLFSATLRdnllLAAPNASDEALI---EVLQQVGLEKLLEDDKGLNA 467
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 18401096 963 ITG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 999
Cdd:PRK11160 468 WLGeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAE 509
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
828-1019 |
2.38e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 828 EMKeqGVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISGFPKRqetfarisgy 903
Cdd:COG3845 7 ELR--GITKrfGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGlyQPD----SGEILIDGKPVR---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 904 ceqndIHSPQV-------------------TVKESLIYSAfLRLPKEVTKYEKMRfvDEVMELVELESLK---DAVVGlp 961
Cdd:COG3845 71 -----IRSPRDaialgigmvhqhfmlvpnlTVAENIVLGL-EPTKGGRLDRKAAR--ARIRELSERYGLDvdpDAKVE-- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 18401096 962 gitGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVV 1019
Cdd:COG3845 141 ---DLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSII 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
825-1074 |
2.62e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 825 MPKEMKEQGVSKD--KLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPkrqetFARIS- 901
Cdd:PRK15439 8 APPLLCARSISKQysGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD--SGTLEIGGNP-----CARLTp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 902 GYCEQNDIH--------SPQVTVKESLIYsaflRLPKEVTKYEKMRFVdevmeLVELE-SLK-DAVVGLpgitgLSTEQR 971
Cdd:PRK15439 81 AKAHQLGIYlvpqepllFPNLSVKENILF----GLPKRQASMQKMKQL-----LAALGcQLDlDSSAGS-----LEVADR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 972 KRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLkRGGQVIYAGPL 1051
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLP-EIRQLADRISVM-RDGTIALSGKT 224
|
250 260
....*....|....*....|...
gi 18401096 1052 GQNSHKIIeyFQAIhgVPKIKEK 1074
Cdd:PRK15439 225 ADLSTDDI--IQAI--TPAAREK 243
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
163-404 |
3.14e-07 |
|
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: 53.11 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 163 LRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDQSLKvtGRVTYNGHGLEEFVPQKTS-AYISQNDVHVGVMTVQET 241
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAG-LERPDS--GTILFGGEDATDVPVQERNvGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 242 LDFSARCQGVGTRYdllselvrrekdagilPEPEVDLFMKSIaagnvksslitdytLRILGLDickdtVVGDEMIRGISG 321
Cdd:cd03296 95 VAFGLRVKPRSERP----------------PEAEIRAKVHEL--------------LKLVQLD-----WLADRYPAQLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 322 GQKKRVTTGEMIVGPTKTLFMDEISTGLDSsttyQIVKCLQEIVR-FTDATVLMSLL--QPAPETFELFDDIILLSEGQI 398
Cdd:cd03296 140 GQRQRVALARALAVEPKVLLLDEPFGALDA----KVRKELRRWLRrLHDELHVTTVFvtHDQEEALEVADRVVVMNKGRI 215
|
250
....*....|....
gi 18401096 399 --------VYQGPR 404
Cdd:cd03296 216 eqvgtpdeVYDHPA 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
855-997 |
3.30e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.11 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 855 TALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISG---FPKRQETFA-----RIsGYCEQNDIHSPQVTVKESLIYSafl 926
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQ--KGRIVLNGrvlFDAEKGICLppekrRI-GYVFQDARLFPHYKVRGNLRYG--- 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18401096 927 rlpkeVTKYEKMRFvDEVMELVELESLKDAvvgLPGitGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 997
Cdd:PRK11144 101 -----MAKSMVAQF-DKIVALLGIEPLLDR---YPG--SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
852-1042 |
3.54e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.22 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKRQETFARIS---GYCEQNdihsPQVTVKESLI-YSAFLR 927
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIGIEK--VKSGEIFYNNQAITDDNFEKLRkhiGIVFQN----PDNQFVGSIVkYDVAFG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 928 LPKEVTKYEKM-RFVDEVMELVELESLKDAVvglPgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMR 1006
Cdd:PRK13648 109 LENHAVPYDEMhRRVSEALKQVDMLERADYE---P--NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 18401096 1007 TVRNT-VDTGRTVVCTIHqpsiDIFEAF--DELLLLKRG 1042
Cdd:PRK13648 184 LVRKVkSEHNITIISITH----DLSEAMeaDHVIVMNKG 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
849-1024 |
3.79e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.02 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 849 FRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEG--DIRISGFPKRQETfarisGYCEQNDIHSPQVTVKESLIYS 923
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGllpPTSGTVLVGgkDIETNLDAVRQSL-----GMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 924 AFLrlpkevtkyeKMRFVDEVMelVELES-LKDAvvGL-----PGITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 997
Cdd:TIGR01257 1028 AQL----------KGRSWEEAQ--LEMEAmLEDT--GLhhkrnEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190
....*....|....*....|....*....|
gi 18401096 998 A---RAAAIVMRTVRntvdTGRTVVCTIHQ 1024
Cdd:TIGR01257 1094 PysrRSIWDLLLKYR----SGRTIIMSTHH 1119
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
834-1052 |
3.91e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.29 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 834 VSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGY------IEGDIRISGFPKRQ---ETFARISGYC 904
Cdd:PRK13547 9 VARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarVTGDVTLNGEPLAAidaPRLARLRAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 905 EQNDIHSPQVTVKESLIYSAFLRLPKE-VTKYEKMRFVDEVMELVELESL--KDavvglpgITGLSTEQRKRLTIAVEL- 980
Cdd:PRK13547 89 PQAAQPAFAFSAREIVLLGRYPHARRAgALTHRDGEIAWQALALAGATALvgRD-------VTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 981 --------VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTI-HQPSIDIFEAfDELLLLKRGGQVIYAGPL 1051
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIvHDPNLAARHA-DRIAMLADGAIVAHGAPA 240
|
.
gi 18401096 1052 G 1052
Cdd:PRK13547 241 D 241
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
841-1024 |
4.14e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.26 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 841 LLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIegdirisgFPKRQETFARISGYCEQ-------NDIhS 911
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGllNPEKGEI--------LFERQSIKKDLCTYQKQlcfvghrSGI-N 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 912 PQVTVKESLIYSaflrLPKEVTKYEkmrfVDEVMELVELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANPSIIFMDE 991
Cdd:PRK13540 87 PYLTLRENCLYD----IHFSPGAVG----ITELCRLFSLEHLIDYPCGL-----LSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 18401096 992 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1024
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
851-1046 |
4.21e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 851 PGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE---GDIRISGfPK-RQEtfARISgyceqnDIHS-----PQVTVKES 919
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGiyTRDAGSILylgKEVTFNG-PKsSQE--AGIG------IIHQelnliPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 920 LIysaflrLPKEVT------KYEKMRfvDEVMELVELESLKDAVVGLPGitGLSTEQRKRLTIAVELVANPSIIFMDEPT 993
Cdd:PRK10762 100 IF------LGREFVnrfgriDWKKMY--AEADKLLARLNLRFSSDKLVG--ELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 18401096 994 SGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLkRGGQVI 1046
Cdd:PRK10762 170 DALTDTETESLFRVIRELKSQGRGIVYISHRLK-EIFEICDDVTVF-RDGQFI 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
160-402 |
4.82e-07 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 52.37 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 160 VTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGL--EEFVPQKTSAYISQNDVHVGVMT 237
Cdd:cd03266 18 VQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD---AGFATVDGFDVvkEPAEARRRLGFVSDSTGLYDRLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 238 VQETLDFSARCQGvgtrydllseLVRREKDAGIlpEPEVDLF-MKSIAagnvksslitdytlrilgldickdtvvgDEMI 316
Cdd:cd03266 95 ARENLEYFAGLYG----------LKGDELTARL--EELADRLgMEELL----------------------------DRRV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 317 RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIvRFTDATVLMS--LLQpapETFELFDDIILLS 394
Cdd:cd03266 135 GGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSthIMQ---EVERLCDRVVVLH 210
|
....*...
gi 18401096 395 EGQIVYQG 402
Cdd:cd03266 211 RGRVVYEG 218
|
|
| ABC_trans_N |
pfam14510 |
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins ... |
88-138 |
5.13e-07 |
|
ABC-transporter N-terminal; This domain is found at the N-terminus of ABC-transporter proteins from fungi, plants to higher eukaryotes. It is predicted to be an intracellular domain.
Pssm-ID: 464194 Cd Length: 80 Bit Score: 48.47 E-value: 5.13e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 18401096 88 EEDNEKFLKKFRNRIDRV-RIKLPTVEVRFEKVTIEAnCHIGKRALPTLPNA 138
Cdd:pfam14510 30 EFDLRKWLKNLRRLIDEDgYIKPRKLGVAFKNLTVSG-VGAGADYQPTVGNA 80
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
176-402 |
5.13e-07 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. 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: 213265 [Multi-domain] Cd Length: 211 Bit Score: 52.11 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 176 TLLLGPPSSGKTTLLLALAG-KLDQSlkvtGRVTYNG--HGLEEFVPQKTSAYISQNDV--HvgvMTVQETLDFsarcqG 250
Cdd:cd03298 27 TAIVGPSGSGKSTLLNLIAGfETPQS----GRVLINGvdVTAAPPADRPVSMLFQENNLfaH---LTVEQNVGL-----G 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 251 VGTRYDLLSElvRREKDAGILPEPEVDLFMKSIAagnvksslitdytlrilgldickdtvvgdemiRGISGGQKKRVTTG 330
Cdd:cd03298 95 LSPGLKLTAE--DRQAIEVALARVGLAGLEKRLP--------------------------------GELSGGERQRVALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18401096 331 EMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSLLQPApETFELFDDIILLSEGQIVYQG 402
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPE-DAKRLAQRVVFLDNGRIAAQG 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
161-409 |
5.48e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 52.71 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQslkVTGRVTYNGHGLEEFVPQKTSAYIS---QndvhvgVMT 237
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP---QSGTVFLGDKPISMLSSRQLARRLAllpQ------HHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 238 VQEtldfsarcqGVGTRydllsELVRREKDagilpePEVDLFMKSiaagNVKSSLITDYTLRILGLDICKDTVVGDemir 317
Cdd:PRK11231 87 TPE---------GITVR-----ELVAYGRS------PWLSLWGRL----SAEDNARVNQAMEQTRINHLADRRLTD---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 318 gISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRF--TDATVLMSLLQPApetfELFDDIILLSE 395
Cdd:PRK11231 139 -LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgkTVVTVLHDLNQAS----RYCDHLVVLAN 213
|
250
....*....|....
