|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
74-634 |
9.98e-166 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 512.40 E-value: 9.98e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 74 LIIIGCLGALINGGSQPWYSYLFGNFVNKIALDNDKDQMIKdvreLCVLMSALSGIVVIGAYLQIACWRLVGERLGHRIR 153
Cdd:COG1132 22 LLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLL----LLLLLLGLALLRALLSYLQRYLLARLAQRVVADLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 154 SKYLRAVLRQDVSFFDtDISTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMF 233
Cdd:COG1132 98 RDLFEHLLRLPLSFFD-RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 234 CGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTY 313
Cdd:COG1132 177 VLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 314 STWALAFWYGSILVSRNELSGGAAIACFFGVTIGGRGLALSLSYFAQFAQGTVAASKVFAIIDRIPAIdPYSTTGRKPET 393
Cdd:COG1132 257 LGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEI-PDPPGAVPLPP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 394 VHGRLELKNVSFAYPSrmSVPILNSLNLVIPS-QRIsALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWL 472
Cdd:COG1132 336 VRGEIEFENVSFSYPG--DRPVLKDISLTIPPgETV-ALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 473 RSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMI 552
Cdd:COG1132 413 RRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALL 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 553 KDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSLI 632
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLY 572
|
..
gi 1770234124 633 KL 634
Cdd:COG1132 573 RL 574
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
74-1269 |
2.43e-150 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 497.63 E-value: 2.43e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 74 LIIIGCLGALINGGSQPWYSYLFGNFVNKIALDNDKDQMIKDVRELCVLMSALSgivVIGAYlqiaCWRLVGERLGHRIR 153
Cdd:PTZ00265 61 LLGVSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILS---FISSF----CMDVVTTKILKTLK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 154 SKYLRAVLRQDVSFFDTDiSTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMF 233
Cdd:PTZ00265 134 LEFLKSVFYQDGQFHDNN-PGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 234 CGVaykavyvgLAAKEVNSYKKAG--------SIAEQAIGSIRTVFSFVAEDSLAARYDavLDESV--PIGKKLGFAKGI 303
Cdd:PTZ00265 213 CGV--------ICNKKVKINKKTSllynnntmSIIEEALVGIRTVVSYCGEKTILKKFN--LSEKLysKYILKANFMESL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 304 GLGVIYLVTYSTWALAFWYGSILV--------SRNELSGGAAIACFFGVTIGGRGLALSLSYFAQFAQGTVAASKVFAII 375
Cdd:PTZ00265 283 HIGMINGFILASYAFGFWYGTRIIisdlsnqqPNNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEII 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 376 DRIPAIDPySTTGRKPETVHgRLELKNVSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKG 455
Cdd:PTZ00265 363 NRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 456 -LILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENIL--------------------------------------- 495
Cdd:PTZ00265 441 dIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKyslyslkdlealsnyynedgndsqenknkrnscrakcag 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 496 ----------------MGKENATKK--EAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKI 557
Cdd:PTZ00265 521 dlndmsnttdsnelieMRKNYQTIKdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKI 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 558 LLLDEPTSALDPKSESLVQQAID--KISKGRTTIVIAHRLATVKNAETIIVL---EQGS--------------------- 611
Cdd:PTZ00265 601 LILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLsnrERGStvdvdiigedptkdnkennnk 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 612 -----------------------VIEIGDHNKLMA-QEGAYFSLI---KLATEAISSNPVSK----KGKTVINQETSSNC 660
Cdd:PTZ00265 681 nnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKnKNGIYYTMInnqKVSSKKSSNNDNDKdsdmKSSAYKDSERGYDP 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 661 DLLKQNHVYEISPSGYMKS--IQDANQPESAKLNKIKSYK----------------IREVWKLQKPeagllcVGVIFG-- 720
Cdd:PTZ00265 761 DEMNGNSKHENESASNKKSckMSDENASENNAGGKLPFLRnlfkrkpkapnnlrivYREIFSYKKD------VTIIALsi 834
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 721 MLAGAILSLFPLVLGQALTVYFnpDKSKLQKDVGYLCLALVGLGFGCILTMMGQQGFCGWAGTKLTKRVRDLLFRSILNQ 800
Cdd:PTZ00265 835 LVAGGLYPVFALLYAKYVSTLF--DFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQ 912
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 801 EPGWFDSDQNSPGSLVSKLSVNCTSFRS------ILGDRYSVLFMglssaaVGLSVSFYLewrLALLATIVTpftlgASY 874
Cdd:PTZ00265 913 EISFFDQDKHAPGLLSAHINRDVHLLKTglvnniVIFTHFIVLFL------VSMVMSFYF---CPIVAAVLT-----GTY 978
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 875 FSLI-------------------INIGSKL-----DNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSS 930
Cdd:PTZ00265 979 FIFMrvfairarltankdvekkeINQPGTVfaynsDDEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKG 1058
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 931 SIKRSQITGIALGISQGAMYSAYTLVLFFGAYLVKKDYTKFGDVYKIFLILVLSTFSVGQFAGLAPDTSMASTAIPAVFE 1010
Cdd:PTZ00265 1059 QKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYP 1138
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1011 IMNRNPLIDGK---GKKIEQSKPFD--LEFKMVNFAYPSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFY 1085
Cdd:PTZ00265 1139 LIIRKSNIDVRdngGIRIKNKNDIKgkIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFY 1218
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1086 D-----------------------------PIG-------------------------GKVMMGGRDLRDLDLKWLRLQT 1111
Cdd:PTZ00265 1219 DlkndhhivfknehtndmtneqdyqgdeeqNVGmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLF 1298
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSK 1191
Cdd:PTZ00265 1299 SIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1192 VLLLDEATSALDLESEKHVQDAIRKIIKRT--TTIVVVHRLSTIKKANAIAVVQNGK-----VSEYGTHDTLLTNHsNGV 1264
Cdd:PTZ00265 1379 ILLLDEATSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQ-DGV 1457
|
....*
gi 1770234124 1265 YATLV 1269
Cdd:PTZ00265 1458 YKKYV 1462
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
699-1275 |
1.10e-148 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 466.95 E-value: 1.10e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 699 IREVWKLQKPEAGLLCVGVIFGMLAGAILSLFPLVLGQALTVYFNPDKSKLqkdVGYLCLALVGLGFGCILTMMGQQGFC 778
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA---LLLLLLLLLGLALLRALLSYLQRYLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 779 GWAGTKLTKRVRDLLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRL 858
Cdd:COG1132 86 ARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 859 ALLATIVTPFTLGAS-YFSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQI 937
Cdd:COG1132 164 ALIVLLVLPLLLLVLrLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 938 TGIALGISQGAMYSAYTLVLFFGAYLVKKDYTKFGDVYKIFLILVLSTFSVGQFAGLAPDTSMASTAIPAVFEIMNRNPL 1017
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1018 I-DGKGKKIEQSKPFDLEFKMVNFAYPsrPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGG 1096
Cdd:COG1132 324 IpDPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1097 RDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQ 1176
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1177 KQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTL 1256
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
570
....*....|....*....
gi 1770234124 1257 LTNhsNGVYATLVHSEMEA 1275
Cdd:COG1132 562 LAR--GGLYARLYRLQFGE 578
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
72-632 |
9.33e-129 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 417.59 E-value: 9.33e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 72 LFLIIIGCLGALinggSQPWYSylfGNFVNKIALDNDKDQMIKDVRELCVL--MSALSGIVVIGaylqiaCWRLVGERLG 149
Cdd:TIGR00958 167 FVFLTLSSLGEM----FIPFYT---GRVIDTLGGDKGPPALASAIFFMCLLsiASSVSAGLRGG------SFNYTMARIN 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 150 HRIRSKYLRAVLRQDVSFFDTDiSTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTP 229
Cdd:TIGR00958 234 LRIREDLFRSLLRQDLGFFDEN-KTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLP 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 230 LTMFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKgiglgVIY 309
Cdd:TIGR00958 313 LVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAY-----AGY 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 310 LVTYSTWALA-----FWYGSILVSRNELSGGAAIACFFGVTIGGRGLALSLSYFAQFAQGTVAASKVFAIIDRIPAIDPy 384
Cdd:TIGR00958 388 LWTTSVLGMLiqvlvLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPL- 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 385 sTTGRKPETVHGRLELKNVSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDI 464
Cdd:TIGR00958 467 -TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 465 RTLQVKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQR 544
Cdd:TIGR00958 546 VQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 545 IALARAMIKDPKILLLDEPTSALDPKSESLVQQaiDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQ 624
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMED 703
|
....*...
gi 1770234124 625 EGAYFSLI 632
Cdd:TIGR00958 704 QGCYKHLV 711
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
399-635 |
1.30e-128 |
|
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: 399.22 E-value: 1.30e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 399 ELKNVSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGM 478
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 479 VGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKIL 558
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 559 LLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSLIKLA 635
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
72-633 |
7.73e-126 |
|
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: 409.61 E-value: 7.73e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 72 LFLIIIGCLGALINggsqpwySYLFGNFVNKIALDNDKDQMIkdvrelcVLMSALSGIVVIGAYLQIACWRLV---GERL 148
Cdd:COG2274 162 LLASLLINLLALAT-------PLFTQVVIDRVLPNQDLSTLW-------VLAIGLLLALLFEGLLRLLRSYLLlrlGQRI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 149 GHRIRSKYLRAVLRQDVSFFDTDiSTSDIMHGISsDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVT 228
Cdd:COG2274 228 DLRLSSRFFRHLLRLPLSFFESR-SVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 229 PLTMFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVI 308
Cdd:COG2274 306 PLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLS 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 309 YLVTYSTWALAFWYGSILVSRNELSGGAAIACffgVTIGGRGLA--LSL-SYFAQFAQGTVAASKVFAIIDRIPAIDPYS 385
Cdd:COG2274 386 GLLQQLATVALLWLGAYLVIDGQLTLGQLIAF---NILSGRFLApvAQLiGLLQRFQDAKIALERLDDILDLPPEREEGR 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 386 TTGRKPEtVHGRLELKNVSFAYPSRmSVPILNSLNLVIPS-QRIsALVGASGAGKSTIFALLERFYDPNKGLILLDGQDI 464
Cdd:COG2274 463 SKLSLPR-LKGDIELENVSFRYPGD-SPPVLDNISLTIKPgERV-AIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 465 RTLQVKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQR 544
Cdd:COG2274 540 RQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 545 IALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQ 624
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
....*....
gi 1770234124 625 EGAYFSLIK 633
Cdd:COG2274 700 KGLYAELVQ 708
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
121-634 |
1.66e-121 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 393.30 E-value: 1.66e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 121 VLMSALSGIVVIGAYLQIACWRLVGERLGHRIRSKYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGDKMSQFI 200
Cdd:TIGR02204 62 AFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDK-NRSGEVVSRLTTDTTLLQSVIGSSLSMAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 201 YHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLA 280
Cdd:TIGR02204 141 RNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAER 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 281 ARYDAVLDESVPIGKKLGFAKGI-GLGVIYLVtYSTWALAFWYGSILVSRNELSGG--AAIAcFFGVTIGGRGLALSlSY 357
Cdd:TIGR02204 221 SRFGGAVEKAYEAARQRIRTRALlTAIVIVLV-FGAIVGVLWVGAHDVIAGKMSAGtlGQFV-FYAVMVAGSIGTLS-EV 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 358 FAQFAQGTVAASKVFAIIDRIPAIDPYSTTGRKPETVHGRLELKNVSFAYPSRMSVPILNSLNLVI-PSQRIsALVGASG 436
Cdd:TIGR02204 298 WGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVrPGETV-ALVGPSG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 437 AGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAH 516
Cdd:TIGR02204 377 AGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAH 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 517 NFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLA 596
Cdd:TIGR02204 457 EFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLA 536
|
490 500 510
....*....|....*....|....*....|....*...
gi 1770234124 597 TVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSLIKL 634
Cdd:TIGR02204 537 TVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARL 574
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1034-1270 |
2.54e-118 |
|
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: 371.10 E-value: 2.54e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1034 EFKMVNFAYPSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTAL 1113
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1114 VGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVL 1193
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1194 LLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTNHsnGVYATLVH 1270
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK--GVYAKLVK 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
693-1273 |
1.50e-110 |
|
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: 367.24 E-value: 1.50e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 693 KIKSYKIREVWKLQKPEAGLLcVGVIFGMLAGAILSL-FPLVLgQAL--TVYFNPDKSKLqkdVGYLCLALVGLGFGCIL 769
Cdd:COG2274 138 GEKPFGLRWFLRLLRRYRRLL-LQVLLASLLINLLALaTPLFT-QVVidRVLPNQDLSTL---WVLAIGLLLALLFEGLL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 770 TMMgQQGFCGWAGTKLTKRVRDLLFRSILNQEPGWFDsdQNSPGSLVSKLSVNcTSFRSILGDRYSVLFMGLSSAAVGLS 849
Cdd:COG2274 213 RLL-RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRFRDV-ESIREFLTGSLLTALLDLLFVLIFLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 850 VSFYLEWRLALLATIVTPFTLGASYFSLiiNIGSKLDNDSFDKASGIASA---AVSNIRTVTTLATQEKIVQSFEQSLSK 926
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLLFQ--PRLRRLSREESEASAKRQSLlveTLRGIETIKALGAESRFRRRWENLLAK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 927 PKSSSIKRSQITGIALGISQGAMYSAYTLVLFFGAYLVKKDYTKFGDVykI-FLILVLSTFS-VGQFAGLAPDTSMASTA 1004
Cdd:COG2274 367 YLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQL--IaFNILSGRFLApVAQLIGLLQRFQDAKIA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1005 IPAVFEIMNRNPLIDGKGKKIEQSKPF-DLEFKMVNFAYPSRpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQR 1083
Cdd:COG2274 445 LERLDDILDLPPEREEGRSKLSLPRLKgDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1084 FYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYET 1163
Cdd:COG2274 524 LYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDT 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1164 EVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQ 1243
Cdd:COG2274 604 VVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLD 683
|
570 580 590
....*....|....*....|....*....|
gi 1770234124 1244 NGKVSEYGTHDTLLTNhsNGVYATLVHSEM 1273
Cdd:COG2274 684 KGRIVEDGTHEELLAR--KGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
699-1269 |
3.09e-110 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 362.10 E-value: 3.09e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 699 IREVWKLQKPEAGLLcVGVIFGMLAGAILSLfplVLGQALTVY----FNPDKSKL--QKDVGYLCLALV-GLGFGCILTM 771
Cdd:TIGR02204 6 LAALWPFVRPYRGRV-LAALVALLITAAATL---SLPYAVRLMidhgFSKDSSGLlnRYFAFLLVVALVlALGTAARFYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 772 MGqqgfcgWAGTKLTKRVRDLLFRSILNQEPGWFDSdqNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVS 851
Cdd:TIGR02204 82 VT------WLGERVVADIRRAVFAHLISLSPSFFDK--NRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 852 FYLEWRLALLATIVTPFTLGA-SYFSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSS 930
Cdd:TIGR02204 154 FITSPKLTSLVLLAVPLVLLPiLLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 931 SIKRSQITGIALGISQGAMYSAYTLVLFFGAYLVKKDYTKFGDVYKIFLILVLSTFSVGQFAGLAPDTSMASTAIPAVFE 1010
Cdd:TIGR02204 234 ARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1011 IMNRNPLIDGKG--KKIEQSKPFDLEFKMVNFAYPSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPI 1088
Cdd:TIGR02204 314 LLQAEPDIKAPAhpKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1089 GGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGES 1168
Cdd:TIGR02204 394 SGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGER 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1169 GIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVS 1248
Cdd:TIGR02204 474 GVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIV 553
|
570 580
....*....|....*....|.
gi 1770234124 1249 EYGTHDTLLTnhSNGVYATLV 1269
Cdd:TIGR02204 554 AQGTHAELIA--KGGLYARLA 572
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
74-631 |
5.02e-106 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 350.17 E-value: 5.02e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 74 LIIIGCLGALINGGSQPWYSYLFGNFVNkialdndkDQMIKDVRELCVLMS-ALSGIVV---IGAYLQIACWRLVGERLG 149
Cdd:TIGR02203 15 GLVLAGVAMILVAATESTLAALLKPLLD--------DGFGGRDRSVLWWVPlVVIGLAVlrgICSFVSTYLLSWVSNKVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 150 HRIRSKYLRAVLRQDVSFFDTDISTSDIMHgISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTP 229
Cdd:TIGR02203 87 RDIRVRMFEKLLGLPVSFFDRQPTGTLLSR-ITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 230 LTMFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIY 309
Cdd:TIGR02203 166 VLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 310 LVTYSTWALAFWYGSILVSRNELSGGAAIACFFGVTIGGRGLALSLSYFAQFAQGTVAASKVFAIIDRIPAIDpysTTGR 389
Cdd:TIGR02203 246 LIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKD---TGTR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 390 KPETVHGRLELKNVSFAYPSRmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQV 469
Cdd:TIGR02203 323 AIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 470 KWLRSQMGMVGQEPVLFADTILENILMGK-ENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALA 548
Cdd:TIGR02203 402 ASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIA 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 549 RAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAY 628
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
...
gi 1770234124 629 FSL 631
Cdd:TIGR02203 562 AQL 564
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
699-1269 |
3.29e-104 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 349.79 E-value: 3.29e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 699 IREVWKLQKPEAGLLCVGVIFGMLAGAILSLFPLVLGQALTVYFNpDKS--KLQKDVGYLCL------ALVGLGFGCILT 770
Cdd:TIGR00958 149 LFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGG-DKGppALASAIFFMCLlsiassVSAGLRGGSFNY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 771 MMGqqgfcgwagtKLTKRVRDLLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSV 850
Cdd:TIGR00958 228 TMA----------RINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGF 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 851 SFYLEWRLALLATIVTPFTLGAS-YFSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKS 929
Cdd:TIGR00958 296 MLWLSPRLTMVTLINLPLVFLAEkVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQ 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 930 SSIKRSqITGIALGISQGAMYSA-YTLVLFFGAYLVKKDYTKFGDVykifLILVLSTFSVGQ----FAGLAPDTSMASTA 1004
Cdd:TIGR00958 376 LNKRKA-LAYAGYLWTTSVLGMLiQVLVLYYGGQLVLTGKVSSGNL----VSFLLYQEQLGEavrvLSYVYSGMMQAVGA 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1005 IPAVFEIMNRNPLIDGKGkkiEQSKPFD---LEFKMVNFAYPSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLM 1081
Cdd:TIGR00958 451 SEKVFEYLDRKPNIPLTG---TLAPLNLeglIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1082 QRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGY 1161
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGY 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1162 ETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAirKIIKRTTTIVVVHRLSTIKKANAIAV 1241
Cdd:TIGR00958 608 DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILV 685
|
570 580
....*....|....*....|....*...
gi 1770234124 1242 VQNGKVSEYGTHDTLLTNhsNGVYATLV 1269
Cdd:TIGR00958 686 LKKGSVVEMGTHKQLMED--QGCYKHLV 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
398-631 |
3.05e-103 |
|
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: 329.19 E-value: 3.05e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:cd03251 1 VEFKNVTFRYPGD-GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKI 557
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 558 LLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSL 631
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
362-626 |
1.90e-98 |
|
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: 328.64 E-value: 1.90e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 362 AQGTVAASKVFAIIDRiPAIDPYSTTGRKPETVHGRLELKNVSFAYPSRmsVPILNSLNLVIPSQRISALVGASGAGKST 441
Cdd:COG4988 302 ANGIAAAEKIFALLDA-PEPAAPAGTAPLPAAGPPSIELEDVSFSYPGG--RPALDGLSLTIPPGERVALVGPSGAGKST 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 442 IFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICD 521
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 522 LPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNA 601
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538
|
250 260
....*....|....*....|....*
gi 1770234124 602 ETIIVLEQGSVIEIGDHNKLMAQEG 626
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
363-631 |
2.91e-97 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 326.39 E-value: 2.91e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 363 QGTVAASKVFAIIDRIPAI-DPystTGRKPETV-HGRLELKNVSFAY-PSRmsvPILNSLNLVIPSQRISALVGASGAGK 439
Cdd:COG5265 324 QALADMERMFDLLDQPPEVaDA---PDAPPLVVgGGEVRFENVSFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 440 STIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFI 519
Cdd:COG5265 398 STLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFI 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 520 CDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVK 599
Cdd:COG5265 478 ESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIV 557
|
250 260 270
....*....|....*....|....*....|..
gi 1770234124 600 NAETIIVLEQGSVIEIGDHNKLMAQEGAYFSL 631
Cdd:COG5265 558 DADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
75-371 |
4.43e-97 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 314.80 E-value: 4.43e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 75 IIIGCLGALINGGSQPWYSYLFGNFVNKIA----LDNDKDQMIKDVRELCVLMSALSGIVVIGAYLQIACWRLVGERLGH 150
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 151 RIRSKYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPL 230
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK-NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 231 TMFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYL 310
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 311 VTYSTWALAFWYGSILVSRNELSGGAAIACFFGVTIGGRGLALSLSYFAQFAQGTVAASKV 371
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
398-631 |
4.81e-97 |
|
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: 311.86 E-value: 4.81e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAY-PSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQM 476
Cdd:cd03253 1 IEFENVTFAYdPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPK 556
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 557 ILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSL 631
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
396-626 |
8.56e-96 |
|
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: 308.00 E-value: 8.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 396 GRLELKNVSFAYPSRmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQ 475
Cdd:cd03254 1 GEIEFENVNFSYDEK--KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDP 555
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 556 KILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEG 626
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
700-1268 |
3.95e-94 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 316.66 E-value: 3.95e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 700 REVWKLQKPEAGLLCVGVIFGMLAGAILSLFPLVLGQALTVYFN-PDKSKLQkdvgYLCLALVGL----GFGCILTMMgq 774
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGgRDRSVLW----WVPLVVIGLavlrGICSFVSTY-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 775 qgFCGWAGTKLTKRVRDLLFRSILnQEPGWFdSDQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYL 854
Cdd:TIGR02203 77 --LLSWVSNKVVRDIRVRMFEKLL-GLPVSF-FDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 855 EWRLALLATIVTPFTLG-ASYFS-LIINIGSKLDNdSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSI 932
Cdd:TIGR02203 153 SWQLTLIVVVMLPVLSIlMRRVSkRLRRISKEIQN-SMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 933 KRSQITGIALGISQGAMYSAYTLVLFFGAYLVKKDYTKFGDVYKIFLILVLSTFSVGQFAGLAPDTSMASTAIPAVFEIM 1012
Cdd:TIGR02203 232 KMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1013 NRNPLIDGKGKKIEQSKPfDLEFKMVNFAYPSRpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKV 1092
Cdd:TIGR02203 312 DSPPEKDTGTRAIERARG-DVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1093 MMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNP-NASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQ 1171
Cdd:TIGR02203 390 LLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1172 LSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYG 1251
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
|
570
....*....|....*..
gi 1770234124 1252 THDTLLTnhSNGVYATL 1268
Cdd:TIGR02203 550 THNELLA--RNGLYAQL 564
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
703-1018 |
1.31e-93 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 305.53 E-value: 1.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 703 WKLQKPEAGLLCVGVIFGMLAGAILSLFPLVLGQALTVYFNPDKSKLQKDVGYLCLALVGLGFGCILTMMGQQGFCGWAG 782
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 783 TKLTKRVRDLLFRSILNQEPGWFDSDQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLA 862
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 863 TIVTPFTLGASYFSLIINIG-SKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIA 941
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGfEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 942 LGISQGAMYSAYTLVLFFGAYLVKKDYTKFGDVYKIFLILVLSTFSVGQFAGLAPDTSMASTAIPAVFEIMNRNPLI 1018
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1033-1268 |
5.52e-93 |
|
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: 300.30 E-value: 5.52e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPDViVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKV 1192
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1193 LLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTnhSNGVYATL 1268
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA--QGGVYAKL 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
145-634 |
1.11e-92 |
|
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: 312.47 E-value: 1.11e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 145 GERL-GH--------RIRSKYLRAVLRQDVSFFdTDISTSDIMHGISSDVAQIQEVMgdkmSQFIYHIFTFICGYI--VG 213
Cdd:COG4987 74 LERLvSHdatlrllaDLRVRLYRRLEPLAPAGL-ARLRSGDLLNRLVADVDALDNLY----LRVLLPLLVALLVILaaVA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 214 FLKSWKVSLAVLAVTPLTMFCGVAykAVYVGLAAKevnsykKAGSIAEQAIGSIRTVFS-----------FVAEDSLAAR 282
Cdd:COG4987 149 FLAFFSPALALVLALGLLLAGLLL--PLLAARLGR------RAGRRLAAARAALRARLTdllqgaaelaaYGALDRALAR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 283 YDAVLDESVPIGKKLGFAKGIGLGVIYLVTYSTWALAFWYGSILVSRNELSGGAAIACFFGV-----TIGGRGLAlslsy 357
Cdd:COG4987 221 LDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAAlalfeALAPLPAA----- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 358 FAQFAQGTVAASKVFAIIDRIPAI-DPYSTTgrkPETVHGRLELKNVSFAYPSRmSVPILNSLNLVI-PSQRIsALVGAS 435
Cdd:COG4987 296 AQHLGRVRAAARRLNELLDAPPAVtEPAEPA---PAPGGPSLELEDVSFRYPGA-GRPVLDGLSLTLpPGERV-AIVGPS 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 436 GAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNA 515
Cdd:COG4987 371 GSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 516 HNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRL 595
Cdd:COG4987 451 GDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRL 530
|
490 500 510
....*....|....*....|....*....|....*....
gi 1770234124 596 ATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSLIKL 634
Cdd:COG4987 531 AGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1005-1268 |
3.89e-89 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 303.28 E-value: 3.89e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1005 IPAVFEIMNRNPLI-DGKGKKIEQSKPFDLEFKMVNFAY-PSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQ 1082
Cdd:COG5265 329 MERMFDLLDQPPEVaDAPDAPPLVVGGGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1083 RFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYE 1162
Cdd:COG5265 406 RFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYD 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1163 TEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVV 1242
Cdd:COG5265 486 TRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVL 565
|
250 260
....*....|....*....|....*.
gi 1770234124 1243 QNGKVSEYGTHDTLLTnhSNGVYATL 1268
Cdd:COG5265 566 EAGRIVERGTHAELLA--QGGLYAQM 589
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
152-634 |
2.30e-88 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 300.40 E-value: 2.30e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 152 IRSKYLRAVLRQDVSFFDTDiSTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLT 231
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQ-STGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 232 mfcgvaykAVYVGLAAKEV--------NSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGI 303
Cdd:PRK11176 179 --------SIAIRVVSKRFrnisknmqNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 304 GLGVIYLVtySTWALAF--WYGSILVSRNELSGGAaIACFFGVTIG-GRGLALSLSYFAQFAQGTVAASKVFAIIDripa 380
Cdd:PRK11176 251 SDPIIQLI--ASLALAFvlYAASFPSVMDTLTAGT-ITVVFSSMIAlMRPLKSLTNVNAQFQRGMAACQTLFAILD---- 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 381 IDPYSTTG-RKPETVHGRLELKNVSFAYPSRmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILL 459
Cdd:PRK11176 324 LEQEKDEGkRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 460 DGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAID-ACIAVNAHNFICDLPQGYDTQVGEKGTQLS 538
Cdd:PRK11176 403 DGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEeAARMAYAMDFINKMDNGLDTVIGENGVLLS 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 539 GGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDH 618
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTH 562
|
490
....*....|....*.