gi 18401096 396 GQIVYQGPRDHVLT 409
Cdd:PRK11231 214 GHVMAQGTPEEVMT 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
152-398 |
6.17e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 53.16 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 152 FNFTKttkvtILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLeefvpqktsAYISQNDV 231
Cdd:PRK10851 12 FGRTQ-----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT---SGHIRFHGTDV---------SRLHARDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 232 HVGV----------MTVQETLDFSarcqgvgtrydlLSELVRREKdagilpepevdlfmKSIAAGNVKSSLItdytlril 301
Cdd:PRK10851 75 KVGFvfqhyalfrhMTVFDNIAFG------------LTVLPRRER--------------PNAAAIKAKVTQL-------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 302 gLDICKDTVVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQI---VKCLQEIVRFTdaTVLMSLLQ 378
Cdd:PRK10851 121 -LEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELrrwLRQLHEELKFT--SVFVTHDQ 197
|
250 260
....*....|....*....|
gi 18401096 379 paPETFELFDDIILLSEGQI 398
Cdd:PRK10851 198 --EEAMEVADRVVVMSQGNI 215
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
1193-1348 |
6.47e-07 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 51.35 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1193 VIGAMYAAVLFVGVNNSSSVqplIAVERS--VFYRERAAEMySALPYALAQVVCEIPYVLIQTTYYTLIIYAMMCFEWTL 1270
Cdd:COG0842 6 VPGLLAMSLLFTALMLTALS---IAREREqgTLERLLVTPV-SRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18401096 1271 AKFFWFYFVSFMSFLYFTYYGMMTVALTPNQQVAAVFAGAFYGLFNLFSGFVIPRPRIPKWWIWYYWICPVAWTVYGL 1348
Cdd:COG0842 82 LSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
845-1042 |
7.44e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.24 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 845 VTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyiEGDIRISGFPKRQ---ETFARISGYCEQNDIHSPQVTVKESLI 921
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG---SGSIQFAGQPLEAwsaAELARHRAYLSQQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 922 ysafLRLPKEVTKYEKMRFVDEVMELVELESLkdavvgLP-GITGLS-TE-QRKRLTiAVEL----VANPS--IIFMDEP 992
Cdd:PRK03695 92 ----LHQPDKTRTEAVASALNEVAEALGLDDK------LGrSVNQLSgGEwQRVRLA-AVVLqvwpDINPAgqLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18401096 993 TSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAfDELLLLKRG 1042
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHA-DRVWLLKQG 209
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
852-1049 |
7.58e-07 |
|
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: 50.78 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMdvlagrKTGGYIEGDIRISGFPKRqetfarisgyceqndiHSPQVTVkesliysaflrlpke 931
Cdd:cd03238 21 NVLVVVTGVSGSGKSTLV------NEGLYASGKARLISFLPK----------------FSRNKLI--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 932 vtkyekmrFVDEVMELVEleslkdavVGLPGIT------GLSTEQRKRLTIAVELVANP--SIIFMDEPTSGLDARAAAI 1003
Cdd:cd03238 64 --------FIDQLQFLID--------VGLGYLTlgqklsTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQ 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18401096 1004 VMRTVRNTVDTGRTVVCTIHQPsiDIFEAFDELLLL-----KRGGQVIYAG 1049
Cdd:cd03238 128 LLEVIKGLIDLGNTVILIEHNL--DVLSSADWIIDFgpgsgKSGGKVVFSG 176
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
163-402 |
7.66e-07 |
|
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: 51.44 E-value: 7.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 163 LRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEFVPQKTSAyisqndvHVGVMTvQETL 242
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT---SGSVLLDGTDIRQLDPADLRR-------NIGYVP-QDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 243 DFSarcqgvGTRYDLLSELVRREKDAGILPEPEVdlfmksiaAGnvksslITDYTLRI-LGLDickdTVVGdEMIRGISG 321
Cdd:cd03245 89 LFY------GTLRDNITLGAPLADDERILRAAEL--------AG------VTDFVNKHpNGLD----LQIG-ERGRGLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 322 GQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRftDATVL-----MSLLQpapetfeLFDDIILLSEG 396
Cdd:cd03245 144 GQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIiithrPSLLD-------LVDRIIVMDSG 214
|
....*.
gi 18401096 397 QIVYQG 402
Cdd:cd03245 215 RIVADG 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
160-405 |
1.10e-06 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 51.39 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 160 VTILRDVSGIIKPSRMTLLLGPPSSGKTTLLlalagKLDQSL--KVTGRVTYNGHGLEEFVPQKTS---AYISQnDVHVG 234
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVV-----SLLERFydPTSGEILLDGVDIRDLNLRWLRsqiGLVSQ-EPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 235 VMTVQETLDFSarcqgvgtRYDLLSELVRRekdagilpepevdlfmksiAAgnvKSSLITDYtlrILGLDICKDTVVGDe 314
Cdd:cd03249 90 DGTIAENIRYG--------KPDATDEEVEE-------------------AA---KKANIHDF---IMSLPDGYDTLVGE- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 315 miRG--ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRftDATVLM-----SLLQPApetfelf 387
Cdd:cd03249 136 --RGsqLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIViahrlSTIRNA------- 204
|
250
....*....|....*...
gi 18401096 388 DDIILLSEGQIVYQGPRD 405
Cdd:cd03249 205 DLIAVLQNGQVVEQGTHD 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
812-1076 |
1.11e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.09 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 812 LTMSFDNVNYyvdmpkeMKEQGVSKDKlQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRIS 888
Cdd:PRK13646 1 MTIRFDNVSY-------TYQKGTPYEH-QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAllKPTTGTVTvDDITIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 889 GFPKRQE--TFARISGYCEQndihSPQVTVKESLIYSAFLRLPKEVtkyeKMRfVDEVME-----LVELESLKDAVVGLP 961
Cdd:PRK13646 73 HKTKDKYirPVRKRIGMVFQ----FPESQLFEDTVEREIIFGPKNF----KMN-LDEVKNyahrlLMDLGFSRDVMSQSP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 962 giTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQPSiDIFEAFDELLLLK 1040
Cdd:PRK13646 144 --FQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENKTIILVSHDMN-EVARYADEVIVMK 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 18401096 1041 RGGQVIYAGP--LGQNSHKIIEYFQAIHGVPK----IKEKYN 1076
Cdd:PRK13646 221 EGSIVSQTSPkeLFKDKKKLADWHIGLPEIVQlqydFEQKYQ 262
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
856-1045 |
1.15e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.18 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 856 ALMGVSGAGKTTLMDVLAgrktgGYI---EGDIRISGFPkrqetFARISGYCEQNDIHSPQ---VTVKESLIysAFLRLP 929
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLM-----GYYpltEGEIRLDGRP-----LSSLSHSVLRQGVAMVQqdpVVLADTFL--ANVTLG 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 930 KEVTKyEKMRFVDEVMELVEL-ESLKDAVVGLPGITG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA---RAAAI 1003
Cdd:PRK10790 439 RDISE-EQVWQALETVQLAELaRSLPDGLYTPLGEQGnnLSVGQKQLLALARVLVQTPQILILDEATANIDSgteQAIQQ 517
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 18401096 1004 VMRTVRNTVdtgrTVVCTIHQPSIdIFEAfDELLLLKRGGQV 1045
Cdd:PRK10790 518 ALAAVREHT----TLVVIAHRLST-IVEA-DTILVLHRGQAV 553
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
840-1049 |
1.17e-06 |
|
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: 50.39 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 840 QLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPkrqetfarISGYCEQndiHSPQVTVkes 919
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ--QGEITLDGVP--------VSDLEKA---LSSLISV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 920 LIYSAFLrlpkevtkyekmrFVDEVMElveleslkdaVVGLPgitgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 999
Cdd:cd03247 80 LNQRPYL-------------FDTTLRN----------NLGRR----FSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 18401096 1000 AAAIVMRTVRNtVDTGRTVV-CTIHQPSIdifEAFDELLLLKRgGQVIYAG 1049
Cdd:cd03247 133 TERQLLSLIFE-VLKDKTLIwITHHLTGI---EHMDKILFLEN-GKIIMQG 178
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
833-1089 |
1.27e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 833 GVSKD--KLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTggyiEGDIRISG----FPKRQETFARISGYC 904
Cdd:PRK10982 3 NISKSfpGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGiyQKD----SGSILFQGkeidFKSSKEALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 905 EQNDIHSPQVTVKESLIYSaflRLPKevtkyeKMRFVDEVMELVELESLKDA----VVGLPGITGLSTEQRKRLTIAVEL 980
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLG---RYPT------KGMFVDQDKMYRDTKAIFDEldidIDPRAKVATLSVSQMQMIEIAKAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 981 VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLkRGGQVIYAGPL-GQNSHKII 1059
Cdd:PRK10982 150 SYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKME-EIFQLCDEITIL-RDGQWIATQPLaGLTMDKII 227
|
250 260 270
....*....|....*....|....*....|.
gi 18401096 1060 EYFQAIHGVPKIKEKYN-PATWMLEVSSMAA 1089
Cdd:PRK10982 228 AMMVGRSLTQRFPDKENkPGEVILEVRNLTS 258
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
841-1021 |
1.40e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 841 LLKEVTGVFRPGVLTALMGVSGAGKTTLMDVL--AGRKTGGY-IEGDIRISG---FPKRQE-TFARISGYCEQNDIHSPQ 913
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrMNDKVSGYrYSGDVLLGGrsiFNYRDVlEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 914 VTVKESLiysAFLRLPKEVTKYEkMRFVDE--VMELVELESLKDAVVGLPgiTGLSTEQRKRLTIAVELVANPSIIFMDE 991
Cdd:PRK14271 116 SIMDNVL---AGVRAHKLVPRKE-FRGVAQarLTEVGLWDAVKDRLSDSP--FRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190
....*....|....*....|....*....|
gi 18401096 992 PTSGLDARAAAIVMRTVRNTVDTGRTVVCT 1021
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
853-1026 |
1.72e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.00 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 853 VLTALMGVSGAGKTTLM---DVLAGRKTGGYIEGDIRISGFPKRQETFARIS-----GYCEQNDIHSPQVTVKES----L 920
Cdd:PRK14267 31 GVFALMGPSGCGKSTLLrtfNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEvrrevGMVFQYPNPFPHLTIYDNvaigV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 921 IYSAFLRLPKEVTK-----YEKMRFVDEVmelveleslKDAVVGLPGitGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 995
Cdd:PRK14267 111 KLNGLVKSKKELDErvewaLKKAALWDEV---------KDRLNDYPS--NLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190
....*....|....*....|....*....|.
gi 18401096 996 LDARAAAIVMRTVRNtVDTGRTVVCTIHQPS 1026
Cdd:PRK14267 180 IDPVGTAKIEELLFE-LKKEYTIVLVTHSPA 209
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
852-1073 |
1.91e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 51.28 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFpkrqetfaRISGYCEQNDIHSPQVTV------KESLIYS-- 923
Cdd:PRK13649 33 GSYTAFIGHTGSGKSTIMQLLNGLHVP--TQGSVRVDDT--------LITSTSKNKDIKQIRKKVglvfqfPESQLFEet 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 924 -----AFLRLPKEVTKYEKMRFVDEVMELVEL-ESLKDAvvglpGITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 997
Cdd:PRK13649 103 vlkdvAFGPQNFGVSQEEAEALAREKLALVGIsESLFEK-----NPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 998 ARAAAIVMRTVRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKRGGQVIYAGPlgqnshkiIEYFQAIH-------GVPK 1070
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMD-DVANYADFVYVLEKGKLVLSGKP--------KDIFQDVDfleekqlGVPK 248
|
...
gi 18401096 1071 IKE 1073
Cdd:PRK13649 249 ITK 251
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
828-1023 |
2.00e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 828 EMKEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISG---FPKRQETFARISGYC 904
Cdd:CHL00131 9 EIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILEGDILFKGesiLDLEPEERAHLGIFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 905 E-QNDIHSPQVTVKE--SLIYSA---FLRLPkEVTKYEKMRFVDEVMELVELES--LKDAVVglpgiTGLSTEQRKRLTI 976
Cdd:CHL00131 89 AfQYPIEIPGVSNADflRLAYNSkrkFQGLP-ELDPLEFLEIINEKLKLVGMDPsfLSRNVN-----EGFSGGEKKRNEI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 18401096 977 AVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1023
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
840-1024 |
2.04e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 50.74 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 840 QLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpkRQETFARIS-GYCEQNDIHSPQ-VTVK 917
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPS--EGSIVVNG---QTINLVRDKdGQLKVADKNQLRlLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 918 ESLIYSAFlrlpkevTKYEKMRFVDEVME-------LVELESLKDAVVGLP--GITG---------LSTEQRKRLTIAVE 979
Cdd:PRK10619 94 LTMVFQHF-------NLWSHMTVLENVMEapiqvlgLSKQEARERAVKYLAkvGIDEraqgkypvhLSGGQQQRVSIARA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18401096 980 LVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1024
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
149-402 |
2.18e-06 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 50.41 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 149 LLGFNFTKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGhgleeFVPQK-TSAYIS 227
Cdd:cd03267 23 LKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT---SGEVRVAG-----LVPWKrRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 228 QndvhVGVMTVQET---LDFSARcqgvgTRYDLLSELVRREKDAgilpepevdlfmksiaagnvksslitdYTLRILGL- 303
Cdd:cd03267 95 R----IGVVFGQKTqlwWDLPVI-----DSFYLLAAIYDLPPAR---------------------------FKKRLDELs 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 304 DICKDTVVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMsllqpapeT 383
Cdd:cd03267 139 ELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLL--------T 210
|
250 260
....*....|....*....|....*.
gi 18401096 384 FELFDDI-------ILLSEGQIVYQG 402
Cdd:cd03267 211 SHYMKDIealarrvLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
154-405 |
2.55e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 50.95 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 154 FT-KTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSLKVTGRVTYNGHGLEEF----VPQKTSAYISQ 228
Cdd:PRK13640 13 FTyPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKtvwdIREKVGIVFQN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 229 NDVHVGVMTVQETLDFSARCQGVgtrydllselvrrekdagilPEPEvdlfMKSIAAGNVKSSLITDYTlrilgldickd 308
Cdd:PRK13640 93 PDNQFVGATVGDDVAFGLENRAV--------------------PRPE----MIKIVRDVLADVGMLDYI----------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 309 tvvgDEMIRGISGGQKKRVT-TGEMIVGPtKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLmSLLQPAPETfELF 387
Cdd:PRK13640 138 ----DSEPANLSGGQKQRVAiAGILAVEP-KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVI-SITHDIDEA-NMA 210
|
250
....*....|....*....
gi 18401096 388 DDIILLSEGQIVYQG-PRD 405
Cdd:PRK13640 211 DQVLVLDDGKLLAQGsPVE 229
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
162-413 |
3.56e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.39 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 162 ILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDqslkvtgrvtynghgleefvPQKTSayisqndvhvgVMTVQET 241
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLR--------------------PQKGA-----------VLWQGKP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 242 LDFSARcqGVgtrydllseLVRREKDAGILPEPEVDLFMKSIaagnvkSSLITdYTLRILGL---DICKD-----TVVGD 313
Cdd:PRK13638 65 LDYSKR--GL---------LALRQQVATVFQDPEQQIFYTDI------DSDIA-FSLRNLGVpeaEITRRvdealTLVDA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 314 EMIRG-----ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMSllQPAPETFELFD 388
Cdd:PRK13638 127 QHFRHqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISS--HDIDLIYEISD 204
|
250 260
....*....|....*....|....*
gi 18401096 389 DIILLSEGQIVYQGPRDHVLTFFET 413
Cdd:PRK13638 205 AVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
166-409 |
4.11e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.93 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 166 VSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvtGRVTYNGHGLEEFVPQKTS---AYISQNDVHVGVMTVQETL 242
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS----GSIQFAGQPLEAWSAAELArhrAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 243 DFSarcQGVGTR----YDLLSELVRRekdagilpepevdlfmksiaagnvksslitdytlriLGLDickdtvvgDEMIRG 318
Cdd:PRK03695 91 TLH---QPDKTRteavASALNEVAEA------------------------------------LGLD--------DKLGRS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 319 I---SGGQKKRVTTGEMI--VGPT-----KTLFMDEISTGLD---SSTTYQIVK--CLQEIvrftdaTVLMS------LL 377
Cdd:PRK03695 124 VnqlSGGEWQRVRLAAVVlqVWPDinpagQLLLLDEPMNSLDvaqQAALDRLLSelCQQGI------AVVMSshdlnhTL 197
|
250 260 270
....*....|....*....|....*....|..
gi 18401096 378 QPApetfelfDDIILLSEGQIVYQGPRDHVLT 409
Cdd:PRK03695 198 RHA-------DRVWLLKQGKLLASGRRDEVLT 222
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
851-1023 |
4.13e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 851 PGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKRQETFARISGYCEQNDIHSPQVTVKESLIYSAFLRlpk 930
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVE--SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLH--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 931 evtKYEKMRFVDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1010
Cdd:PRK13543 111 ---GRRAKQMPGSALAIVGLAGYEDTLV-----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISA 182
|
170
....*....|...
gi 18401096 1011 TVDTGRTVVCTIH 1023
Cdd:PRK13543 183 HLRGGGAALVTTH 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
837-1025 |
4.45e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.05 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 837 DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVL--------AGRKTGG---YIEGDI-RISGFPKRQETfarisGYC 904
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlieiydSKIKVDGkvlYFGKDIfQIDAIKLRKEV-----GMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 905 EQNDIHSPQVTVKESLIYSAFLRLPKEvtKYEKMRFVDEVMELVELESLKDAVVGLPGiTGLSTEQRKRLTIAVELVANP 984
Cdd:PRK14246 96 FQQPNPFPHLSIYDNIAYPLKSHGIKE--KREIKKIVEECLRKVGLWKEVYDRLNSPA-SQLSGGQQQRLTIARALALKP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18401096 985 SIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQP 1025
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLI-TELKNEIAIVIVSHNP 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
161-402 |
5.22e-06 |
|
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: 48.46 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSLkvtGRVTYNGHgleefvpqKTSAYisqndvhvgvmtvqe 240
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQ---GEITLDGV--------PVSDL--------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 241 tldfsarcqgvgtrYDLLSELVrrekdaGILPEpEVDLFmksiaagnvksslitdytlrilgldickDTVVGDEMIRGIS 320
Cdd:cd03247 70 --------------EKALSSLI------SVLNQ-RPYLF----------------------------DTTLRNNLGRRFS 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 321 GGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRftDATVLM---SLLqpapeTFELFDDIILLSEGQ 397
Cdd:cd03247 101 GGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWithHLT-----GIEHMDKILFLENGK 173
|
....*
gi 18401096 398 IVYQG 402
Cdd:cd03247 174 IIMQG 178
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
946-1058 |
5.35e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.50 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 946 ELVELESLKDAVVglPGITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIhQP 1025
Cdd:NF000106 127 ELLERFSLTEAAG--RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT-QY 203
|
90 100 110
....*....|....*....|....*....|...
gi 18401096 1026 SIDIFEAFDELLLLKRgGQVIYAGPLGQNSHKI 1058
Cdd:NF000106 204 MEEAEQLAHELTVIDR-GRVIADGKVDELKTKV 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
817-1033 |
5.65e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.65 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 817 DNVNYYVDMPKEMkeQGVSKDKLQllkevtgvfrpGVLTALMGVSGAGKTTLMDVLAGRKTggyIEGDIRISGfpkRQET 896
Cdd:PRK14258 11 NNLSFYYDTQKIL--EGVSMEIYQ-----------SKVTAIIGPSGCGKSTFLKCLNRMNE---LESEVRVEG---RVEF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 897 FAR--------ISGYCEQNDIHSPQVTVKESLIYSAFLRLPKEVTKYEKMRFVDEVMELVELESLKDAVVGL--PGITGL 966
Cdd:PRK14258 72 FNQniyerrvnLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKihKSALDL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18401096 967 STEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHQ----PSIDIFEAF 1033
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSlRLRSELTMVIVSHNlhqvSRLSDFTAF 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
838-1022 |
5.67e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.11 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 838 KLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-ISGFPKRQETFARISGYCEQNDIHSpQV 914
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGdpRATSGRIVFDGKdITDWQTAKIMREAVAIVPEGRRVFS-RM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 915 TVKESLIYSAFLrlpKEVTKYEKMrfVDEVMELveLESLKDAVVGLPGItgLSTEQRKRLTIAVELVANPSIIFMDEPTS 994
Cdd:PRK11614 96 TVEENLAMGGFF---AERDQFQER--IKWVYEL--FPRLHERRIQRAGT--MSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
170 180
....*....|....*....|....*...