gi 1770234124 619 NKLMAQEGAYFSLIKL 634
Cdd:PRK11176 563 AELLAQNGVYAQLHKM 578
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1033-1268 |
5.09e-88 |
|
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: 286.43 E-value: 5.09e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAY-PSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQT 1111
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSK 1191
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1192 VLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTnhSNGVYATL 1268
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA--KGGLYAEM 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
700-1260 |
6.64e-87 |
|
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: 295.51 E-value: 6.64e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 700 REVWKLQKPEAGLLCVGVIFGMLAGAILSLFPLVLGQALTVYFNPDKSKLQkdVGYLCLALVGLGFGCILTMMGQQGFCG 779
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSA--LLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 780 WAGTKLTKRVRDLLFRSILNQEPGWfdSDQNSPGSLVSklsvnctsfrsILGD----------RY--SVLFMGLSSAAVg 847
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAW--LRGKSTGELAT-----------LLTEgvealdgyfaRYlpQLFLAALVPLLI- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 848 LSVSFYLEWR--LALLATI-VTPFtlgasyFSLIINIGSKLDNDS-FDKASGIASAAVSNIRTVTTL-------ATQEKI 916
Cdd:COG4988 150 LVAVFPLDWLsgLILLVTApLIPL------FMILVGKGAAKASRRqWRALARLSGHFLDRLRGLTTLklfgrakAEAERI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 917 VQSFEQSlskpksssikrSQIT----GIALGISqgamysaytLVLFFGAYLVkkdytkfgdvykIFLILVLSTFSV--GQ 990
Cdd:COG4988 224 AEASEDF-----------RKRTmkvlRVAFLSS---------AVLEFFASLS------------IALVAVYIGFRLlgGS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 991 ---FAG-----LAP--------------DTSMASTAIPAVFEIMNRNPLIDGKG-KKIEQSKPFDLEFKMVNFAYPSRPD 1047
Cdd:COG4988 272 ltlFAAlfvllLAPefflplrdlgsfyhARANGIAAAEKIFALLDAPEPAAPAGtAPLPAAGPPSIELEDVSFSYPGGRP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1048 VivLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGE 1127
Cdd:COG4988 352 A--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRE 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1128 NIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESE 1207
Cdd:COG4988 430 NLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1208 KHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTNH 1260
Cdd:COG4988 510 AEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
316-649 |
8.83e-83 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 284.55 E-value: 8.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 316 WALA---------------FWYGSILVSRNELSGGAAIAcF--FGVTIGGRglalsLSYFAQFAQGTV-AASKV---FAI 374
Cdd:PRK13657 239 WALAsvlnraastitmlaiLVLGAALVQKGQLRVGEVVA-FvgFATLLIGR-----LDQVVAFINQVFmAAPKLeefFEV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 375 IDRIPAI-DPYSTtgRKPETVHGRLELKNVSFAYPSrmSVPILNSLNL-VIPSQRIsALVGASGAGKSTIFALLERFYDP 452
Cdd:PRK13657 313 EDAVPDVrDPPGA--IDLGRVKGAVEFDDVSFSYDN--SRQGVEDVSFeAKPGQTV-AIVGPTGAGKSTLINLLQRVFDP 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 453 NKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGE 532
Cdd:PRK13657 388 QSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 533 KGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSV 612
Cdd:PRK13657 468 RGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1770234124 613 IEIGDHNKLMAQEGAYFSLIK---LATEAISSNPVSKKGK 649
Cdd:PRK13657 548 VESGSFDELVARGGRFAALLRaqgMLQEDERRKQPAAEGA 587
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1032-1257 |
2.22e-81 |
|
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: 267.17 E-value: 2.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1032 DLEFKMVNFAYpsRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQT 1111
Cdd:cd03254 2 EIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSK 1191
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1192 VLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLL 1257
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
398-610 |
5.97e-78 |
|
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: 255.00 E-value: 5.97e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFADTILENIlmgkenatkkeaidaciavnahnficdlpqgydtqvgekgtqLSGGQKQRIALARAMIKDPKI 557
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 558 LLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQG 610
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
391-612 |
6.22e-78 |
|
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: 257.01 E-value: 6.22e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 391 PETVHGRLELKNVSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVK 470
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 471 WLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARA 550
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 551 MIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSV 612
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
71-381 |
1.06e-77 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 260.08 E-value: 1.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 71 DLFLIIIGCLGALINGGSQPWYSYLFGNFVNKIALDNDkDQMIKDVRELCVLMSALSGIVVIGAYLQIACWRLVGERLGH 150
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDD-DELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 151 RIRSKYLRAVLRQDVSFFDTDI-STSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTP 229
Cdd:cd18578 86 RLRKLAFRAILRQDIAWFDDPEnSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 230 LTMFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIY 309
Cdd:cd18578 166 LLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQ 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 310 LVTYSTWALAFWYGSILVSRNELSGGAAIACFFGVTIGGRGLALSLSYFAQFAQGTVAASKVFAIIDRIPAI 381
Cdd:cd18578 246 SLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
398-634 |
1.30e-77 |
|
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: 256.64 E-value: 1.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSVpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:cd03252 1 ITFEHVRFRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKI 557
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 558 LLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSLIKL 634
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
227-637 |
1.68e-77 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 272.39 E-value: 1.68e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 227 VTPLTMFCGVAYKAVYVGLA-------AKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGF 299
Cdd:TIGR01846 280 LTGVVIGSLVCYALLSVFVGpilrkrvEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 300 AKGIGLGVIYLVTYSTWALAFWYGSILVSRNELSGGAAIAcfFGVtIGGR--GLALSLSYFAQ-FAQGTVAASKVFAIID 376
Cdd:TIGR01846 360 LGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVA--FNM-LAGRvtQPVLRLAQLWQdFQQTGIALERLGDILN 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 377 RipAIDPYSTTGRKPETVHGRLELKNVSFAYPSRmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGL 456
Cdd:TIGR01846 437 S--PTEPRSAGLAALPELRGAITFENIRFRYAPD-SPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQ 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 457 ILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQ 536
Cdd:TIGR01846 514 VLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGAN 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 537 LSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIG 616
Cdd:TIGR01846 594 LSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESG 673
|
410 420
....*....|....*....|.
gi 1770234124 617 DHNKLMAQEGAYFSLIKLATE 637
Cdd:TIGR01846 674 RHEELLALQGLYARLWQQQSG 694
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
758-1268 |
4.58e-77 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 267.66 E-value: 4.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 758 LALVGLGFgciltMMGQQGF----C-GWAGTKLTKRVRDLLFRSILNQEPGWFDsdQNSPGSLVSKLS------VNCTSF 826
Cdd:PRK11176 69 LVVIGLMI-----LRGITSFissyCiSWVSGKVVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITydseqvASSSSG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 827 RSILGDRYSVLFMGLssaavgLSVSFYLEWRLALLATIVTPFTlgasyfSLIINIGSKldndSFDKASgiasaavSNIRT 906
Cdd:PRK11176 142 ALITVVREGASIIGL------FIMMFYYSWQLSLILIVIAPIV------SIAIRVVSK----RFRNIS-------KNMQN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 907 ----VTTLATQ----EKIVQSFE-QSLSKP---KSSSIKRSQITGI--ALGISQGAMYSAYTLVLFFGAYLVKKDytkfg 972
Cdd:PRK11176 199 tmgqVTTSAEQmlkgHKEVLIFGgQEVETKrfdKVSNRMRQQGMKMvsASSISDPIIQLIASLALAFVLYAASFP----- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 973 dvyKIFLILVLSTFSV---GQFAGLAPDTS-----------MAstAIPAVFEIMNRNPLIDGKGKKIEQSKPfDLEFKMV 1038
Cdd:PRK11176 274 ---SVMDTLTAGTITVvfsSMIALMRPLKSltnvnaqfqrgMA--ACQTLFAILDLEQEKDEGKRVIERAKG-DIEFRNV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1039 NFAYPSRpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEP 1118
Cdd:PRK11176 348 TFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1119 ALFGGTIGENIRFG-NPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDE 1197
Cdd:PRK11176 427 HLFNDTIANNIAYArTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1198 ATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTNhsNGVYATL 1268
Cdd:PRK11176 507 ATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ--NGVYAQL 575
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1030-1247 |
1.35e-75 |
|
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: 250.47 E-value: 1.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1030 PFDLE----FKMVNFAYPSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLK 1105
Cdd:cd03248 5 PDHLKgivkFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1106 WLRLQTALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARA 1185
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1186 IVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKV 1247
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1033-1269 |
8.31e-75 |
|
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: 248.56 E-value: 8.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYpsRPD-VIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQT 1111
Cdd:cd03252 1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSK 1191
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1192 VLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTnhSNGVYATLV 1269
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA--ENGLYAYLY 234
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
793-1268 |
2.61e-74 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 262.76 E-value: 2.61e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 793 LFRSILNQEPGWFDSDQNspGSLVSKLSvNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPFtlga 872
Cdd:TIGR01846 218 LYRHLLGLPLGYFESRRV--GDTVARVR-ELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVC---- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 873 sYFSLIINIGSKLDNDSFDKASGIASA------AVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQ 946
Cdd:TIGR01846 291 -YALLSVFVGPILRKRVEDKFERSAAAtsflveSVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 947 GAMYSAYTLVLFFGAYLVKKDYTKFGDVYKIFLILVLSTFSVGQFAGLAPDTSMASTAIPAVFEIMN--RNPLIDGKGKK 1024
Cdd:TIGR01846 370 LIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNspTEPRSAGLAAL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1025 IEQSKpfDLEFKMVNFAYpsRPDV-IVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLD 1103
Cdd:TIGR01846 450 PELRG--AITFENIRFRY--APDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1104 LKWLRLQTALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIA 1183
Cdd:TIGR01846 526 PAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIA 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1184 RAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTnhSNG 1263
Cdd:TIGR01846 606 RALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLA--LQG 683
|
....*
gi 1770234124 1264 VYATL 1268
Cdd:TIGR01846 684 LYARL 688
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
933-1270 |
1.02e-72 |
|
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: 254.69 E-value: 1.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 933 KRSQITGIALGISQGAMYSAYTLVLFFGAYLVKKdytkfGDVYKIFL-ILVLSTFSVGQ-FAGLAPdtsmASTAIPA--- 1007
Cdd:COG4987 234 RLARLSALAQALLQLAAGLAVVAVLWLAAPLVAA-----GALSGPLLaLLVLAALALFEaLAPLPA----AAQHLGRvra 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1008 ----VFEIMNRNPLIDGKGKKIEQSKPFDLEFKMVNFAYPSRPDvIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQR 1083
Cdd:COG4987 305 aarrLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1084 FYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYET 1163
Cdd:COG4987 384 FLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDT 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1164 EVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQ 1243
Cdd:COG4987 464 WLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLE 543
|
330 340
....*....|....*....|....*..
gi 1770234124 1244 NGKVSEYGTHDTLLTNhsNGVYATLVH 1270
Cdd:COG4987 544 DGRIVEQGTHEELLAQ--NGRYRQLYQ 568
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
353-607 |
2.89e-72 |
|
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: 252.21 E-value: 2.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 353 LSLSYFAQfAQGTVAASKVFAIIDRIPAidPYSTTGRKPETVHGRLELKNVSFAYPSRMsvPILNSLNLVIPSQRISALV 432
Cdd:TIGR02857 280 LGAQYHAR-ADGVAAAEALFAVLDAAPR--PLAGKAPVTAAPASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALV 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 433 GASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIA 512
Cdd:TIGR02857 355 GPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALER 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 513 VNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIA 592
Cdd:TIGR02857 435 AGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVT 514
|
250
....*....|....*
gi 1770234124 593 HRLATVKNAETIIVL 607
Cdd:TIGR02857 515 HRLALAALADRIVVL 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
843-1270 |
1.55e-70 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 248.72 E-value: 1.55e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 843 SAAVGLSV----SFYLEWRLALLAtivtpFTLGASYFSLIINIGSKLDN------DSFDKASGIASAAVSNIrtvttlat 912
Cdd:PRK13657 139 ATLVALVVllplALFMNWRLSLVL-----VVLGIVYTLITTLVMRKTKDgqaaveEHYHDLFAHVSDAIGNV-------- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 913 qeKIVQSF-----EQSLSKPKSSSIKRSQIT-----GIALGISQGAMYSAYTLVLFFGAYLVKKDYTKFGDvykIFLILV 982
Cdd:PRK13657 206 --SVVQSYnrieaETQALRDIADNLLAAQMPvlswwALASVLNRAASTITMLAILVLGAALVQKGQLRVGE---VVAFVG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 983 LSTFSVG---QFAGLAPDTSMASTAIPAVFEIMNRNPLIDGKGKKIE-QSKPFDLEFKMVNFAYP-SRPDVivlREFCLK 1057
Cdd:PRK13657 281 FATLLIGrldQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDlGRVKGAVEFDDVSFSYDnSRQGV---EDVSFE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1058 VKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNPNAS 1137
Cdd:PRK13657 358 AKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDAT 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1138 WSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKI 1217
Cdd:PRK13657 438 DEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1218 IKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLtnHSNGVYATLVH 1270
Cdd:PRK13657 518 MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV--ARGGRFAALLR 568
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1033-1246 |
2.44e-68 |
|
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: 227.27 E-value: 2.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPDViVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:cd03228 1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGGTIGENIrfgnpnaswseveeaakeayihnficglprgyetevgesgiqLSGGQKQRIAIARAIVKKSKV 1192
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1193 LLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGK 1246
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
323-624 |
5.31e-67 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 241.31 E-value: 5.31e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 323 GSILVSRNELSGGAAIACffgVTIGGRGLA----LSlSYFAQFAQGTVAaskvFAIIDRI---PAIDPYSTTGRKPETVH 395
Cdd:TIGR03375 390 GVYLISDGELTMGGLIAC---VMLSGRALAplgqLA-GLLTRYQQAKTA----LQSLDELmqlPVERPEGTRFLHRPRLQ 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 396 GRLELKNVSFAYPSrMSVPILNSLNLVI-PSQRIsALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRS 474
Cdd:TIGR03375 462 GEIEFRNVSFAYPG-QETPALDNVSLTIrPGEKV-AIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRR 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKD 554
Cdd:TIGR03375 540 NIGYVPQDPRLFYGTLRDNIALGAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRD 619
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 555 PKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQ 624
Cdd:TIGR03375 620 PPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVLEA 689
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
66-635 |
1.03e-64 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 243.01 E-value: 1.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 66 YSTKFDLFLIIigcLGALINGGSQPWYSYLFGNFVNKIaLDNDKDQMIKDVRELCVLMSALSgiVVIGAYLQIACWRLVG 145
Cdd:PTZ00265 821 FSYKKDVTIIA---LSILVAGGLYPVFALLYAKYVSTL-FDFANLEANSNKYSLYILVIAIA--MFISETLKNYYNNVIG 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 146 ERLGHRIRSKYLRAVLRQDVSFFDTDISTSDIMHG-ISSDVAQIQEVMGDKMSQFIYhiftFICGYIVGFLKSWKVSLAV 224
Cdd:PTZ00265 895 EKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAhINRDVHLLKTGLVNNIVIFTH----FIVLFLVSMVMSFYFCPIV 970
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 225 LAVTPLTMFCGVAYKAVYVGLAA------KEVNS-------------YKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDA 285
Cdd:PTZ00265 971 AAVLTGTYFIFMRVFAIRARLTAnkdvekKEINQpgtvfaynsddeiFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEK 1050
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 286 VLDESVPIGKKLGFAKGIGLGVIYLVTYSTWALAFWYGSILVSRNELSGGAAIACFFGVTIGGRGLALSLSYFAQFAQGT 365
Cdd:PTZ00265 1051 AIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAK 1130
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 366 VAASKVFAIIDRIPAIDPYSTTG---RKPETVHGRLELKNVSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTI 442
Cdd:PTZ00265 1131 LSFEKYYPLIIRKSNIDVRDNGGiriKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTV 1210
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 443 FALLERFYD------------------------------------------------------PNKGLILLDGQDIRTLQ 468
Cdd:PTZ00265 1211 MSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYN 1290
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 469 VKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALA 548
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIA 1370
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 549 RAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKNAETIIVLEQ----GSVIEI-GDHNKL 621
Cdd:PTZ00265 1371 RALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEEL 1450
|
650
....*....|....*
gi 1770234124 622 M-AQEGAYFSLIKLA 635
Cdd:PTZ00265 1451 LsVQDGVYKKYVKLA 1465
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
396-613 |
2.00e-63 |
|
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: 215.15 E-value: 2.00e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 396 GRLELKNVSFAYPSrMSVPILNSLNLVI-PSQRIsALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRS 474
Cdd:cd03245 1 GRIEFRNVSFSYPN-QEIPALDNVSLTIrAGEKV-AIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKD 554
Cdd:cd03245 79 NIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 555 PKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVI 613
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
398-1257 |
2.80e-63 |
|
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: 238.69 E-value: 2.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYpSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSqmg 477
Cdd:TIGR00957 637 ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQN--- 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 mvgqepvlfaDTILENILMGK--ENATKKEAIDACiAVNAHNFIcdLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDP 555
Cdd:TIGR00957 713 ----------DSLRENILFGKalNEKYYQQVLEAC-ALLPDLEI--LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 556 KILLLDEPTSALDPK-SESLVQQAI--DKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSLI 632
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 633 K--------LATEAISSNPVSKKGKTVINQE-TSSNCDLLKQNHVYEISPSGYMKSIQDANQPESAKLNKIKSYKirEVW 703
Cdd:TIGR00957 860 RtyapdeqqGHLEDSWTALVSGEGKEAKLIEnGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKE--ETW 937
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 704 KL---QKPEAGLLCVGVIFGM-----LAGAILSLFpLVLGQA---------LTVYFN-PDKSKLQKDVGYLCLALVGLGF 765
Cdd:TIGR00957 938 KLmeaDKAQTGQVELSVYWDYmkaigLFITFLSIF-LFVCNHvsalasnywLSLWTDdPMVNGTQNNTSLRLSVYGALGI 1016
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 766 GCILTMMGQQGFCGWAGTKLTKRVRDLLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDrYSVLFMGLSSAA 845
Cdd:TIGR00957 1017 LQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPP-VIKMFMGSLFNV 1093
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 846 VGLSVSFYLEWRLAllATIVTPftLGASYFslIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQekIVQSFEQS-- 923
Cdd:TIGR00957 1094 IGALIVILLATPIA--AVIIPP--LGLLYF--FVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVS--VIRAFEEQer 1165
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 924 ---LSKPKSSSIKRSQITGIALG--ISQGAMYSAYTLVLFFGaylvkkdytkfgdvykIFLILVLSTFSVGqFAGLAPDT 998
Cdd:TIGR00957 1166 fihQSDLKVDENQKAYYPSIVANrwLAVRLECVGNCIVLFAA----------------LFAVISRHSLSAG-LVGLSVSY 1228
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 999 SMASTA---------------IPAVFEIMNRNPLIDGKGKKIEQSKPFD-------LEFKmvNFAYPSRPDV-IVLREFC 1055
Cdd:TIGR00957 1229 SLQVTFylnwlvrmssemetnIVAVERLKEYSETEKEAPWQIQETAPPSgwpprgrVEFR--NYCLRYREDLdLVLRHIN 1306
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIrfgNPN 1135
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPF 1383
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1136 ASWSEVE--EAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDA 1213
Cdd:TIGR00957 1384 SQYSDEEvwWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQST 1463
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 1770234124 1214 IRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLL 1257
Cdd:TIGR00957 1464 IRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
997-1242 |
1.18e-62 |
|
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: 224.09 E-value: 1.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 997 DTSMASTAIPAVFEIMNRNPLIDGKGKKIEQSKPFDLEFKMVNFAYPSRPDVivLREFCLKVKGGTMVAVVGGSGSGKST 1076
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKST 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1077 VIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICG 1156
Cdd:TIGR02857 364 LLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1157 LPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKA 1236
Cdd:TIGR02857 444 LPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
....*.
gi 1770234124 1237 NAIAVV 1242
Cdd:TIGR02857 524 DRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
358-632 |
3.35e-62 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 223.93 E-value: 3.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 358 FAQFAQGTVAASKVFAIIDRIPAIDpYSTTGrKPETVHGRLELKNVSFAYPSRmSVPILNSLNLVIPS-QRIsALVGASG 436
Cdd:PRK11160 301 FQHLGQVIASARRINEITEQKPEVT-FPTTS-TAAADQVSLTLNNVSFTYPDQ-PQPVLKGLSLQIKAgEKV-ALLGRTG 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 437 AGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAH 516
Cdd:PRK11160 377 CGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 517 NFIcDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLA 596
Cdd:PRK11160 457 KLL-EDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLT 535
|
250 260 270
....*....|....*....|....*....|....*.
gi 1770234124 597 TVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSLI 632
Cdd:PRK11160 536 GLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
665-1272 |
8.18e-62 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 233.77 E-value: 8.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 665 QNHVYEISPSGYMKSIQDANQPEsakLNKIKSYKIREVWKLQK------------PEAGLLCVGVIFGMLAGAILSLFPL 732
Cdd:PTZ00265 5 QRQKKDNNSGGGNLSIKDEVEKE---LNKKGTFELYKKIKTQKipfflpfkclpaSHRKLLGVSFVCATISGGTLPFFVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 733 VLGQALTvyfnpdKSKLQKDVGYLCLALVGLG-FGCILTMMGQqgFC-GWAGTKLTKRVRDLLFRSILNQEPGWFDsdqN 810
Cdd:PTZ00265 82 VFGVIMK------NMNLGENVNDIIFSLVLIGiFQFILSFISS--FCmDVVTTKILKTLKLEFLKSVFYQDGQFHD---N 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 811 SPGS-LVSKLSVNCTSFRSILGDRYSVLFMgLSSAAVGLSV-SFYLEWRLALLATIVTPFTlgasYF-SLIINIGSKLDN 887
Cdd:PTZ00265 151 NPGSkLTSDLDFYLEQVNAGIGTKFITIFT-YASAFLGLYIwSLFKNARLTLCITCVFPLI----YIcGVICNKKVKINK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 888 DSF----DKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMYSAYTLVLFFGAYL 963
Cdd:PTZ00265 226 KTSllynNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 964 VKKDYTKF--------GDVYKIFLILVLSTFSVGQFAGLAPDTSMASTAIPAVFEIMNRNPLIDGK--GKKIEQSKpfDL 1033
Cdd:PTZ00265 306 IISDLSNQqpnndfhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNddGKKLKDIK--KI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1034 EFKMVNFAYPSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMG-GRDLRDLDLKWLRLQTA 1112
Cdd:PTZ00265 384 QFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIG 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGGTIGENIRFG----------------NPNASW-------------------------------------- 1138
Cdd:PTZ00265 464 VVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQenknkrnscrakcagdlndmsnttdsneliemrknyqt 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1139 ---SEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIR 1215
Cdd:PTZ00265 544 ikdSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1216 KII--KRTTTIVVVHRLSTIKKANAIAVV----------------------------------------QNGKVS----- 1248
Cdd:PTZ00265 624 NLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnNNNKINnagsy 703
|
730 740
....*....|....*....|....*.
gi 1770234124 1249 --EYGTHDTLLTNhSNGVYATLVHSE 1272
Cdd:PTZ00265 704 iiEQGTHDALMKN-KNGIYYTMINNQ 728
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
713-1004 |
2.61e-61 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 212.33 E-value: 2.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 713 LCVGVIFGMLAGAILSLFPLVLGQALTVY-----FNPDKSKLQKDVGYLCLALVGLGFGCILTMMGQQGFCGWAGTKLTK 787
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 788 RVRDLLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTP 867
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 868 FTLGASYF-SLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQ 946
Cdd:cd18577 159 LIAIVGGImGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 947 GAMYSAYTLVLFFGAYLVKKDYTKFGDVYKIFLILVLSTFSVGQFAGLAPDTSMASTA 1004
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAA 296
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
363-634 |
6.95e-61 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 220.36 E-value: 6.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 363 QGTVAASKVFAIIDRipAIDPYSTTGRKPETvhGRLELKNVSFAYpsRMSVPILNSLNLVIPSQRISALVGASGAGKSTI 442
Cdd:PRK10790 310 QAVVAGERVFELMDG--PRQQYGNDDRPLQS--GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 443 FALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKEnaTKKEAI-DACIAVNAHNFICD 521
Cdd:PRK10790 384 ASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD--ISEEQVwQALETVQLAELARS 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 522 LPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNA 601
Cdd:PRK10790 462 LPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEA 541
|
250 260 270
....*....|....*....|....*....|...
gi 1770234124 602 ETIIVLEQGSVIEIGDHNKLMAQEGAYFSLIKL 634
Cdd:PRK10790 542 DTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQL 574
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1032-1247 |
1.58e-59 |
|
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: 203.98 E-value: 1.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1032 DLEFKMVNFAYPSRPdVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQT 1111
Cdd:cd03245 2 RIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSK 1191
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1192 VLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKV 1247
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1033-1270 |
2.34e-59 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 218.66 E-value: 2.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYpSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:TIGR03796 478 VELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVA 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKV 1192
Cdd:TIGR03796 557 MVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSI 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1193 LLLDEATSALDLESEKHVQDAIRKiiKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTnhSNGVYATLVH 1270
Cdd:TIGR03796 637 LILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWA--VGGAYARLIR 710
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
323-624 |
7.71e-59 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 213.84 E-value: 7.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 323 GSILVSRNELSGGAAIAcffGVTIGGRGLA---LSLSYFAQFAQGTVAASKVFAIIDRIPAiDPYSTTGRKPEtvhGRLE 399
Cdd:COG4618 260 GAYLVIQGEITPGAMIA---ASILMGRALApieQAIGGWKQFVSARQAYRRLNELLAAVPA-EPERMPLPRPK---GRLS 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 400 LKNVSFAYPSRmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTlqvkWLRSQMG-M 478
Cdd:COG4618 333 VENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ----WDREELGrH 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 479 VG---QEPVLFADTILENI-LMGKENATKkeAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKD 554
Cdd:COG4618 408 IGylpQDVELFDGTIAENIaRFGDADPEK--VVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGD 485
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 555 PKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQ 624
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
260-628 |
1.84e-58 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 212.65 E-value: 1.84e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 260 AEQAIGSIRTVFSFVAEDSLAARYDAVLDESvpiGKK-LGFAKGIGL--GVIYLVTYSTWALAFWYGSILVSRNELSGGA 336
Cdd:PRK10789 179 TQESLTSIRMIKAFGLEDRQSALFAADAEDT---GKKnMRVARIDARfdPTIYIAIGMANLLAIGGGSWMVVNGSLTLGQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 337 --AIACFFGVTIGGRgLALSLsYFAQFAQGTVAASKVFAIIDRIPAIDpySTTGRKPETvHGRLELKNVSFAYPSRmSVP 414
Cdd:PRK10789 256 ltSFVMYLGLMIWPM-LALAW-MFNIVERGSAAYSRIRAMLAEAPVVK--DGSEPVPEG-RGELDVNIRQFTYPQT-DHP 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 415 ILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENI 494
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 495 LMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESL 574
Cdd:PRK10789 410 ALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQ 489
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 575 VQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAY 628
Cdd:PRK10789 490 ILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
419-639 |
2.08e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 210.09 E-value: 2.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 419 LNLVIPS-QRIsALVGASGAGKSTIFALLERFYdPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMG 497
Cdd:PRK11174 369 LNFTLPAgQRI-ALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 498 KENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQ 577
Cdd:PRK11174 447 NPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQ 526
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 578 AIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSLIKLATEAI 639
Cdd:PRK11174 527 ALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEEI 588
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
398-1281 |
9.59e-57 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 217.54 E-value: 9.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGK-STIFALLERFYDPNKGLILLDGQDIRTLQVKWLrsqm 476
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVIRGSVAYVPQVSWI---- 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 gmvgqepvlFADTILENILMGKENATKK--EAIDaciaVNAHNFICDLPQGYD-TQVGEKGTQLSGGQKQRIALARAMIK 553
Cdd:PLN03232 691 ---------FNATVRENILFGSDFESERywRAID----VTALQHDLDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 554 DPKILLLDEPTSALDPK-SESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLmAQEGAYFSli 632
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGSLFK-- 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 633 KLATEAissnpvskkGKTVINQETSSNCD-LLKQNHVYEISPSGY-MKSIQDANQPESAKLNK------IKSYKIreVWK 704
Cdd:PLN03232 835 KLMENA---------GKMDATQEVNTNDEnILKLGPTVTIDVSERnLGSTKQGKRGRSVLVKQeeretgIISWNV--LMR 903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 705 LQKPEAGLLCVGVIFgmLAGAILSLFPLVLGQALTVYFNPDKSKLQKDvGYLCLALVGLGFGCILTMMGQQGFCGWAGTK 784
Cdd:PLN03232 904 YNKAVGGLWVVMILL--VCYLTTEVLRVSSSTWLSIWTDQSTPKSYSP-GFYIVVYALLGFGQVAVTFTNSFWLISSSLH 980
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 785 LTKRVRDLLFRSILNQEPGWFDSdqNSPGSLVSKLSVNC----TSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLAL 860
Cdd:PLN03232 981 AAKRLHDAMLNSILRAPMLFFHT--NPTGRVINRFSKDIgdidRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMP 1058
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 861 LATIvtpFTLGASYFSLIINIGSKLDndSFDKAS-----GIASAAVSNIRTVTTLATQEKIV-QSFEQSL--SKPKSSSI 932