gi 18401096 995 GLdaraAAIVMRTVRNTVDTGRTVVCTI 1022
Cdd:PRK11614 167 GL----APIIIQQIFDTIEQLREQGMTI 190
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
840-1050 |
5.79e-06 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. 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: 213269 [Multi-domain] Cd Length: 207 Bit Score: 48.95 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 840 QLLKEVTGVFRPGVLTALMGVSGAGKTTLmdVLAGRKTGGYIEGDIRISGfpkrqetfarisgyceQNDIHSPQVTVKES 919
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLEAEEGKIEIDG----------------IDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 920 L--------IYSAFLRLPKEV-TKYEKmrfvDEVMELVELESlkdavvglpGITGLSTEQRKRLTIAVELVANPSIIFMD 990
Cdd:cd03369 84 LtiipqdptLFSGTIRSNLDPfDEYSD----EEIYGALRVSE---------GGLNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18401096 991 EPTSGLDARAAAIVMRTVRNTVdTGRTVVCTIH--QPSIDifeaFDELLLLKRGGQVIYAGP 1050
Cdd:cd03369 151 EATASIDYATDALIQKTIREEF-TNSTILTIAHrlRTIID----YDKILVMDAGEVKEYDHP 207
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
828-1027 |
7.39e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 828 EMKEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDIRISGFPKRQETFARISG----Y 903
Cdd:PRK09580 3 SIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLELSPEDRAGegifM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 904 CEQNDIHSPQVTVKESLIYSA-FLRLPKEVTKYEKMRFVDEVMELVELESLKDAVVGLPGITGLSTEQRKRLTIAVELVA 982
Cdd:PRK09580 83 AFQYPVEIPGVSNQFFLQTALnAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 18401096 983 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1027
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRI 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
155-455 |
9.30e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 155 TKTTKVTiLRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKL----DQSLKVTGRVTYnghgleefVPQKTSAYISqnd 230
Cdd:PLN03232 626 SKTSKPT-LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELshaeTSSVVIRGSVAY--------VPQVSWIFNA--- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 231 vhvgvmTVQETLDFsarcqgvGTRYDllSELVRREKDAGILpEPEVDLFMksiaagnvksslitdytlrilGLDIckdTV 310
Cdd:PLN03232 694 ------TVRENILF-------GSDFE--SERYWRAIDVTAL-QHDLDLLP---------------------GRDL---TE 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 311 VGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIV-KCLQEIVRFTDATVLMSLLQPAPetfeLFDD 389
Cdd:PLN03232 734 IGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDELKGKTRVLVTNQLHFLP----LMDR 808
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18401096 390 IILLSEGQIVYQGprdhvlTFFE-----TCGFKCPDRKGTADFLQEVTSRKDQeqywADSKKPYSYISVSE 455
Cdd:PLN03232 809 IILVSEGMIKEEG------TFAElsksgSLFKKLMENAGKMDATQEVNTNDEN----ILKLGPTVTIDVSE 869
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
847-1009 |
1.08e-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: 48.56 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 847 GVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpkrqetfARISgyceqndiHSPQ-VTVKESLIYSAF 925
Cdd:cd03237 20 GSISESEVIGILGPNGIGKTTFIKMLAGVLKPD--EGDIEIEL--------DTVS--------YKPQyIKADYEGTVRDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 926 LRlpkEVTK--YEKMRFVDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1003
Cdd:cd03237 82 LS---SITKdfYTHPYFKTEIAKPLQIEQILDREV-----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
....*.
gi 18401096 1004 VMRTVR 1009
Cdd:cd03237 154 ASKVIR 159
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
842-1049 |
1.23e-05 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 47.91 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRIS-------GFpkrqetfarisgyceqndihSP 912
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiyPPDSGTVTVRGRVSsllglggGF--------------------NP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 913 QVTVKESLIYSAFL--RLPKEVTKYEkmrfvDEVMELVELESLKDavvgLPgITGLSTEQRKRLTIAVELVANPSIIFMD 990
Cdd:cd03220 98 ELTGRENIYLNGRLlgLSRKEIDEKI-----DEIIEFSELGDFID----LP-VKTYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 991 EPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLLKRgGQVIYAG 1049
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEK-GKIRFDG 224
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
852-1024 |
1.39e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 47.71 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKRQETFARISGYCEQNDIHSPQ------VTVKESLIYSAf 925
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQT--LEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQkpwllnATVEENITFGS- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 926 lrlPKEVTKYEKMRFVDEVMELVELESLKDAV-VGLPGITgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1004
Cdd:cd03290 104 ---PFNKQRYKAVTDACSLQPDIDLLPFGDQTeIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHL 179
|
170 180
....*....|....*....|..
gi 18401096 1005 MRT--VRNTVDTGRTVVCTIHQ 1024
Cdd:cd03290 180 MQEgiLKFLQDDKRTLVLVTHK 201
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
844-1019 |
1.61e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 49.05 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 844 EVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYiEGDIRISGFP-----KRQETFARISGYCEQNDIHS--PQVTV 916
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKF-EGNVFINGKPvdirnPAQAIRAGIAMVPEDRKRHGivPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 917 KESLIYSAflrlpkeVTKYEKMRFVDEVMEL------VELESLKDAVVGLPgITGLSTEQRKRLTIAVELVANPSIIFMD 990
Cdd:TIGR02633 357 GKNITLSV-------LKSFCFKMRIDAAAELqiigsaIQRLKVKTASPFLP-IGRLSGGNQQKAVLAKMLLTNPRVLILD 428
|
170 180
....*....|....*....|....*....
gi 18401096 991 EPTSGLDARAAAIVMRTVRNTVDTGRTVV 1019
Cdd:TIGR02633 429 EPTRGVDVGAKYEIYKLINQLAQEGVAII 457
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
852-997 |
1.98e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 48.06 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKRQ---ETFARISGYCEQNDIHSPQVTVKESLiysAFLRL 928
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTP--AHGHVWLDGEHIQHyasKEVARRIGLLAQNATTPGDITVQELV---ARGRY 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18401096 929 PKE--VTKYEK--MRFVDEVMELVELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 997
Cdd:PRK10253 108 PHQplFTRWRKedEEAVTKAMQATGITHLADQSVDT-----LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
835-1019 |
1.99e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.01 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 835 SKDKLQLlKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISgfPKRQ-ETFARISGYCEQNDIH 910
Cdd:PRK09700 273 SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGvdkRAGGEIRLNGKDIS--PRSPlDAVKKGMAYITESRRD 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 911 S---PQVTVKESLIYSAFLRLpkevTKYE-KMRFVDEVMELV------ELESLKDAVVGlPGITGLSTEQRKRLTIAVEL 980
Cdd:PRK09700 350 NgffPNFSIAQNMAISRSLKD----GGYKgAMGLFHEVDEQRtaenqrELLALKCHSVN-QNITELSGGNQQKVLISKWL 424
|
170 180 190
....*....|....*....|....*....|....*....
gi 18401096 981 VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVV 1019
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
842-1050 |
2.02e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 48.06 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKRQEtFARISGYCEQNdihsPQV---- 914
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGllrPQKGKVLVSGIDTGDFSKLQG-IRKLVGIVFQN----PETqfvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 915 -TVKESLIYSA--FLRLPKEVTKYEKMRFVDEVMELVELESLKDavvglpgitgLSTEQRKRLTIAVELVANPSIIFMDE 991
Cdd:PRK13644 93 rTVEEDLAFGPenLCLPPIEIRKRVDRALAEIGLEKYRHRSPKT----------LSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 992 PTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAFDELLLLKRGGQVIYAGP 1050
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLHEKGKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEP 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
850-997 |
2.28e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 47.27 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 850 RPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKRQETFAR--ISGYCEQNDIHsPQVTVKE--SLIYSAF 925
Cdd:PRK10771 23 ERGERVAILGPSGAGKSTLLNLIAGFLTPA--SGSLTLNGQDHTTTPPSRrpVSMLFQENNLF-SHLTVAQniGLGLNPG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18401096 926 LRLpkevTKYEKMRfVDEVMELVELESLKDAvvgLPGitGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 997
Cdd:PRK10771 100 LKL----NAAQREK-LHAIARQMGIEDLLAR---LPG--QLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
161-344 |
3.35e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 48.14 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNghgleefvPQKTSAYISQNDVHVGVMTVQE 240
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD---SGEVSIP--------KGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 241 TLdfsarCQGVGTRYDLLSELVRREKDagiLPEPEVDlfMKSIAAGNVKSSLITDYTL-----RIL-GLDIckDTVVGDE 314
Cdd:COG0488 81 TV-----LDGDAELRALEAELEELEAK---LAEPDED--LERLAELQEEFEALGGWEAearaeEILsGLGF--PEEDLDR 148
|
170 180 190
....*....|....*....|....*....|
gi 18401096 315 MIRGISGGQKKRVTTGEMIVGPTKTLFMDE 344
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDE 178
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
852-999 |
3.57e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 47.91 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGD-IRISGFPKRQetfaRISGYCEQNDIHSPQVTVKESLiysAFL-- 926
Cdd:PRK11607 45 GEIFALLGASGCGKSTLLRMLAGfeQPTAGQIMLDgVDLSHVPPYQ----RPINMMFQSYALFPHMTVEQNI---AFGlk 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18401096 927 --RLPK-EVTkyekmrfvDEVMELVELESLKDAVVGLPgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 999
Cdd:PRK11607 118 qdKLPKaEIA--------SRVNEMLGLVHMQEFAKRKP--HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
852-1050 |
3.58e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.40 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKRQET---FARISGYCEQN-DIHSPQVTVKESLiysAFLR 927
Cdd:PRK13642 33 GEWVSIIGQNGSGKSTTARLIDGLFE--EFEGKVKIDGELLTAENvwnLRRKIGMVFQNpDNQFVGATVEDDV---AFGM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 928 LPKEVTKYEKMRFVDEVMELVELESLKDAVVGLpgitgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRT 1007
Cdd:PRK13642 108 ENQGIPREEMIKRVDEALLAVNMLDFKTREPAR-----LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 18401096 1008 VRNTVDTGRTVVCTIHQpSIDIFEAFDELLLLKRGGQVIYAGP 1050
Cdd:PRK13642 183 IHEIKEKYQLTVLSITH-DLDEAASSDRILVMKAGEIIKEAAP 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
849-1049 |
3.96e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.31 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 849 FRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRI-SGFPKRQET--FARISGYCEQ-NDIHSPQVTVKESLi 921
Cdd:PRK13645 34 FKKNKVTCVIGTTGSGKSTMIQLTNGliiSETGQTIVGDYAIpANLKKIKEVkrLRKEIGLVFQfPEYQLFQETIEKDI- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 922 ysAFLRLPKEVTKYEKMRFVDEVMELVELEslKDAVVGLPgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1001
Cdd:PRK13645 113 --AFGPVNLGENKQEAYKKVPELLKLVQLP--EDYVKRSP--FELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18401096 1002 AIVMRT-VRNTVDTGRTVVCTIHQPSiDIFEAFDELLLLKRgGQVIYAG 1049
Cdd:PRK13645 187 EDFINLfERLNKEYKKRIIMVTHNMD-QVLRIADEVIVMHE-GKVISIG 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
842-1042 |
5.04e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 46.65 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMdvlagRKTGGYIE---GDIRISGFPKRQETFARIS---GYCEQN-DIHSPQV 914
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTV-----RLIDGLLEaesGQIIIDGDLLTEENVWDIRhkiGMVFQNpDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 915 TVKESLiysAFlRLPKEVTKYEKMR-FVDEVMELVELESLKDAVvglPgiTGLSTEQRKRLTIAVELVANPSIIFMDEPT 993
Cdd:PRK13650 98 TVEDDV---AF-GLENKGIPHEEMKeRVNEALELVGMQDFKERE---P--ARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 18401096 994 SGLDARAAAIVMRTVRNTVDT-GRTVVCTIHqpSIDIFEAFDELLLLKRG 1042
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDyQMTVISITH--DLDEVALSDRVLVMKNG 216
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
849-1041 |
5.26e-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: 45.04 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 849 FRPGVLTALMGVSGAGKTTLMDVLagrktgGYIEGdirisgfpkrQETFARISGYCEQNDIHSPQVTVkeSLIYSaflrl 928
Cdd:cd03227 18 FGEGSLTIITGPNGSGKSTILDAI------GLALG----------GAQSATRRRSGVKAGCIVAAVSA--ELIFT----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 929 pkevtkyekmrfvdevmelveleslkdavvglpgITGLSTEQRKRLTIAVEL----VANPSIIFMDEPTSGLDARAAAIV 1004
Cdd:cd03227 75 ----------------------------------RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQAL 120
|
170 180 190
....*....|....*....|....*....|....*..