Cdd:PLN03232 1059 LLIL---FYAAYLYYQSTSREVRRLD--SVTRSPiyaqfGEALNGLSSIRAYKAYDRMAKINgKSMDNNIrfTLANTSSN 1133
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 933 KRSQITGIALGisqGAM--YSAYTLVLFFGAylvKKDYTKFGDVYKIFLILVLSTFSVgqFAGLAPDTSMASTAIPAVFE 1010
Cdd:PLN03232 1134 RWLTIRLETLG---GVMiwLTATFAVLRNGN---AENQAGFASTMGLLLSYTLNITTL--LSGVLRQASKAENSLNSVER 1205
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1011 IMNRNPLIDGKGKKIEQSKPFD-------LEFKMVNFAYpsRPDVI-VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQ 1082
Cdd:PLN03232 1206 VGNYIDLPSEATAIIENNRPVSgwpsrgsIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALF 1283
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1083 RFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIR-FGNPNASwsEVEEAAKEAYIHNFICGLPRGY 1161
Cdd:PLN03232 1284 RIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDpFSEHNDA--DLWEALERAHIKDVIDRNPFGL 1361
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1162 ETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAV 1241
Cdd:PLN03232 1362 DAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILV 1441
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1770234124 1242 VQNGKVSEYGTHDTLLTNHSNGvYATLVHSEMEANADHFS 1281
Cdd:PLN03232 1442 LSSGQVLEYDSPQELLSRDTSA-FFRMVHSTGPANAQYLS 1480
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
396-616 |
1.23e-56 |
|
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: 195.79 E-value: 1.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 396 GRLELKNVSFAYPSRmSVPILNSLNLVI-PSQRIsALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRS 474
Cdd:cd03244 1 GDIEFKNVSLRYRPN-LPPVLKNISFSIkPGEKV-GIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFADTILENiLMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKD 554
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSN-LDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 555 PKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIG 616
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
75-371 |
1.09e-55 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 196.73 E-value: 1.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 75 IIIGCLGALINGGSQPWYSYLFGNFVNKIA------------LDNDKDQMIKDVRE----LCVLMSALSGIVVIGAYLQI 138
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTnggmtnitgnssGLNSSAGPFEKLEEemtlYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 139 ACWRLVGERLGHRIRSKYLRAVLRQDVSFFDTDiSTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSW 218
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVN-DTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 219 KVSLAVLAVTPLTMFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLG 298
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 299 FAKGIGLGVIYLVTYSTWALAFWYGSILVSRNELSGGAAIACFFGVTIGGRGLALSLSYFAQFAQGTVAASKV 371
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
135-632 |
3.03e-55 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 206.51 E-value: 3.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 135 YLQIACWRLVGERLGHRIRSKYLRAVLRQDVSFFDTDiSTSDIMHGISsDVAQIQEVMGDKM-SQFIYHIFTFICGYIVG 213
Cdd:TIGR01193 214 YIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTR-RTGEIVSRFT-DASSIIDALASTIlSLFLDMWILVIVGLFLV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 214 FLKSwKVSLAVLAVTPLTMFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSlaaRYDAVLDESVP- 292
Cdd:TIGR01193 292 RQNM-LLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAE---RYSKIDSEFGDy 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 293 IGKKLGFAKG-IGLGVIYLVTYSTWALA-FWYGSILVSRNELSGGAAIAcffgvtiggrgLALSLSYFAQFAQGTV---- 366
Cdd:TIGR01193 368 LNKSFKYQKAdQGQQAIKAVTKLILNVViLWTGAYLVMRGKLTLGQLIT-----------FNALLSYFLTPLENIInlqp 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 367 ---AASKVFAIIDRIPAIDPYSTTGRKP---ETVHGRLELKNVSFAYPsrMSVPILNSLNLVIPSQRISALVGASGAGKS 440
Cdd:TIGR01193 437 klqAARVANNRLNEVYLVDSEFINKKKRtelNNLNGDIVINDVSYSYG--YGSNILSDISLTIKMNSKTTIVGMSGSGKS 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 441 TIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMG-KENATKKEAIDACIAVNAHNFI 519
Cdd:TIGR01193 515 TLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDI 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 520 CDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSEslvQQAIDKIS--KGRTTIVIAHRLAT 597
Cdd:TIGR01193 595 ENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLLnlQDKTIIFVAHRLSV 671
|
490 500 510
....*....|....*....|....*....|....*
gi 1770234124 598 VKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSLI 632
Cdd:TIGR01193 672 AKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1032-1252 |
1.79e-54 |
|
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: 189.63 E-value: 1.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1032 DLEFKMVNFAYPSRPDViVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQT 1111
Cdd:cd03244 2 DIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVGQEPALFGGTIGENIrfgNPNASWSEVE--EAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKK 1189
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNL---DPFGEYSDEElwQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1190 SKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGT 1252
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1039-1289 |
1.03e-53 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 198.78 E-value: 1.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1039 NFAYPSRpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEP 1118
Cdd:PRK10789 320 QFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1119 ALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEA 1198
Cdd:PRK10789 399 FLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1199 TSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTnhSNGVYATLVH-SEMEANA 1277
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ--QSGWYRDMYRyQQLEAAL 556
|
250
....*....|..
gi 1770234124 1278 DHFSLVQQPVTD 1289
Cdd:PRK10789 557 DDAPEIREEAVD 568
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1058-1275 |
3.76e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 197.37 E-value: 3.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1058 VKGGTMVAVVGGSGSGKSTVIWLMQRFYdPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNPNAS 1137
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDAS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1138 WSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKI 1217
Cdd:PRK11174 452 DEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA 531
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1218 IKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLltNHSNGVYATLVHSEMEA 1275
Cdd:PRK11174 532 SRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL--SQAGGLFATLLAHRQEE 587
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
281-595 |
4.32e-53 |
|
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: 196.04 E-value: 4.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 281 ARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYSTWALAFWYGSILVSRNELSGgAAIACFfgvtiggrgLALSLSYFAQ 360
Cdd:TIGR02868 217 AQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAP-VTLAVL---------VLLPLAAFEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 361 FAQGTVAASKVFAII---DRI--------PAIDPYSTTGRKPETVHGRLELKNVSFAYPSrmSVPILNSLNLVIPSQRIS 429
Cdd:TIGR02868 287 FAALPAAAQQLTRVRaaaERIvevldaagPVAEGSAPAAGAVGLGKPTLELRDLSAGYPG--APPVLDGVSLDLPPGERV 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 430 ALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDA 509
Cdd:TIGR02868 365 AILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 510 CIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTI 589
Cdd:TIGR02868 445 LERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVV 524
|
....*.
gi 1770234124 590 VIAHRL 595
Cdd:TIGR02868 525 LITHHL 530
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
853-1270 |
8.90e-53 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 198.81 E-value: 8.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 853 YLEWRLALLATIVTPFtlgasYFSLII---NIGSKLDNDSFDKASGIASAAVSN---IRTVTTLATQE----KIVQSFEQ 922
Cdd:TIGR01193 292 RQNMLLFLLSLLSIPV-----YAVIIIlfkRTFNKLNHDAMQANAVLNSSIIEDlngIETIKSLTSEAerysKIDSEFGD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 923 SLSKpkssSIKRSQITGIALGISQGAMYSAYTLVLFFGAYLVKKDYTKFGDVYKIFLILVLSTFSVGQFAGLAPDTSMAS 1002
Cdd:TIGR01193 367 YLNK----SFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAAR 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1003 TAipavFEIMNRNPLIDG----KGKKIEQSKP-FDLEFKMVNFAYPSRPDVivLREFCLKVKGGTMVAVVGGSGSGKSTV 1077
Cdd:TIGR01193 443 VA----NNRLNEVYLVDSefinKKKRTELNNLnGDIVINDVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTL 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1078 IWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGN-PNASWSEVEEAAKEAYIHNFICG 1156
Cdd:TIGR01193 517 AKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIEN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1157 LPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKiIKRTTTIVVVHRLSTIKKA 1236
Cdd:TIGR01193 597 MPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQS 675
|
410 420 430
....*....|....*....|....*....|....
gi 1770234124 1237 NAIAVVQNGKVSEYGTHDTLLTnhSNGVYATLVH 1270
Cdd:TIGR01193 676 DKIIVLDHGKIIEQGSHDELLD--RNGFYASLIH 707
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
717-1273 |
1.59e-52 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 197.87 E-value: 1.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 717 VIFGMLAGAILSLFPLVLGQALTVYFNPDKSKLQkdVGYLCLALVGLGFGCI-------LTMMGQQGFCGWAgtkLTKRV 789
Cdd:TIGR03797 141 ILAMGLLGTLLGMLVPIATGILIGTAIPDADRSL--LVQIALALLAAAVGAAafqlaqsLAVLRLETRMDAS---LQAAV 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 790 RDLLfrsiLNQEPGWFDsdQNSPGSLVSK-LSVNctSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPF 868
Cdd:TIGR03797 216 WDRL----LRLPVSFFR--QYSTGDLASRaMGIS--QIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALVAVALALV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 869 ----TLGASYFSL-----IINIGSKLDNDSFDKASGIasaavSNIRtvttLATQEKivQSFEQsLSKPKSSSIK---RSQ 936
Cdd:TIGR03797 288 aiavTLVLGLLQVrkerrLLELSGKISGLTVQLINGI-----SKLR----VAGAEN--RAFAR-WAKLFSRQRKlelSAQ 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 937 ITGIALGISQGAMYSAYTLVLF-FGAYLVKKDYTKFGDvykiFLilvlsTF--SVGQFAGLApdTSMASTAIpavfEIMN 1013
Cdd:TIGR03797 356 RIENLLTVFNAVLPVLTSAALFaAAISLLGGAGLSLGS----FL-----AFntAFGSFSGAV--TQLSNTLI----SILA 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1014 RNPLIDgKGKKIEQSKPFDLEFKM-------------VNFAYpsRPD-VIVLREFCLKVKGGTMVAVVGGSGSGKSTVIW 1079
Cdd:TIGR03797 421 VIPLWE-RAKPILEALPEVDEAKTdpgklsgaievdrVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLR 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1080 LMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNPnASWSEVEEAAKEAYIHNFICGLPR 1159
Cdd:TIGR03797 498 LLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAP-LTLDEAWEAARMAGLAEDIRAMPM 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1160 GYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIikRTTTIVVVHRLSTIKKANAI 1239
Cdd:TIGR03797 577 GMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRI 654
|
570 580 590
....*....|....*....|....*....|....
gi 1770234124 1240 AVVQNGKVSEYGTHDTLLTnhSNGVYATLVHSEM 1273
Cdd:TIGR03797 655 YVLDAGRVVQQGTYDELMA--REGLFAQLARRQL 686
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1033-1254 |
2.08e-51 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 191.50 E-value: 2.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTV------IWLmqrfydPIGGKVMMGGRDLRDLDlkw 1106
Cdd:COG4618 331 LSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLarllvgVWP------PTAGSVRLDGADLSQWD--- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1107 lrlQTAL---VG---QEPALFGGTIGENI-RFGNPNASwsEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQR 1179
Cdd:COG4618 401 ---REELgrhIGylpQDVELFDGTIAENIaRFGDADPE--KVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1180 IAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKKANAIAVVQNGKVSEYGTHD 1254
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVItHRPSLLAAVDKLLVLRDGRVQAFGPRD 551
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
75-347 |
3.05e-51 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 182.46 E-value: 3.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 75 IIIGCLGALINGGSQPWYSYLFGNFVNKIALDNDKDQMikDVRELCVLMSALSGIVVIGAYLQIACWRLVGERLGHRIRS 154
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQ--ALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 155 KYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFC 234
Cdd:pfam00664 79 KLFKKILRQPMSFFDT-NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 235 GVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYS 314
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*
gi 1770234124 315 TWALAFWYGSILVSRNELSGG--AAIACFFGVTIG 347
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGdlVAFLSLFAQLFG 272
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
323-624 |
2.25e-50 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 188.33 E-value: 2.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 323 GSILVSRNELSGGAAIAcffGVTIGGRGLA---LSLSYFAQFAQGTVAASKVFAIIDRIPAIDPYSttgRKPEtVHGRLE 399
Cdd:TIGR01842 246 GAYLAIDGEITPGMMIA---GSILVGRALApidGAIGGWKQFSGARQAYKRLNELLANYPSRDPAM---PLPE-PEGHLS 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 400 LKNVSFAYPSRMSvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRtlqvKWLRSQMG-M 478
Cdd:TIGR01842 319 VENVTIVPPGGKK-PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK----QWDRETFGkH 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 479 VG---QEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDP 555
Cdd:TIGR01842 394 IGylpQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDP 473
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 556 KILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQ 624
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
400-1283 |
4.01e-50 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 196.11 E-value: 4.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 400 LKNVSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGK-STIFALLERFYDPNKGLILLDGQDIRTLQVKWLrsqmgm 478
Cdd:PLN03130 617 IKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRGTVAYVPQVSWI------ 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 479 vgqepvlFADTILENILMGKE-NATKKE-AIDacIAVNAHNFICdLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPK 556
Cdd:PLN03130 691 -------FNATVRDNILFGSPfDPERYErAID--VTALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 557 ILLLDEPTSALDPKsesLVQQAIDKISK----GRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQeGAYF--- 629
Cdd:PLN03130 761 VYIFDDPLSALDAH---VGRQVFDKCIKdelrGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN-GPLFqkl 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 630 -----SLIKLATEAISSNPVSKKGKTVINQETSSncdlLKQNhvyeispSGYMKsiqdanQPESAKLNKIKSYKiREV-- 702
Cdd:PLN03130 837 menagKMEEYVEENGEEEDDQTSSKPVANGNANN----LKKD-------SSSKK------KSKEGKSVLIKQEE-RETgv 898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 703 --WKL----QKPEAGLLCVGVIFgmLAGAILSLFPLVLGQALTVYFNPDKSKLQKDvGYLCLALVGLGFGCILTMMGQQG 776
Cdd:PLN03130 899 vsWKVleryKNALGGAWVVMILF--LCYVLTEVFRVSSSTWLSEWTDQGTPKTHGP-LFYNLIYALLSFGQVLVTLLNSY 975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 777 FCGWAGTKLTKRVRDLLFRSILNQEPGWFDSdqNSPGSLVSKlsvnctsFRSILG--DRYSVLF--MGLSSAAVGLSVSF 852
Cdd:PLN03130 976 WLIMSSLYAAKRLHDAMLGSILRAPMSFFHT--NPLGRIINR-------FAKDLGdiDRNVAVFvnMFLGQIFQLLSTFV 1046
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 853 ylewrlalLATIVTPFTLGASYFSLIINIGSKLdndsfdkasgiasaavsnirtvttlatqekivqsFEQSLSK--PKSS 930
Cdd:PLN03130 1047 --------LIGIVSTISLWAIMPLLVLFYGAYL----------------------------------YYQSTARevKRLD 1084
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 931 SIKRSQIT---GIAL-GISQGAMYSAY-----------------TLV------------LFFGAYLV------------- 964
Cdd:PLN03130 1085 SITRSPVYaqfGEALnGLSTIRAYKAYdrmaeingrsmdnnirfTLVnmssnrwlairlETLGGLMIwltasfavmqngr 1164
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 965 KKDYTKFGDVYKIFLILVLSTFS----VGQFAGLAPDTSMASTAIPAVFEIMNRNPLIdgkgkkIEQSKP-------FDL 1033
Cdd:PLN03130 1165 AENQAAFASTMGLLLSYALNITSlltaVLRLASLAENSLNAVERVGTYIDLPSEAPLV------IENNRPppgwpssGSI 1238
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1034 EFKMVNFAYpsRPDVI-VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:PLN03130 1239 KFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGGTIGENIR-FGNPNASwsEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSK 1191
Cdd:PLN03130 1317 IIPQAPVLFSGTVRFNLDpFNEHNDA--DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1192 VLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTNhSNGVYATLVHS 1271
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSN-EGSAFSKMVQS 1473
|
970
....*....|...