gi 18401096 1005 MRTVRNTVDTGRTVVCTIHQPsiDIFEAFDELLLLKR 1041
Cdd:cd03227 121 AEAILEHLVKGAQVIVITHLP--ELAELADKLIHIKK 155
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
833-1008 |
5.32e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 47.75 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 833 GVSK--DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGR---KTGGYIEGD-IRISGFPKRQETFarisgyceq 906
Cdd:COG0488 320 GLSKsyGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGElepDSGTVKLGEtVKIGYFDQHQEEL--------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 907 ndihSPQVTVKESLIYSAFLRLPKEVTKY-EKMRFV-DEVMELVEleslkdavvglpgitGLSTEQRKRLTIAVELVANP 984
Cdd:COG0488 391 ----DPDKTVLDELRDGAPGGTEQEVRGYlGRFLFSgDDAFKPVG---------------VLSGGEKARLALAKLLLSPP 451
|
170 180
....*....|....*....|....
gi 18401096 985 SIIFMDEPTSGLDaraaaIVMRTV 1008
Cdd:COG0488 452 NVLLLDEPTNHLD-----IETLEA 470
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
930-1024 |
5.53e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 930 KEVTKYEKMRFVDEVMElvELESLKDAVVGlPGITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVR 1009
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIE--SLPNKYDTNVG-PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
|
90
....*....|....*.
gi 18401096 1010 NTVDTG-RTVVCTIHQ 1024
Cdd:PTZ00265 1403 DIKDKAdKTIITIAHR 1418
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
313-409 |
5.92e-05 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 46.23 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 313 DEMIRGISGGQKKRVttgeMI----VGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMS--LLQPAPETFel 386
Cdd:COG1119 137 DRPFGTLSQGEQRRV----LIaralVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVthHVEEIPPGI-- 210
|
90 100
....*....|....*....|...
gi 18401096 387 fDDIILLSEGQIVYQGPRDHVLT 409
Cdd:COG1119 211 -THVLLLKDGRVVAAGPKEEVLT 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
829-997 |
5.98e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.26 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 829 MKEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAgrktgGYIEGDiriSGFPKRQETFaRIsGYCEQN- 907
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVL-----GLVAPD---EGVIKRNGKL-RI-GYVPQKl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 908 --DIHSPqVTVKEsliysaFLRLPKEVTKYEKMrfvdEVMELVELESLKDAvvglPgITGLSTEQRKRLTIAVELVANPS 985
Cdd:PRK09544 77 ylDTTLP-LTVNR------FLRLRPGTKKEDIL----PALKRVQAGHLIDA----P-MQKLSGGETQRVLLARALLNRPQ 140
|
170
....*....|..
gi 18401096 986 IIFMDEPTSGLD 997
Cdd:PRK09544 141 LLVLDEPTQGVD 152
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
839-1049 |
6.28e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.62 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 839 LQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGR--KTGGYIEGDIRISGFPKRQETFARisgYCEQNDIHSPQV-- 914
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllPDTGTIEWIFKDEKNKKKTKEKEK---VLEKLVIQKTRFkk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 915 -------------------------TVKESLIYSAflrLPKEVTKYEKMRFVDEVMELVEL--ESLKDAVVGLPGitgls 967
Cdd:PRK13651 97 ikkikeirrrvgvvfqfaeyqlfeqTIEKDIIFGP---VSMGVSKEEAKKRAAKYIELVGLdeSYLQRSPFELSG----- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 968 tEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAFDELLLLKRGGQVIY 1047
Cdd:PRK13651 169 -GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH--DLDNVLEWTKRTIFFKDGKIIK 245
|
..
gi 18401096 1048 AG 1049
Cdd:PRK13651 246 DG 247
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
832-997 |
7.44e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 46.61 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 832 QGVSK------DKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE-GDIRISGFPKRQETFARisg 902
Cdd:COG1135 5 ENLSKtfptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLleRPTSGSVLvDGVDLTALSERELRAAR--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 903 yceqNDI-----HS---PQVTVKESLiysAF-LRL---PKEVTKyEKmrfVDEVMELVELESLKDAvvgLPGItgLSTEQ 970
Cdd:COG1135 82 ----RKIgmifqHFnllSSRTVAENV---ALpLEIagvPKAEIR-KR---VAELLELVGLSDKADA---YPSQ--LSGGQ 145
|
170 180
....*....|....*....|....*..
gi 18401096 971 RKRLTIAVELVANPSIIFMDEPTSGLD 997
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
842-997 |
8.96e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTT----LMDVLAGRktggyieGDIRISGFPKRQETFARISGYCEQ--------NDI 909
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-------GEIWFDGQPLHNLNRRQLLPVRHRiqvvfqdpNSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 910 HSPQVTVKEslIYSAFLRL-PKEVTKYEKMRFVDEVMELVELeslkDAVVGLPGITGLSTEQRKRLTIAVELVANPSIIF 988
Cdd:PRK15134 375 LNPRLNVLQ--IIEEGLRVhQPTLSAAQREQQVIAVMEEVGL----DPETRHRYPAEFSGGQRQRIAIARALILKPSLII 448
|
....*....
gi 18401096 989 MDEPTSGLD 997
Cdd:PRK15134 449 LDEPTSSLD 457
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
170-375 |
9.50e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.32 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 170 IKPSRMTLLLGPPSSGKTTLLLALAGklDQSLkVTGRVTYNGHGLEEFVPQ--KTSAYISQNDVHVGVMTVQETLDFSAR 247
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTG--DTTV-TSGDATVAGKSILTNISDvhQNMGYCPQFDAIDDLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 248 CQGVgtrydllselvrrekdagilPEPEVDLfmksiaagnvksslITDYTLRILGLDICKDTVVGDemirgISGGQKKRV 327
Cdd:TIGR01257 2039 LRGV--------------------PAEEIEK--------------VANWSIQSLGLSLYADRLAGT-----YSGGNKRKL 2079
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 18401096 328 TTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMS 375
Cdd:TIGR01257 2080 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTS 2127
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
160-214 |
9.67e-05 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 45.50 E-value: 9.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 18401096 160 VTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDQSlkVTGRVTYNGHGL 214
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG-LDRP--TSGTVRLAGQDL 76
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
851-1042 |
1.09e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 851 PGVLTALMGVSGAGKTTLMDVLAGRktggyiegdirisgFPKRQETFARISGyceqndihspqvtvkesliysaflrlpk 930
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE--------------LGPPGGGVIYIDG---------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 931 evtkyekmrfvdevmELVELESLKDAVVGLPGITGLSTEQRKRLTIAVELV--ANPSIIFMDEPTSGLDARAAAIVMRTV 1008
Cdd:smart00382 39 ---------------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALArkLKPDVLILDEITSLLDAEQEALLLLLE 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 18401096 1009 RNTVD------TGRTVVCTIHQPSI----DIFEAFDELLLLKRG 1042
Cdd:smart00382 104 ELRLLlllkseKNLTVILTTNDEKDlgpaLLRRRFDRRIVLLLI 147
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
161-409 |
1.24e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 45.47 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDqslkvtgrvtynghgleefvpqKTSAYISQNDVHVG---VMT 237
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMND----------------------KVSGYRYSGDVLLGgrsIFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 238 VQETLDFSARcqgVGTrydllseLVRRekdagilPEPEVDLFMKSIAAGNVKSSLITDYTLR--------ILGL-DICKD 308
Cdd:PRK14271 93 YRDVLEFRRR---VGM-------LFQR-------PNPFPMSIMDNVLAGVRAHKLVPRKEFRgvaqarltEVGLwDAVKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 309 TVvGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIV-RFTDATVLMSLLQPApetfELF 387
Cdd:PRK14271 156 RL-SDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAdRLTVIIVTHNLAQAA----RIS 229
|
250 260
....*....|....*....|..