gi 1770234124 1272 EMEANADHF-SLV 1283
Cdd:PLN03130 1474 TGAANAQYLrSLV 1486
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1010-1271 |
2.47e-48 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 182.72 E-value: 2.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1010 EIMNRNPLIDGKGKKIEQSKPFDLEFKMVNFAYPSRPDvIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIG 1089
Cdd:PRK11160 316 EITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1090 GKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAYIHNFICGlPRGYETEVGESG 1169
Cdd:PRK11160 395 GEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1170 IQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSE 1249
Cdd:PRK11160 474 RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
250 260
....*....|....*....|..
gi 1770234124 1250 YGTHDTLLTNHsnGVYATLVHS 1271
Cdd:PRK11160 554 QGTHQELLAQQ--GRYYQLKQR 573
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
398-610 |
2.11e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 168.84 E-value: 2.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:COG4619 1 LELEGLSFRVGGK---PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFADTILENIL----MGKENATKKEAIDACIAVNahnficdLPQGY-DTQVGEkgtqLSGGQKQRIALARAMI 552
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPfpfqLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 553 KDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAH------RLATvknaeTIIVLEQG 610
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHdpeqieRVAD-----RVLTLEAG 207
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
398-625 |
8.16e-47 |
|
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: 167.89 E-value: 8.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPV--LFADTILENILMGKEN-----ATKKEAIDACIAvnahnficdlpqgydtQVG-----EKGT-QLSGGQKQR 544
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENlglprEEIRERVEEALE----------------LVGlehlaDRPPhELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 545 IALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIA-HRLATV-KNAETIIVLEQGSVIEIGDHNKLM 622
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVF 222
|
...
gi 1770234124 623 AQE 625
Cdd:COG1122 223 SDY 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
398-621 |
9.41e-47 |
|
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: 167.74 E-value: 9.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYD-----PNKGLILLDGQDIRTLQ--VK 470
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDvdVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 471 WLRSQMGMVGQEPVLFADTILENILMGK---------------ENATKKEAIDACIAVNAHnficdlpqgydtqvgekGT 535
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLrlhgiklkeeldervEEALRKAALWDEVKDRLH-----------------AL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 536 QLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKN-AETIIVLEQGSVIE 614
Cdd:cd03260 141 GLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVE 220
|
....*..
gi 1770234124 615 IGDHNKL 621
Cdd:cd03260 221 FGPTEQI 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
398-612 |
4.37e-46 |
|
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: 163.54 E-value: 4.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFADTILENILmgkenatkkeaidaciavnahnficdlpqgydtqvgekgtqlSGGQKQRIALARAMIKDPKI 557
Cdd:cd03246 80 YLPQDDELFSGSIAENIL------------------------------------------SGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 558 LLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLATVKNAETIIVLEQGSV 612
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
398-616 |
6.92e-46 |
|
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: 163.25 E-value: 6.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSvPILNSLNLVI-PSQRIsALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQvKWLRSQM 476
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELkQGEKI-ALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQEPVLFADTILENIlmgkenatkkeaidaciavnahnficdlpqgydtqvgekGTQLSGGQKQRIALARAMIKDPK 556
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 557 ILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIG 616
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
980-1230 |
7.51e-46 |
|
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: 174.47 E-value: 7.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 980 ILVLSTFSVgqFAGLAPdTSMASTAIPAVFEIMNR-NPLIDGKGKKIEQSKP---------FDLEFKMVNFAYPsrPDVI 1049
Cdd:TIGR02868 275 VLVLLPLAA--FEAFAA-LPAAAQQLTRVRAAAERiVEVLDAAGPVAEGSAPaagavglgkPTLELRDLSAGYP--GAPP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENI 1129
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1130 RFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKH 1209
Cdd:TIGR02868 430 RLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
250 260
....*....|....*....|.
gi 1770234124 1210 VQDAIRKIIKRTTTIVVVHRL 1230
Cdd:TIGR02868 510 LLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
399-610 |
2.14e-45 |
|
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: 163.02 E-value: 2.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 399 ELKNVSFAYPSRmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGM 478
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 479 VGQEP--VLFADTILENILMGKENA------TKKEAIDACIAVNAHNFICDLPQgydtqvgekgtQLSGGQKQRIALARA 550
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLglpeeeIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 551 MIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIA-HRLATVKN-AETIIVLEQG 610
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDG 210
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
999-1257 |
6.00e-45 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 172.98 E-value: 6.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 999 SMASTAIPA---VFEIMNRNPLIDGKGKKIEQSKPFDLEfkMVNFAYpsRPDVIVLREFCLKVKGGTMVAVVGGSGSGKS 1075
Cdd:PRK10790 306 SMLQQAVVAgerVFELMDGPRQQYGNDDRPLQSGRIDID--NVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKS 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1076 TVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNpNASWSEVEEAAKEAYIHNFIC 1155
Cdd:PRK10790 382 TLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELAR 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1156 GLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKK 1235
Cdd:PRK10790 461 SLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVE 540
|
250 260
....*....|....*....|..
gi 1770234124 1236 ANAIAVVQNGKVSEYGTHDTLL 1257
Cdd:PRK10790 541 ADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
713-991 |
9.34e-45 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 163.58 E-value: 9.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 713 LCVGVIFGMLAGAILSLFPLVLGQALTVYFnPDKSKLQKDVGYLCLALVGLGFGCILTMMGQQGFCGWAGTKLTKRVRDL 792
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLL-PDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 793 LFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTP-FTLG 871
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPlYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 872 ASYFSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMYS 951
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1770234124 952 AYTLVLFFGAYLVKKDYTKFGDvykIFLILVLSTFSVGQF 991
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGD---LVAFLSLFAQLFGPL 274
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
395-616 |
4.50e-44 |
|
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: 159.11 E-value: 4.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 395 HGRLELKNVSFAYPSRMSvPILNSLNL-VIPSQRIsALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLR 473
Cdd:cd03369 4 HGEIEVENLSVRYAPDLP-PVLKNVSFkVKAGEKI-GIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 474 SQMGMVGQEPVLFADTILENilMGKENATKKEAIDACIavnahnficdlpqgydtQVGEKGTQLSGGQKQRIALARAMIK 553
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSN--LDPFDEYSDEEIYGAL-----------------RVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 554 DPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIG 616
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1033-1256 |
6.65e-43 |
|
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: 156.57 E-value: 6.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPsrpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYD-----PIGGKVMMGGRDLRDLDLK-- 1105
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1106 WLRLQTALVGQEPALFGGTIGENIRFG------NPNASWSE-VEEAAKEAyihnficGLPRgyetEVGE--SGIQLSGGQ 1176
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDErVEEALRKA-------ALWD----EVKDrlHALGLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1177 KQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDT 1255
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 1770234124 1256 L 1256
Cdd:cd03260 227 I 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
398-633 |
1.16e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 156.38 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWlRSQMG 477
Cdd:COG1131 1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENI-----LMGKENATKKEAIDACIAvnahnfICDLPQGYDTQVGekgtQLSGGQKQRIALARAM 551
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIDELLE------LFGLTDAADRKVG----TLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 552 IKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIA-HRLATV-KNAETIIVLEQGSVIEIGDHNKLMAQ--EGA 627
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARllEDV 226
|
....*.
gi 1770234124 628 YFSLIK 633
Cdd:COG1131 227 FLELTG 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
397-617 |
1.86e-42 |
|
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: 156.36 E-value: 1.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQM 476
Cdd:COG1120 1 MLEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQEPVL-FADTILENILMG---------KENATKKEAIDACIA-VNAHNFIcdlpqgyDTQVgekgTQLSGGQKQRI 545
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGryphlglfgRPSAEDREAVEEALErTGLEHLA-------DRPV----DELSGGERQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 546 ALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAH--RLAtVKNAETIIVLEQGSVIEIGD 617
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHdlNLA-ARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
72-371 |
6.32e-42 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 156.18 E-value: 6.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 72 LFLIIIGCLGALInggsqpwYSYLFGNFVNKIALDNDKDqmikDVRELCVLMSALSGIVVIGAYLQIACWRLVGERLGHR 151
Cdd:cd18557 2 LLFLLISSAAQLL-------LPYLIGRLIDTIIKGGDLD----VLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 152 IRSKYLRAVLRQDVSFFDTDiSTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLT 231
Cdd:cd18557 71 LRRDLFSSLLRQEIAFFDKH-KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 232 MFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLV 311
Cdd:cd18557 150 LIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 312 TYSTWALAFWYGSILVSRNELSGGAAIA---CFFGVTIGGRGLalsLSYFAQFAQGTVAASKV 371
Cdd:cd18557 230 IYLSLLLVLWYGGYLVLSGQLTVGELTSfilYTIMVASSVGGL---SSLLADIMKALGASERV 289
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1050-1258 |
8.33e-42 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 162.52 E-value: 8.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENI 1129
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1130 -RFGNpNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEK 1208
Cdd:TIGR01842 413 aRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQ 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1209 HVQDAIRKIIKR-TTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLT 1258
Cdd:TIGR01842 492 ALANAIKALKARgITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| Longin |
cd14824 |
longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including ... |
1341-1463 |
1.00e-41 |
|
longin domain; Longin-domain is N-terminal domain of a subgroup of R-SNARE proteins, including VAMP7, Ykt6, and Sec22. Longin is one of the approximately 26 components required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus. It is necessary for the steps of the transfer from the ER to the Golgi complex. Longins are the only R-SNAREs that are common to all eukaryotes, and they are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain.
Pssm-ID: 341428 Cd Length: 122 Bit Score: 149.33 E-value: 1.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1341 TMIARVTDGLPLAEGLDDGRDMQDAEFYKQQVKALFKNLSRgqnEASRMSVETGPYVFHYIIEGRVCYLTMCDRAYPKKL 1420
Cdd:cd14824 3 ALIARGSDGLILAEYTDLSSFSSVKENFKFVAKTILERTPP---SGQRQSVEEGDYVFHYLVEDGLCYLCITDKEYPKRV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1770234124 1421 AFQYLEDLKNEFERGYGNQIETAARPYAFIKFDTFIQKTKKLY 1463
Cdd:cd14824 80 AFAFLEEVLDEFLSKYGSSAWTAARPYLFSEFDPELKKLMKKY 122
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
398-635 |
2.41e-41 |
|
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: 152.70 E-value: 2.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTlQVKWLRSQMG 477
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENILM-GKENATKKEAIDACIAVNAHNFicDLPQGYDTQVGEkgtqLSGGQKQRIALARAMIKDP 555
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYfAELYGLFDEELKKRIEELIELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 556 KILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIA-HRLATVKN-AETIIVLEQGSVIEIGDHNKLMAQEG------A 627
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGeenledA 231
|
....*...