gi 18401096 388 DDIILLSEGQIVYQGPRDHVLT 409
Cdd:PRK14271 230 DRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
319-365 |
1.56e-04 |
|
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: 43.85 E-value: 1.56e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 18401096 319 ISGGQKKRV-TTGEMIVGPTKTLF-MDEISTGLDSSTTYQIVKCLQEIV 365
Cdd:cd03238 88 LSGGELQRVkLASELFSEPPGTLFiLDEPSTGLHQQDINQLLEVIKGLI 136
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
854-997 |
1.74e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.16 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 854 LTALMGVSGAGKTTLMDVLagRKTGGYIEGdirisgfpkrqetfARISG--YCEQNDIHSPQVTVKE--SLIYSAFLR-- 927
Cdd:PRK14243 38 ITAFIGPSGCGKSTILRCF--NRLNDLIPG--------------FRVEGkvTFHGKNLYAPDVDPVEvrRRIGMVFQKpn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 928 -LPKEVtkYEKMRFVDEVM-------ELVElESLKDAVV-----------GLpgitGLSTEQRKRLTIAVELVANPSIIF 988
Cdd:PRK14243 102 pFPKSI--YDNIAYGARINgykgdmdELVE-RSLRQAALwdevkdklkqsGL----SLSGGQQQRLCIARAIAVQPEVIL 174
|
....*....
gi 18401096 989 MDEPTSGLD 997
Cdd:PRK14243 175 MDEPCSALD 183
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
162-405 |
2.02e-04 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 45.93 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 162 ILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDqslkVT-GRVTYNGHGLEEfvpqktsayISQNDV--HVGVMTv 238
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD----PTsGRILIDGVDIRD---------LTLESLrrQIGVVP- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 239 QETLDFSarcqgvGT-----RYdllselvrREKDAgilPEPEVdlfmksIAAgnvksslitdytLRILGLD--ICK---- 307
Cdd:COG1132 421 QDTFLFS------GTireniRY--------GRPDA---TDEEV------EEA------------AKAAQAHefIEAlpdg 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 308 -DTVVGDemiRGI--SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRftDATVLM-----SLLQP 379
Cdd:COG1132 466 yDTVVGE---RGVnlSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIViahrlSTIRN 540
|
250 260
....*....|....*....|....*.
gi 18401096 380 ApetfelfDDIILLSEGQIVYQGPRD 405
Cdd:COG1132 541 A-------DRILVLDDGRIVEQGTHE 559
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
153-411 |
2.08e-04 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 45.56 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 153 NFTKTTK-VTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDQSLKVTGRVTYNGHGLEEFVPQKTSAYISQNDV 231
Cdd:TIGR03269 5 NLTKKFDgKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG-MDQYEPTSGRIIYHVALCEKCGYVERPSKVGEPCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 232 HVGVMTVQETLDFSArcqgvgtrydlLSELVRRE--KDAGILPEPEVDLFMKSIAAGNVKSSL-ITDYTLRI---LGLDI 305
Cdd:TIGR03269 84 VCGGTLEPEEVDFWN-----------LSDKLRRRirKRIAIMLQRTFALYGDDTVLDNVLEALeEIGYEGKEavgRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 306 CKDTVVGDEMI---RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATvlMSLLQPAPE 382
Cdd:TIGR03269 153 IEMVQLSHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIS--MVLTSHWPE 230
|
250 260 270
....*....|....*....|....*....|
gi 18401096 383 TFE-LFDDIILLSEGQIVYQGPRDHVLTFF 411
Cdd:TIGR03269 231 VIEdLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
841-997 |
2.11e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.06 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 841 LLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpkrqetfaRISgYCEQNDIHSPQvTVKESL 920
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPS--EGKIKHSG---------RIS-FSPQTSWIMPG-TIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 921 IYSaflrlpkevTKYEKMRFVdEVMELVELE------SLKDAVVGLPGITGLSTEQRKRLTIAVELVANPSIIFMDEPTS 994
Cdd:TIGR01271 508 IFG---------LSYDEYRYT-SVIKACQLEedialfPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
...
gi 18401096 995 GLD 997
Cdd:TIGR01271 578 HLD 580
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
155-374 |
2.22e-04 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 44.70 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 155 TKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDQSlkVTGRVTYNGHGLEEfvPQKTSAYISQNDvhvG 234
Cdd:COG1116 19 TGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAG-LEKP--TSGEVLVDGKPVTG--PGPDRGVVFQEP---A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 235 VM---TVQETLDFSARCQGVGtrydllselvRREKDAgilpepevdlfmksiaagnvksslITDYTLRILGLdicKDtvV 311
Cdd:COG1116 91 LLpwlTVLDNVALGLELRGVP----------KAERRE------------------------RARELLELVGL---AG--F 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18401096 312 GDEMIRGISGGQKKRV----TtgeMIVGPtKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLM 374
Cdd:COG1116 132 EDAYPHQLSGGMRQRVaiarA---LANDP-EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLF 194
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
955-1010 |
2.99e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 2.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 18401096 955 DAVVGlPGITGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1010
Cdd:PTZ00265 570 ETLVG-SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
915-999 |
3.85e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 915 TVKESLIYSAFL-RLPKEVTKyekmRFVDEVMELVELESLKDAvvgLPGitGLSTEQRKRLTIAVELVANPSIIFMDEPT 993
Cdd:NF033858 355 TVRQNLELHARLfHLPAAEIA----ARVAEMLERFDLADVADA---LPD--SLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
....*...
gi 18401096 994 SGLD--AR 999
Cdd:NF033858 426 SGVDpvAR 433
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
159-212 |
3.87e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 43.28 E-value: 3.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 18401096 159 KVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGklDQSLKVT-GRVTYNGH 212
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKYEVTeGEILFKGE 64
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
320-409 |
3.90e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 320 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRfTDATVLMSlLQPAPETFELFDDIILLSEGQIV 399
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLT-TQYMEEAEQLAHELTVIDRGRVI 223
|
90
....*....|
gi 18401096 400 YQGPRDHVLT 409
Cdd:NF000106 224 ADGKVDELKT 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
841-1050 |
4.06e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 44.94 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 841 LLKEVTGVFRPGVLTALMGVSGAGKTTLmdVLAGRKTGGYIEGDIRISGFpkrqeTFARISgyceQNDIHSpQVTV--KE 918
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGL-----NIAKIG----LHDLRF-KITIipQD 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 919 SLIYSAFLRLPKE-VTKYEKmrfvDEVMELVELESLKDAVVGLP---------GITGLSTEQRKRLTIAVELVANPSIIF 988
Cdd:TIGR00957 1369 PVLFSGSLRMNLDpFSQYSD----EEVWWALELAHLKTFVSALPdkldhecaeGGENLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18401096 989 MDEPTSGLDARAAAIVMRTVRNTVDTGrTVVCTIHQpsIDIFEAFDELLLLKRGGQVIYAGP 1050
Cdd:TIGR00957 1445 LDEATAAVDLETDNLIQSTIRTQFEDC-TVLTIAHR--LNTIMDYTRVIVLDKGEVAEFGAP 1503
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
852-1000 |
4.19e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 43.88 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKRQETFARISGYCEQndihSPQVTVKESLIYS--AF- 925
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGllkPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQ----YPEYQLFEETIEKdiAFg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 926 ---LRLPKEvtkyEKMRFVDEVMELVEL--ESLKDAVvglPgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARA 1000
Cdd:PRK13637 109 pinLGLSEE----EIENRVKRAMNIVGLdyEDYKDKS---P--FELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
850-1019 |
4.31e-04 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II 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. In members of 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: 213182 [Multi-domain] Cd Length: 182 Bit Score: 42.80 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 850 RPGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGFPKRqetfarisgyceqndIHSPqvtvkesliySAFLRLp 929
Cdd:cd03215 24 RAGEIVGIAGLVGNGQTELAEALFGLRP--PASGEITLDGKPVT---------------RRSP----------RDAIRA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 930 kevtkyeKMRFVDE---VMELVELESLKDAVVgLPGItgLS--TEQRkrLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1004
Cdd:cd03215 76 -------GIAYVPEdrkREGLVLDLSVAENIA-LSSL--LSggNQQK--VVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
170
....*....|....*
gi 18401096 1005 MRTVRNTVDTGRTVV 1019
Cdd:cd03215 144 YRLIRELADAGKAVL 158
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
161-350 |
4.43e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSLkVTGRVTYNGHGLEEFVPQKTSAYisqndvhvGV-MTVQ 239
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEV-TGGTVEFKGKDLLELSPEDRAGE--------GIfMAFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 240 etldFSARCQGVGTRYDLLSEL--VRREKDAGILPEPEV-DLFMKSIAAGNVKSSLITdytlRILGLdickdtvvgdemi 316
Cdd:PRK09580 86 ----YPVEIPGVSNQFFLQTALnaVRSYRGQEPLDRFDFqDLMEEKIALLKMPEDLLT----RSVNV------------- 144
|
170 180 190
....*....|....*....|....*....|....
gi 18401096 317 rGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLD 350
Cdd:PRK09580 145 -GFSGGEKKRNDILQMAVLEPELCILDESDSGLD 177
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
141-409 |
5.25e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 43.72 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 141 NIAERGLRLLGFNFTKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLEEFVPQ 220
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLA---SGKISILGQPTRQALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 221 KTSAYISQNdvhvgvmtvqETLDFSarcqgvgtrYDLLSE---LVRREKDAGILPEPEV-DLFMKSIAAGNVKsslITDY 296
Cdd:PRK15056 78 NLVAYVPQS----------EEVDWS---------FPVLVEdvvMMGRYGHMGWLRRAKKrDRQIVTAALARVD---MVEF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 297 TLRILGldickdtvvgdemirGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIvRFTDATVLMSL 376
Cdd:PRK15056 136 RHRQIG---------------ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVST 199
|
250 260 270
....*....|....*....|....*....|...