gi 1770234124 628 YFSLIKLA 635
Cdd:COG4555 232 FVALIGSE 239
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
398-616 |
7.39e-41 |
|
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: 151.12 E-value: 7.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWL---RS 474
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFAD-TILENI-LMGKENATKKEAIdaciavnahnfICDLPQGYDTQVGEKGT------QLSGGQKQRIA 546
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVaFPLREHTRLSEEE-----------IREIVLEKLEAVGLRGAedlypaELSGGMKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 547 LARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATV-KNAETIIVLEQGSVIEIG 616
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEG 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
398-616 |
7.65e-41 |
|
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: 150.73 E-value: 7.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSR-MSVPILNSLNLVIPSQRISALVGASGAGKSTI-FALLeRFYDPNKGLILLDGQDIRTL---QVKWL 472
Cdd:cd03257 2 LEVKNLSVSFPTGgGSVKALDDVSFSIKKGETLGLVGESGSGKSTLaRAIL-GLLKPTSGSIIFDGKDLLKLsrrLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 473 RSQMGMVGQE------PVLFADTILENILMGKENATKKEAIDACIAVNAHNFicDLPqgyDTQVGEKGTQLSGGQKQRIA 546
Cdd:cd03257 81 RKEIQMVFQDpmsslnPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGV--GLP---EEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 547 LARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIG 616
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
398-611 |
8.91e-41 |
|
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: 149.54 E-value: 8.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSR--MSVPILNSLNLVIPSQRISALVGASGAGKST-IFALL-ErfYDPNKGLIlldgqdirtlqvkWLR 473
Cdd:cd03250 1 ISVEDASFTWDSGeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSlLSALLgE--LEKLSGSV-------------SVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 474 SQMGMVGQEPVLFADTILENILMGKE-NATK-KEAIDAC-----IAVnahnficdLPQGYDTQVGEKGTQLSGGQKQRIA 546
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFGKPfDEERyEKVIKACalepdLEI--------LPDGDLTEIGEKGINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 547 LARAMIKDPKILLLDEPTSALDPK-SESLVQQAI-DKISKGRTTIVIAHRLATVKNAETIIVLEQGS 611
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
398-617 |
1.59e-40 |
|
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: 150.13 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL---QVKWLRS 474
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFAD-TILENILMG-KEN-----ATKKEAIDACIAvnahnficdlpqgydtQVGEKGT------QLSGGQ 541
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlREHtdlseAEIRELVLEKLE----------------LVGLPGAadkmpsELSGGM 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 542 KQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGD 617
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGT 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
398-614 |
3.83e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 148.65 E-value: 3.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPS-RMSVPILNSLNLVIPSQRISALVGASGAGKST---IFALLERfydPNKGLILLDGQDIRTL----QV 469
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLsereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 470 KWLRSQMGMVGQEPVLFAD-TILENILMG------KENATKKEAIDACIAVN----AHNFIcdlpqgydtqvgekgTQLS 538
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVALPlllagvSRKERRERARELLERVGlgdrLDHRP---------------SQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 539 GGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKNAETIIVLEQGSVIE 614
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1033-1228 |
4.72e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 147.66 E-value: 4.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGGTIGENIRFGNPNASWSEVEEAAKEAyIHNFicGLPRGY-ETEVGEsgiqLSGGQKQRIAIARAIVKKSK 1191
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFPFQLRERKFDRERALEL-LERL--GLPPDIlDKPVER----LSGGERQRLALIRALLLQPD 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1770234124 1192 VLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVH 1228
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSH 189
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1033-1246 |
5.69e-40 |
|
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: 147.23 E-value: 5.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPDVI--VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRdlrdldlkwlrlq 1110
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1111 TALVGQEPALFGGTIGENIRFGNP-NASW-SEVEEAakeayihnfiCGL-------PRGYETEVGESGIQLSGGQKQRIA 1181
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfDEERyEKVIKA----------CALepdleilPDGDLTEIGEKGINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1182 IARAIVKKSKVLLLDEATSALDLESEKHV-QDAIRKIIKRTTTIVVV-HRLSTIKKANAIAVVQNGK 1246
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLLLNNKTRILVtHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
398-616 |
1.04e-39 |
|
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: 146.90 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwlRSQMG 477
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENILMG-KENATKKEAIDAciavNAHNFICDLpqGYDTQVGEKGTQLSGGQKQRIALARAMIKDP 555
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlKLRGVPKAEIRA----RVRELLELV--GLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 556 KILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLA-TVKNAETIIVLEQGSVIEIG 616
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
362-624 |
1.31e-39 |
|
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: 155.45 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 362 AQGTVAAskVFAIIDRIPAIDPYSTTGRKPETVHGR----LELKNVSFAYPSRMS--VPILNSLNLVIPSQRISALVGAS 435
Cdd:COG1123 223 EDGPPEE--ILAAPQALAAVPRLGAARGRAAPAAAAaeplLEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGES 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 436 GAGKSTIFALLERFYDPNKGLILLDGQDIRTL---QVKWLRSQMGMVGQEPV--LFA-DTILENI--------LMGKENA 501
Cdd:COG1123 301 GSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRELRRRVQMVFQDPYssLNPrMTVGDIIaeplrlhgLLSRAER 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 502 TKK--EAIDACiavnahnficdlpqGYDTQVGEK-GTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQA 578
Cdd:COG1123 381 RERvaELLERV--------------GLPPDLADRyPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNL 446
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1770234124 579 IDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGDHNKLMAQ 624
Cdd:COG1123 447 LRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
398-652 |
2.55e-39 |
|
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: 154.68 E-value: 2.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPN---KGLILLDGQDIRTLQVKWLRS 474
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEP--VLFADTILENILMGKEN--ATKKEAIDACIAVNAHNFICDLPQGYDTQvgekgtqLSGGQKQRIALARA 550
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALENlgLSRAEARARVLELLEAVGLERRLDRYPHQ-------LSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 551 MIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGDHNKLMAQEGA 627
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
250 260
....*....|....*....|....*
gi 1770234124 628 YFSLIKLATEAISSNPVSKKGKTVI 652
Cdd:COG1123 237 LAAVPRLGAARGRAAPAAAAAEPLL 261
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
399-610 |
2.85e-39 |
|
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: 143.54 E-value: 2.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 399 ELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGM 478
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 479 VGQepvlfadtilenilmgkenatkkeaidaciavnahnficdlpqgydtqvgekgtqLSGGQKQRIALARAMIKDPKIL 558
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 559 LLDEPTSALDPKSESLVQQAIDKIS-KGRTTIVIAHRLATVKNA-ETIIVLEQG 610
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
416-565 |
5.10e-39 |
|
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: 142.40 E-value: 5.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 416 LNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFAD-TILENI 494
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 495 LMGKEN-ATKKEAIDACIAVNAHNFicDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTS 565
Cdd:pfam00005 81 RLGLLLkGLSKREKDARAEEALEKL--GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
398-610 |
5.25e-39 |
|
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: 143.48 E-value: 5.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL--QVKWLRSQ 475
Cdd:cd03229 1 LELKNVSKRYGQ---KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MGMVGQEPVLFAD-TILENILMGkenatkkeaidaciavnahnficdlpqgydtqvgekgtqLSGGQKQRIALARAMIKD 554
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 555 PKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQG 610
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1030-1252 |
6.64e-39 |
|
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: 144.48 E-value: 6.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1030 PFDLEFKMVNFAYPSRPDVI-VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLR 1108
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1109 LQTALVGQEPALFGGTIGENIrfgNPNASWSEVE--EAAKeayihnficglprgyeteVGESGIQLSGGQKQRIAIARAI 1186
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEiyGALR------------------VSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1187 VKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGT 1252
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1033-1260 |
7.11e-39 |
|
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: 145.17 E-value: 7.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPsrPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPA--LFGGTIGENIRFG--NPNASWSEVEEAAKEAyihnficgLprgyeTEVGESGI------QLSGGQKQRIAI 1182
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpeNLGLPREEIRERVEEA--------L-----ELVGLEHLadrpphELSGGQKQRVAI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1183 ARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTI-KKANAIAVVQNGKVSEYGTHDTLLTNH 1260
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1034-1246 |
9.31e-39 |
|
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: 144.15 E-value: 9.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1034 EFKMVNFAYPSRpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTAL 1113
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1114 VGQEPA--LFGGTIGENIRFGNPNASWS--EVEEAAKEAyihnficglprgyETEVGESGI------QLSGGQKQRIAIA 1183
Cdd:cd03225 80 VFQNPDdqFFGPTVEEEVAFGLENLGLPeeEIEERVEEA-------------LELVGLEGLrdrspfTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1184 RAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGK 1246
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
398-617 |
1.10e-38 |
|
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: 144.65 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSR-MSVPILNSLNLVIPSQRISALVGASGAGKST---IFALLERfydPNKGLILLDGQDIRTLQVKWL- 472
Cdd:cd03258 2 IELKNVSKVFGDTgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER---PTSGSVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 473 --RSQMGMVGQEPVLFAD-TILENI-----LMGKENATKKEAIDACIA-VNAHNFICDLPqgydtqvgekgTQLSGGQKQ 543
Cdd:cd03258 79 kaRRRIGMIFQHFNLLSSrTVFENValpleIAGVPKAEIEERVLELLElVGLEDKADAYP-----------AQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 544 RIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGD 617
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
398-613 |
1.36e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 144.81 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL---QVKWLRS 474
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFAD-TILENILMGKENAT----------KKEAIDACIAVnahnficdLpqgydTQVG------EKGTQL 537
Cdd:COG3638 81 RIGMIFQQFNLVPRlSVLTNVLAGRLGRTstwrsllglfPPEDRERALEA--------L-----ERVGladkayQRADQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 538 SGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVI 613
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
399-616 |
1.68e-38 |
|
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: 142.19 E-value: 1.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 399 ELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGM 478
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 479 VGQepvlfadtilenilmgkenatkkeaidACIAVNAHNFicdLPQGYDTqvgekgtqLSGGQKQRIALARAMIKDPKIL 558
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHL---ADRPFNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 559 LLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLA-TVKNAETIIVLEQGSVIEIG 616
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
398-613 |
1.96e-38 |
|
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: 144.25 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWL---RS 474
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFAD-TILENILMGKenatkkeaidaciaVNAHNFICDLPQGYD-----------TQVG------EKGTQ 536
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENVLSGR--------------LGRRSTWRSLFGLFPkeekqralaalERVGlldkayQRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 537 LSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAHR--LATvKNAETIIVLEQGSV 612
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQvdLAR-EYADRIVGLKDGRI 223
|
.
gi 1770234124 613 I 613
Cdd:cd03256 224 V 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1033-1247 |
3.89e-38 |
|
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: 140.81 E-value: 3.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYP--SRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQ 1110
Cdd:cd03246 1 LEVENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1111 TALVGQEPALFGGTIGENIrfgnpnaswseveeaakeayihnficglprgyetevgesgiqLSGGQKQRIAIARAIVKKS 1190
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1191 KVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKKANAIAVVQNGKV 1247
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIaHRPETLASADRILVLEDGRV 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
398-614 |
9.14e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.73 E-value: 9.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPsrMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL---QVKWLRS 474
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFAD-TILENI-----LMGKENATKKEAIDACIAvnahnficdlpqgydtQVG--EKG----TQLSGGQK 542
Cdd:COG2884 80 RIGVVFQDFRLLPDrTVYENValplrVTGKSRKEIRRRVREVLD----------------LVGlsDKAkalpHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 543 QRIALARAMIKDPKILLLDEPTSALDPK-SESLVqQAIDKISKGRTTIVIA-HRLATVKNAET-IIVLEQGSVIE 614
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
398-623 |
9.47e-38 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 142.63 E-value: 9.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRM-SVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQM 476
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQEP---------VlfADTILENILMGKENATKKEAIDACIAVnahnficDLPQGYDTQVGEkgtQLSGGQKQRIAL 547
Cdd:COG1124 82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLEQV-------GLPPSFLDRYPH---QLSGGQRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 548 ARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGDHNKLMA 623
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
398-610 |
1.00e-37 |
|
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: 141.47 E-value: 1.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPS-RMSVPILNSLNLVIPSQRISALVGASGAGKST---IFALLERfydPNKGLILLDGQDIRTL----QV 469
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLsekeLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 470 KWLRSQMGMVGQEPVLFAD-TILENILM-----GKENATKKE-AIDACIAVnahnficDLPQGYDTQVGekgtQLSGGQK 542
Cdd:cd03255 78 AFRRRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRErAEELLERV-------GLGDRLNHYPS----ELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 543 QRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKNAETIIVLEQG 610
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
398-623 |
1.31e-37 |
|
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: 142.05 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENI-----LMGKENATKKEAIDACIAvnahnfICDL-PQGYdtqVGEKGTQLSGGQKQRIALARA 550
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIalvpkLLKWPKEKIRERADELLA------LVGLdPAEF---ADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 551 MIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRL-ATVKNAETIIVLEQGSVIEIGDHNKLMA 623
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
415-1275 |
1.39e-37 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 154.94 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 415 ILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLIlldgqdirtlqvkWLRSQMGMVGQEPVLFADTILENI 494
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 495 LM-GKENATKKEAIDACIAVNAHnfICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPK-SE 572
Cdd:PTZ00243 742 LFfDEEDAARLADAVRVSQLEAD--LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGE 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 573 SLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQegayfSLIK-LATEAISSNPVSKKGKTV 651
Cdd:PTZ00243 820 RVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT-----SLYAtLAAELKENKDSKEGDADA 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 652 INQETSSNCDLLKQNHVYEISPSGYMKSIQDAN-QPESAKLNKIKSYKIREV-WKLQKPEAGLlCVGvifGMLAGAILSL 729
Cdd:PTZ00243 895 EVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAAlDAAAGRLMTREEKASGSVpWSTYVAYLRF-CGG---LHAAGFVLAT 970
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 730 FplVLGQALTVYFN-------PDKSKLQKDVG---YLCLALVGlGFGCILTMMgqqgFCGWAGTKLTKRVRDLLFRSILN 799
Cdd:PTZ00243 971 F--AVTELVTVSSGvwlsmwsTRSFKLSAATYlyvYLGIVLLG-TFSVPLRFF----LSYEAMRRGSRNMHRDLLRSVSR 1043
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 800 QEPGWFDSdqnSP-GSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEwRLALLATIVTPFTlgasYFSLI 878
Cdd:PTZ00243 1044 GTMSFFDT---TPlGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQ-PFVLVALVPCGYL----YYRLM 1115
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 879 INIGSKldNDSFDKASGIASA--------AVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSqITGIALGISQGAMY 950
Cdd:PTZ00243 1116 QFYNSA--NREIRRIKSVAKSpvftlleeALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLEN-VANRWLGVRVEFLS 1192
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 951 SAYTLVLFFGAYLVKKDYTKFGDVYKIFLILVLSTFSVGQFAGLAPDTSMASTAIPAVFEIM------------NRNPLI 1018
Cdd:PTZ00243 1193 NIVVTVIALIGVIGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLyytdevphedmpELDEEV 1272
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1019 DGKGKK------------IEQSKPF----------DLEFKMVNFAYpsRPDV-IVLREFCLKVKGGTMVAVVGGSGSGKS 1075
Cdd:PTZ00243 1273 DALERRtgmaadvtgtvvIEPASPTsaaphpvqagSLVFEGVQMRY--REGLpLVLRGVSFRIAPREKVGIVGRTGSGKS 1350
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1076 TVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIrfgNP--NASWSEVEEAAKEAYIHNF 1153
Cdd:PTZ00243 1351 TLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRER 1427
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1154 ICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKK-SKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLST 1232
Cdd:PTZ00243 1428 VASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHT 1507
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1770234124 1233 IKKANAIAVVQNGKVSEYGTHDTLLTNHSngvyaTLVHSEMEA 1275
Cdd:PTZ00243 1508 VAQYDKIIVMDHGAVAEMGSPRELVMNRQ-----SIFHSMVEA 1545
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1047-1251 |
2.55e-37 |
|
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: 139.96 E-value: 2.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwlRLQTALVGQEPALFGG-TI 1125
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPHlTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1126 GENIRFGNPNASWSE------VEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLLLDEAT 1199
Cdd:cd03259 90 AENIAFGLKLRGVPKaeirarVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1200 SALDLESEKHVQDAIRKIIKRT--TTIVVVHRLS-TIKKANAIAVVQNGKVSEYG 1251
Cdd:cd03259 159 SALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
398-615 |
2.85e-37 |
|
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: 140.30 E-value: 2.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSR-MSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLqvkwlRSQM 476
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQEPVLFA-DTILENILMGKE-----NATKKEAIDACIAvnahnficdlpqgydtQVGEKGT------QLSGGQKQR 544
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElqgvpKAEARERAEELLE----------------LVGLSGFenayphQLSGGMRQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 545 IALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLA-TVKNAETIIVLEQ--GSVIEI 615
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
397-621 |
3.76e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 141.33 E-value: 3.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYD--PN---KGLILLDGQDI--RTLQV 469
Cdd:COG1117 11 KIEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 470 KWLRSQMGMVGQEPVLFADTILENILMG-KENATK-KEAIDAcIAVNAhnficdLpqgydTQVG----------EKGTQL 537
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDNVAYGlRLHGIKsKSELDE-IVEES------L-----RKAAlwdevkdrlkKSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 538 SGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKIsKGRTTIVI-------AHRLatvknAETIIVLEQG 610
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVIvthnmqqAARV-----SDYTAFFYLG 229
|
250
....*....|.