gi 18401096 377 LQPAPETfeLFDDIILLSEGQIVYQGPRDHVLT 409
Cdd:PRK15056 200 HNLGSVT--EFCDYTVMVKGTVLASGPTETTFT 230
|
|
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
857-884 |
5.48e-04 |
|
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442496 [Multi-domain] Cd Length: 164 Bit Score: 42.04 E-value: 5.48e-04
10 20
....*....|....*....|....*...
gi 18401096 857 LMGVSGAGKTTLMDVLAGRKTGGYIEGD 884
Cdd:COG3265 6 VMGVSGSGKSTVGQALAERLGWPFIDGD 33
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1193-1360 |
5.91e-04 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 43.92 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1193 VIGAMYAAVLFVGVNNSSSVqplIAVERSVFYRERAAEM-YSALPYALAQVVCEIPYVLIQTTYYTLIIYAMMcfeWTLA 1271
Cdd:pfam12698 163 LVGLILMIIILIGAAIIAVS---IVEEKESRIKERLLVSgVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIG---IPFG 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 1272 KFFWFYFVSFMSFLYFTYYGMMTVALTPNQQVAAVFAGAFYGLFNLFSGFVIPRPRIPKWWIWYYWICPVAWTVYGLIVS 1351
Cdd:pfam12698 237 NLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRL 316
|
....*....
gi 18401096 1352 QYGDVEDTI 1360
Cdd:pfam12698 317 IYGDSLWEI 325
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
162-409 |
6.00e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 43.44 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 162 ILRDVSGIIKPSRMTLLLGPPSSGKTT---LLLALAGKLDQSLKVTGrVTYNGHGLEEFvpQKTSAYISQN--DVHVGVm 236
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKPQSGEIKIDG-ITISKENLKEI--RKKIGIIFQNpdNQFIGA- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 237 TVQETLDFSarcqgvgtrydLLSELVRREKdagilpepevdlfMKSIaagnvksslITDYTlrilgldickdTVVGDEMI 316
Cdd:PRK13632 100 TVEDDIAFG-----------LENKKVPPKK-------------MKDI---------IDDLA-----------KKVGMEDY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 317 -----RGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLmSLLQPAPETFeLFDDII 391
Cdd:PRK13632 136 ldkepQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLI-SITHDMDEAI-LADKVI 213
|
250
....*....|....*...
gi 18401096 392 LLSEGQIVYQGPRDHVLT 409
Cdd:PRK13632 214 VFSEGKLIAQGKPKEILN 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
142-409 |
6.01e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 43.36 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 142 IAERGLRLlgfnftKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAG--KLDQSLKVTGRVTYNGHGleefvp 219
Cdd:PRK14247 4 IEIRDLKV------SFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEARVSGEVYLDGQD------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 220 qktsayISQNDVhvgvmtvqetldfsarcqgvgtrydllSELVRREKDAGILPEPEVDL-FMKSIAAGNVKSSLITD--- 295
Cdd:PRK14247 72 ------IFKMDV---------------------------IELRRRVQMVFQIPNPIPNLsIFENVALGLKLNRLVKSkke 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 296 ------YTLRILGL-DICKDTVvgDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRft 368
Cdd:PRK14247 119 lqervrWALEKAQLwDEVKDRL--DAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-- 194
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 18401096 369 DATVLMSLLQPaPETFELFDDIILLSEGQIVYQGPRDHVLT 409
Cdd:PRK14247 195 DMTIVLVTHFP-QQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
176-408 |
6.47e-04 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 43.56 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 176 TLLLGPPSSGKTTLLLALAG--KLDQslkvtGRVTYNGHGLEE-----FVP--QKTSAYISQNDVHVGVMTVQETLDFS- 245
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGltRPDE-----GEIVLNGRTLFDsrkgiFLPpeKRRIGYVFQEARLFPHLSVRGNLRYGm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 246 ARCQGvgtrydllselvrreKDAGILPEPEVDLfmksiaagnvksslitdytlriLGLDICKDTVVGDemirgISGGQKK 325
Cdd:TIGR02142 101 KRARP---------------SERRISFERVIEL----------------------LGIGHLLGRLPGR-----LSGGEKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 326 RVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLM--SLLQpapETFELFDDIILLSEGQIVYQGP 403
Cdd:TIGR02142 139 RVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYvsHSLQ---EVLRLADRVVVLEDGRVAAAGP 215
|
....*
gi 18401096 404 RDHVL 408
Cdd:TIGR02142 216 IAEVW 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
161-247 |
7.01e-04 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 42.35 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 161 TILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDQSLKvtGRVTYNGHGLEE--FVPQKTSAYISQNDVHVGVMTV 238
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAG-LLRPDS--GEVRWNGTPLAEqrDEPHENILYLGHLPGLKPELSA 90
|
....*....
gi 18401096 239 QETLDFSAR 247
Cdd:TIGR01189 91 LENLHFWAA 99
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
1023-1077 |
8.36e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 43.36 E-value: 8.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 18401096 1023 HQPSIDIFEAFDELLLLKRGGQVIYAGPLgqnsHKIIEYFQAIhGVpKIKEKYNP 1077
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTVYHGPV----KKVEEYFAGL-GI-NVPERVNP 49
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
830-1049 |
1.06e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.10 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 830 KEQGVSKDKLQL-LKEVTGVFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFpkrqeTFARISGyCEQND 908
Cdd:PRK10070 31 KEQILEKTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLL--NRLIEPTRGQVLIDGV-----DIAKISD-AELRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 909 IHSPQVtvkeSLIYSAFLRLPkEVTKYEKMRFVDEVMELVELESLKDAV-----VGLPGITG-----LSTEQRKRLTIAV 978
Cdd:PRK10070 103 VRRKKI----AMVFQSFALMP-HMTVLDNTAFGMELAGINAEERREKALdalrqVGLENYAHsypdeLSGGMRQRVGLAR 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18401096 979 ELVANPSIIFMDEPTSGLDAraaaiVMRT------VRNTVDTGRTVVCTIHqpsiDIFEAF--DELLLLKRGGQVIYAG 1049
Cdd:PRK10070 178 ALAINPDILLMDEAFSALDP-----LIRTemqdelVKLQAKHQRTIVFISH----DLDEAMriGDRIAIMQNGEVVQVG 247
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
852-1042 |
1.30e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAGRktggyiegdirisgFPKRQETFARISGYCEqndiHSPQV------TVKESLIY-SA 924
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGE--------------LSHAETSSVVIRGSVA----YVPQVswifnaTVRENILFgSD 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 925 FlrlpkEVTKYEKMRFVDEVMELVELESLKDAV-VGLPGITgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1003
Cdd:PLN03232 705 F-----ESERYWRAIDVTALQHDLDLLPGRDLTeIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180 190
....*....|....*....|....*....|....*....
gi 18401096 1004 VMRTVRNTVDTGRTVVCTIHQpsIDIFEAFDELLLLKRG 1042
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTNQ--LHFLPLMDRIILVSEG 815
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
259-364 |
1.36e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 259 SELVRREKDAGILPEPEVDLFMKSIAAGNVKSSLITDYtlrilgldickDTVVGDEMIRgISGGQKKRVTTGEMIVGPTK 338
Cdd:PTZ00265 532 NELIEMRKNYQTIKDSEVVDVSKKVLIHDFVSALPDKY-----------ETLVGSNASK-LSGGQKQRISIARAIIRNPK 599
|
90 100
....*....|....*....|....*.
gi 18401096 339 TLFMDEISTGLDSSTTYQIVKCLQEI 364
Cdd:PTZ00265 600 ILILDEATSSLDNKSEYLVQKTINNL 625
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
152-402 |
1.46e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 42.53 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 152 FNFTKTTKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLdqslkvtgrvtynghgleefvpqkTSAYisqNDV 231
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLI------------------------KSKY---GTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 232 HVGVMTVQETLDFSARCQGVGTRYdlLSELVRREKDAGILPE-PEVDLFM----KSIAAGNV-------KSSLITDYTLR 299
Cdd:PRK13631 84 QVGDIYIGDKKNNHELITNPYSKK--IKNFKELRRRVSMVFQfPEYQLFKdtieKDIMFGPValgvkksEAKKLAKFYLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 300 ILGLDickDTVVgDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEiVRFTDATVLMsLLQP 379
Cdd:PRK13631 162 KMGLD---DSYL-ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFV-ITHT 235
|
250 260
....*....|....*....|...
gi 18401096 380 APETFELFDDIILLSEGQIVYQG 402
Cdd:PRK13631 236 MEHVLEVADEVIVMDKGKILKTG 258
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
841-997 |
1.53e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 42.15 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 841 LLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpkrqetfaRISgYCEQNDIHSPQvTVKESL 920
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPS--EGKIKHSG---------RIS-FSSQFSWIMPG-TIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 921 IYSaflrlpkevTKYEKMRFvDEVMELVELE------SLKD-AVVGLPGITgLSTEQRKRLTIAVELVANPSIIFMDEPT 993
Cdd:cd03291 119 IFG---------VSYDEYRY-KSVVKACQLEeditkfPEKDnTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPF 187
|
....
gi 18401096 994 SGLD 997
Cdd:cd03291 188 GYLD 191
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
842-1049 |
1.69e-03 |
|
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: 41.47 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTL-MDVL--AGRKTggYIEG-----DIRISGFPKRQETfaRISGYC-----EQND 908
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLaFDTIyaEGQRR--YVESlsayaRQFLGQMDKPDVD--SIEGLSpaiaiDQKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 909 I-HSPQVTVKE-SLIYSaFLRLpkevtKYEKMRFVDevmelvELESLKDavVGLPGITgLSTE---------QRKRLT-- 975
Cdd:cd03270 87 TsRNPRSTVGTvTEIYD-YLRL-----LFARVGIRE------RLGFLVD--VGLGYLT-LSRSaptlsggeaQRIRLAtq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 976 IAVELVanpSIIF-MDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPsiDIFEAFDELLLL-----KRGGQVIYAG 1049
Cdd:cd03270 152 IGSGLT---GVLYvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDE--DTIRAADHVIDIgpgagVHGGEIVAQG 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
319-402 |
2.01e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 41.92 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 319 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLMsLLQPAPETFELFDDIILLSEGQI 398
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIM-VTHNMDQVLRIADEVIVMHEGKV 229
|
....
gi 18401096 399 VYQG 402
Cdd:PRK13645 230 ISIG 233
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
852-1050 |
2.14e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 42.63 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 852 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKRQETFARIsgyceQNDihspqvTVKESLIYSAFLRLPke 931
Cdd:TIGR00957 664 GALVAVVGQVGCGKSSLLSALLAEMDK--VEGHVHMKGSVAYVPQQAWI-----QND------SLRENILFGKALNEK-- 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 932 vtkyekmrFVDEVME----LVELESLKDA---VVGLPGITgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1004
Cdd:TIGR00957 729 --------YYQQVLEacalLPDLEILPSGdrtEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 18401096 1005 MRTVRNT--VDTGRTVVCTIHqpSIDIFEAFDELLLLKrGGQVIYAGP 1050
Cdd:TIGR00957 800 FEHVIGPegVLKNKTRILVTH--GISYLPQVDVIIVMS-GGKISEMGS 844
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
319-409 |
2.54e-03 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.11 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 319 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLM---SL---LQPAPETfelfddiIL 392
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMvshSLedaARIAPRS-------LV 202
|
90
....*....|....*..
gi 18401096 393 LSEGQIVYQGPRDHVLT 409
Cdd:PRK10771 203 VADGRIAWDGPTDELLS 219
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
974-1027 |
2.61e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 2.61e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 18401096 974 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1027
Cdd:pfam13304 248 LAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
378-421 |
2.66e-03 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 41.82 E-value: 2.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 18401096 378 QPAPETFELFDDIILLSEG-QIVYQGPRDHVLTFFETCGFKCPDR 421
Cdd:pfam19055 2 QPSYTLFKMFDDLILLAKGgLTVYHGPVKKVEEYFAGLGINVPER 46
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
828-997 |
2.68e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 40.85 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 828 EMKEQGVSKDKLQLLKEVTGVFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--EGDiRISGFPKrqETFARISGY 903
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASliSPTSGTLlfEGE-DISTLKP--EIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 904 CEQndihSPQV---TVKESLIYSAFLRLPKEvtkyEKMRFVDEVMELveleslkdavvGLP------GITGLSTEQRKRL 974
Cdd:PRK10247 86 CAQ----TPTLfgdTVYDNLIFPWQIRNQQP----DPAIFLDDLERF-----------ALPdtiltkNIAELSGGEKQRI 146
|
170 180
....*....|....*....|...
gi 18401096 975 TIAVELVANPSIIFMDEPTSGLD 997
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALD 169
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
172-200 |
2.96e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.66 E-value: 2.96e-03
10 20
....*....|....*....|....*....
gi 18401096 172 PSRMTLLLGPPSSGKTTLLLALAGKLDQS 200
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP 29
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
175-261 |
3.62e-03 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 40.17 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 175 MTLLLGPPSSGKTTLLLALAGkldQSLKVTGRVTYNGHGLEEFVP--QKTSAYISQNDVHVGVMTVQETLDFSARCQGVG 252
Cdd:cd03231 28 ALQVTGPNGSGKTTLLRILAG---LSPPLAGRVLLNGGPLDFQRDsiARGLLYLGHAPGIKTTLSVLENLRFWHADHSDE 104
|
....*....
gi 18401096 253 TRYDLLSEL 261
Cdd:cd03231 105 QVEEALARV 113
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
838-1009 |
3.67e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.76 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 838 KLQLLKEVTGVFRPGVLTALMGVSGAGKT----TLMDVLagRKTGGYIEGD-----------IRISGFPKRQetFARISG 902
Cdd:PRK10261 28 KIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLL--EQAGGLVQCDkmllrrrsrqvIELSEQSAAQ--MRHVRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 903 ------YCEQNDIHSPQVTVKESLIYSafLRLPKEVTKYEKMRFVDEVMELVELESLKDAVVGLPgiTGLSTEQRKRLTI 976
Cdd:PRK10261 104 admamiFQEPMTSLNPVFTVGEQIAES--IRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYP--HQLSGGMRQRVMI 179
|
170 180 190
....*....|....*....|....*....|...
gi 18401096 977 AVELVANPSIIFMDEPTSGLDARAAAIVMRTVR 1009
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDVTIQAQILQLIK 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
319-413 |
3.69e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 41.19 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 319 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVLM---SLLQPApetfELFDDIILLSE 395
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILvshSMEDVA----KLADRIIVMNK 220
|
90
....*....|....*...
gi 18401096 396 GQIVYQGPRDHVLTFFET 413
Cdd:PRK13637 221 GKCELQGTPREVFKEVET 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
844-1010 |
3.73e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 844 EVTGVFRPgvltalmgvSGAGKTTLMDVLAGR--KTGGYIEGDIRISGFPKRQETfarisgyceqndihSPQVTVkesli 921
Cdd:PRK13409 366 EVIGIVGP---------NGIGKTTFAKLLAGVlkPDEGEVDPELKISYKPQYIKP--------------DYDGTV----- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 922 ySAFLRlpKEVTKYEKMRFVDEVMELVELESLKDAVVglpgiTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1001
Cdd:PRK13409 418 -EDLLR--SITDDLGSSYYKSEIIKPLQLERLLDKNV-----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
....*....
gi 18401096 1002 AIVMRTVRN 1010
Cdd:PRK13409 490 LAVAKAIRR 498
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
128-409 |
4.06e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 41.62 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 128 GKRALPTLPNA-ALNIAErglrllgFNFTKTTKvTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGR 206
Cdd:PRK10789 303 GSEPVPEGRGElDVNIRQ-------FTYPQTDH-PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS---EGD 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 207 VTYNGHGLEEFvpqktsayisQNDvhvgvmtvqetlDFSARCQGVGTRYDLLSELVRREKDAGiLPEPEVDLFMKSIAAG 286
Cdd:PRK10789 372 IRFHDIPLTKL----------QLD------------SWRSRLAVVSQTPFLFSDTVANNIALG-RPDATQQEIEHVARLA 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 287 NVKSSlitdytlrILGLDICKDTVVGDemiRGI--SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEI 364
Cdd:PRK10789 429 SVHDD--------ILRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW 497
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 18401096 365 VRftDATVL-----MSLLQPApetfelfDDIILLSEGQIVYQGPRDHVLT 409
Cdd:PRK10789 498 GE--GRTVIisahrLSALTEA-------SEILVMQHGHIAQRGNHDQLAQ 538
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
842-1050 |
4.63e-03 |
|
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: 40.68 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 842 LKEVTGVFRPGVLTALMGVSGAGKTTLMD-----VLAGRKTGGyiegdiriSGFPKRqetFARISGYCEQNDIhspqVTV 916
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypALARRLHLK--------KEQPGN---HDRIEGLEHIDKV----IVI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 917 KESLI----------YSAFLRLPKEV-------TKYE--------KMRFVDEVMEL-VE---------------LESLKD 955
Cdd:cd03271 76 DQSPIgrtprsnpatYTGVFDEIRELfcevckgKRYNretlevryKGKSIADVLDMtVEealeffenipkiarkLQTLCD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 956 avVGLPGI------TGLSTEQRKRLTIAVELvANPS----IIFMDEPTSGL---DARAAAIVMRTVrntVDTGRTVVCTI 1022
Cdd:cd03271 156 --VGLGYIklgqpaTTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLhfhDVKKLLEVLQRL---VDKGNTVVVIE 229
|
250 260 270
....*....|....*....|....*....|...
gi 18401096 1023 HQpsIDIFEAFDELLLL-----KRGGQVIYAGP 1050
Cdd:cd03271 230 HN--LDVIKCADWIIDLgpeggDGGGQVVASGT 260
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
172-201 |
4.71e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 40.25 E-value: 4.71e-03
10 20 30
....*....|....*....|....*....|
gi 18401096 172 PSRMTLLLGPPSSGKTTLLLALAGKLDQSL 201
Cdd:COG1223 34 PPRKILFYGPPGTGKTMLAEALAGELKLPL 63
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
158-399 |
6.72e-03 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 39.65 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 158 TKVTILRDVSGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDQSlkvTGRVTYNGHGLeefvpqktsAYISQNDV-----H 232
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPT---SGQVLVNGQDL---------SRLKRREIpylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 233 VGV----------MTVQETLDFSARCQGVGTRydllsELVRREKDAgilpepevdlfmksiaagnvksslitdytLRILG 302
Cdd:COG2884 81 IGVvfqdfrllpdRTVYENVALPLRVTGKSRK-----EIRRRVREV-----------------------------LDLVG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 303 LDickdtVVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEiSTG-LDSSTTYQIVKCLQEIVRfTDATVLMSllqpap 381
Cdd:COG2884 127 LS-----DKAKALPHELSGGEQQRVAIARALVNRPELLLADE-PTGnLDPETSWEIMELLEEINR-RGTTVLIA------ 193
|
250 260
....*....|....*....|....
gi 18401096 382 eT--FELFDD----IILLSEGQIV 399
Cdd:COG2884 194 -ThdLELVDRmpkrVLELEDGRLV 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
850-1012 |
8.50e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 40.44 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 850 RPGVLTALMGVSGAGKTTLmdvlaGR------KTGGYIE-GDIRISGFPKR-------------QETFARISgyceqndi 909
Cdd:COG4172 310 RRGETLGLVGESGSGKSTL-----GLallrliPSEGEIRfDGQDLDGLSRRalrplrrrmqvvfQDPFGSLS-------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 910 hsPQVTVKEslIYSAFLRL-PKEVTKYEKMRFVDEVMElvelEslkdavVGLPGITG------LSTEQRKRLTIAVELVA 982
Cdd:COG4172 377 --PRMTVGQ--IIAEGLRVhGPGLSAAERRARVAEALE----E------VGLDPAARhrypheFSGGQRQRIAIARALIL 442
|
170 180 190
....*....|....*....|....*....|
gi 18401096 983 NPSIIFMDEPTSGLDaraaaivmRTVRNTV 1012
Cdd:COG4172 443 EPKLLVLDEPTSALD--------VSVQAQI 464
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
319-440 |
9.24e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.17 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401096 319 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQEIVRFTDATVL-----MSLLQpapetfELFDDIILL 393
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVlitheMDVVK------RICDRVAVI 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 18401096 394 SEGQIVYQGPRDHVltffetcgFKCPDRKGTADFLQEVTSRKDQEQY 440
Cdd:PRK11153 215 DAGRLVEQGTVSEV--------FSHPKHPLTREFIQSTLHLDLPEDY 253
|
|
| |