gi 1770234124 611 SVIEIGDHNKL 621
Cdd:COG1117 230 ELVEFGPTEQI 240
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
398-612 |
1.62e-36 |
|
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: 136.37 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwLRSQMG 477
Cdd:cd03230 1 IEVRNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENIlmgkenatkkeaidaciavnahnficdlpqgydtqvgekgtQLSGGQKQRIALARAMIKDPK 556
Cdd:cd03230 77 YLPEEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 557 ILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIA-HRLATVKN-AETIIVLEQGSV 612
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
398-617 |
1.73e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 138.59 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTI---FALLERfydPNKGLILLDGQDI--RTLQVKWL 472
Cdd:COG1126 2 IEIENLHKSFGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 473 RSQMGMVGQEPVLFAD-TILENILMG-----KENatKKEAIDacIAVNAhnficdLpqgydTQVG--EKG----TQLSGG 540
Cdd:COG1126 76 RRKVGMVFQQFNLFPHlTVLENVTLApikvkKMS--KAEAEE--RAMEL------L-----ERVGlaDKAdaypAQLSGG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 541 QKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGD 617
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKeGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
398-616 |
1.83e-36 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 139.89 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYP--SRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQ---VKWL 472
Cdd:TIGR04521 1 IKLKNVSYIYQpgTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKkkkLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 473 RSQMGMVGQEP--VLFADTILENILMGKEN--ATKKE----AIDACIAVnahnficdlpqGYDTQVGEKGT-QLSGGQKQ 543
Cdd:TIGR04521 81 RKKVGLVFQFPehQLFEETVYKDIAFGPKNlgLSEEEaeerVKEALELV-----------GLDEEYLERSPfELSGGQMR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 544 RIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAHRLATV-KNAETIIVLEQGSVIEIG 616
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhkEKGLTVILVTHSMEDVaEYADRVIVMHKGKIVLDG 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
151-630 |
5.36e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 149.89 E-value: 5.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 151 RIRSKYLRAVLRQDVSFFDTDiSTSDIMHGISSDVAQIQEVMGDKMSQFIYHIF----TFICGYIVGFLKSWkvslavlA 226
Cdd:PLN03130 987 RLHDAMLGSILRAPMSFFHTN-PLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFqllsTFVLIGIVSTISLW-------A 1058
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 227 VTPLTMFCGVAYkaVYVGLAAKEVnsyKKAGSIAE--------QAIGSIRTVFSFVAEDSLAARYDAVLDESVP------ 292
Cdd:PLN03130 1059 IMPLLVLFYGAY--LYYQSTAREV---KRLDSITRspvyaqfgEALNGLSTIRAYKAYDRMAEINGRSMDNNIRftlvnm 1133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 293 -----IGKKLGFAKGIglgVIYLVtystwalafwyGSILVSRNelsGGAAIACFFGVTIGgrglaLSLSY---------- 357
Cdd:PLN03130 1134 ssnrwLAIRLETLGGL---MIWLT-----------ASFAVMQN---GRAENQAAFASTMG-----LLLSYalnitsllta 1191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 358 ---FAQFAQGTV-AASKVFAIIDrIPAIDPYSTTGRKPET---VHGRLELKNVSFAYPSRMSvPILNSLNLVI-PSQRIs 429
Cdd:PLN03130 1192 vlrLASLAENSLnAVERVGTYID-LPSEAPLVIENNRPPPgwpSSGSIKFEDVVLRYRPELP-PVLHGLSFEIsPSEKV- 1268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 430 ALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKE--NATKKEAI 507
Cdd:PLN03130 1269 GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEhnDADLWESL 1348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 508 DaciavNAH--NFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKG 585
Cdd:PLN03130 1349 E-----RAHlkDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKS 1423
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1770234124 586 RTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFS 630
Cdd:PLN03130 1424 CTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1033-1260 |
8.74e-36 |
|
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: 143.89 E-value: 8.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDP---IGGKVMMGGRDLRDLDLKWLRL 1109
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 QTALVGQEP--ALFGGTIGENIRFG--NPNASWSEVEEAAKEAyihnficgLPR-GYETEVGESGIQLSGGQKQRIAIAR 1184
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLEL--------LEAvGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 1185 AIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTI-KKANAIAVVQNGKVSEYGTHDTLLTNH 1260
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
126-635 |
1.30e-35 |
|
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: 148.56 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 126 LSGIVVIGAYLQIACWRLVGERLGHRirsKYLRAVLRQDVSFFDTDIStSDIMHGISSDVAQIQEVMGDKMSQFIYHIFT 205
Cdd:TIGR00957 1017 LQGFAVFGYSMAVSIGGIQASRVLHQ---DLLHNKLRSPMSFFERTPS-GNLVNRFSKELDTVDSMIPPVIKMFMGSLFN 1092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 206 FICGYIVGFLKSwkvSLAVLAVTPLtmfcGVAYKAVYVGLAAKEvNSYKKAGSIAEQAigsirtVFSFVAEDSLAA---- 281
Cdd:TIGR00957 1093 VIGALIVILLAT---PIAAVIIPPL----GLLYFFVQRFYVASS-RQLKRLESVSRSP------VYSHFNETLLGVsvir 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 282 ------RYDAVLDESVPIGKKLGFAkgiglgviYLVTySTWalafwygsiLVSRNELSGGAAI--ACFFGVtIGGRGLA- 352
Cdd:TIGR00957 1159 afeeqeRFIHQSDLKVDENQKAYYP--------SIVA-NRW---------LAVRLECVGNCIVlfAALFAV-ISRHSLSa 1219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 353 ----LSLSYFAQFAQG----TVAASKVFAIIDRIPAIDPYSTT----------GRKPET--VHGRLELKNVSFAYPSRMS 412
Cdd:TIGR00957 1220 glvgLSVSYSLQVTFYlnwlVRMSSEMETNIVAVERLKEYSETekeapwqiqeTAPPSGwpPRGRVEFRNYCLRYREDLD 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 413 VpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILE 492
Cdd:TIGR00957 1300 L-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRM 1378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 493 NiLMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSE 572
Cdd:TIGR00957 1379 N-LDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 573 SLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSLIKLA 635
Cdd:TIGR00957 1458 NLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDA 1520
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
78-371 |
2.19e-35 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 137.38 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 78 GCLGALINGGSQPWYSYLFGNFVNkIALDNDKDQMIKDVRELCVLMSALSGIVVIGA---YLQIACWRLVGERLGHRIRS 154
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVID-AVTNHSGSGGEEALRALNQAVLILLGVVLIGSiatFLRSWLFTLAGERVVARLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 155 KYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFC 234
Cdd:cd18780 80 RLFSAIIAQEIAFFDV-TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 235 GVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYS 314
Cdd:cd18780 159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 315 TWALAFWYGSILVSRNELSGGAAIAcFFGVTIG-GRGLALSLSYFAQFAQGTVAASKV 371
Cdd:cd18780 239 AIVLVLWYGGRLVIDGELTTGLLTS-FLLYTLTvAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1033-1259 |
2.36e-35 |
|
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: 142.73 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRP--DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDL---DLKWL 1107
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1108 RLQTALVGQEP--ALF-GGTIGENIRFG---NPNASWSEVEEAAKEAyIHnfICGLPRGYEtevGESGIQLSGGQKQRIA 1181
Cdd:COG1123 341 RRRVQMVFQDPysSLNpRMTVGDIIAEPlrlHGLLSRAERRERVAEL-LE--RVGLPPDLA---DRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1182 IARAIVKKSKVLLLDEATSALDLesekHVQDAIRKIIKR------TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHD 1254
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDV----SVQAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
|
....*
gi 1770234124 1255 TLLTN 1259
Cdd:COG1123 491 EVFAN 495
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
398-625 |
3.31e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 134.50 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPS-RMSvpilnsLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVkwlrSQ- 475
Cdd:COG3840 2 LRLDDLTYRYGDfPLR------FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AEr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 -MGMVGQEPVLFAD-TILENILMG-----KENATKKEAIDACIA-VNAHNFICDLPQgydtqvgekgtQLSGGQKQRIAL 547
Cdd:COG3840 72 pVSMLFQENNLFPHlTVAQNIGLGlrpglKLTAEQRAQVEQALErVGLAGLLDRLPG-----------QLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 548 ARAMIKDPKILLLDEPTSALDP--KSE--SLVQQAIDkiSKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGDHNKLM 622
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPalRQEmlDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
...
gi 1770234124 623 AQE 625
Cdd:COG3840 219 DGE 221
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
398-613 |
3.49e-35 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 135.12 E-value: 3.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRS--- 474
Cdd:TIGR02315 2 LEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFAD-TILENILMGKENAT--------------KKEAIDACIAVnahnficdlpqGYDTQVGEKGTQLSG 539
Cdd:TIGR02315 80 RIGMIFQHYNLIERlTVLENVLHGRLGYKptwrsllgrfseedKERALSALERV-----------GLADKAYQRADQLSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 540 GQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVI 613
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKedGITVIINLHQVDLAKKyADRIVGLKAGEIV 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
151-630 |
4.29e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 147.04 E-value: 4.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 151 RIRSKYLRAVLRQDVSFFDTDiSTSDIMHGISSDVAQIQEVMGDKMSQFIYHIF----TFICGYIVGFLKSWkvslavlA 226
Cdd:PLN03232 984 RLHDAMLNSILRAPMLFFHTN-PTGRVINRFSKDIGDIDRNVANLMNMFMNQLWqllsTFALIGTVSTISLW-------A 1055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 227 VTPLTMFCGVAYkaVYVGLAAKEV---NSYKKAGSIAE--QAIGSIRTVFSFVAEDSLAARYDAVLDESVPIgkKLGFAK 301
Cdd:PLN03232 1056 IMPLLILFYAAY--LYYQSTSREVrrlDSVTRSPIYAQfgEALNGLSSIRAYKAYDRMAKINGKSMDNNIRF--TLANTS 1131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 302 GIGLGVIYLVTYStwALAFWY-GSILVSRNelsGGAAIACFFGVTIGgrglaLSLSYF-------------AQFAQGTV- 366
Cdd:PLN03232 1132 SNRWLTIRLETLG--GVMIWLtATFAVLRN---GNAENQAGFASTMG-----LLLSYTlnittllsgvlrqASKAENSLn 1201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 367 AASKVFAIIDrIPAIDPYSTTGRKPET---VHGRLELKNVSFAYPSRMSvPILNSLNL-VIPSQRIsALVGASGAGKSTI 442
Cdd:PLN03232 1202 SVERVGNYID-LPSEATAIIENNRPVSgwpSRGSIKFEDVHLRYRPGLP-PVLHGLSFfVSPSEKV-GVVGRTGAGKSSM 1278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 443 FALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKE--NATKKEAIDaciavNAH--NF 518
Cdd:PLN03232 1279 LNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEhnDADLWEALE-----RAHikDV 1353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 519 ICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATV 598
Cdd:PLN03232 1354 IDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTI 1433
|
490 500 510
....*....|....*....|....*....|..
gi 1770234124 599 KNAETIIVLEQGSVIEIGDHNKLMAQEGAYFS 630
Cdd:PLN03232 1434 IDCDKILVLSSGQVLEYDSPQELLSRDTSAFF 1465
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1056-1200 |
5.62e-35 |
|
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: 130.85 E-value: 5.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGG-TIGENIRFGNP 1134
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLRLGLL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1135 NASWSEVEEAAK-EAYIHNFicGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATS 1200
Cdd:pfam00005 86 LKGLSKREKDARaEEALEKL--GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
398-625 |
6.06e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.45 E-value: 6.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLqvkwlRSQMG 477
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD---TILENILMG---------KENATKKEAIDACIA-VNAHNFIcdlpqgyDTQVGEkgtqLSGGQKQR 544
Cdd:COG1121 79 YVPQRAEVDWDfpiTVRDVVLMGrygrrglfrRPSRADREAVDEALErVGLEDLA-------DRPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 545 IALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLATV-KNAETIIVLEQGsVIEIGDHNKLM 622
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVrEYFDRVLLLNRG-LVAHGPPEEVL 226
|
...
gi 1770234124 623 AQE 625
Cdd:COG1121 227 TPE 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
397-615 |
1.28e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 134.06 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAYPSRM-SVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLqvkwlRSQ 475
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MGMVGQEPVLFA-DTILENI-----LMGKENATKKEAIDACIAvnahnficdlpqgydtQVGEKG------TQLSGGQKQ 543
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNValgleLRGVPKAERRERARELLE----------------LVGLAGfedaypHQLSGGMRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 544 RIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAH------RLATvknaeTIIVLEQ--GSVI 613
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHdvdeavFLAD-----RVVVLSArpGRIV 220
|
..
gi 1770234124 614 EI 615
Cdd:COG1116 221 EE 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1033-1251 |
2.30e-34 |
|
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: 132.24 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPDVI-VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRL-- 1109
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 -QTALVGQEPA-----LFggTIGENIRFGNPNASWSEVEEAAKEAYIHNFI-CGLPRGYETEVGEsgiQLSGGQKQRIAI 1182
Cdd:cd03257 82 kEIQMVFQDPMsslnpRM--TIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgVGLPEEVLNRYPH---ELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1183 ARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYG 1251
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElgLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
398-616 |
2.96e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 132.94 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKW-LRSQM 476
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQEP--VLFADTILENILMGKEN-----ATKKEAIDACIA-VNAHNFICDLPQgydtqvgekgtQLSGGQKQRIALA 548
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgvprEEMRKRVDEALKlVGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 549 RAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKNAETIIVLEQGSVIEIG 616
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEG 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1035-1246 |
3.15e-34 |
|
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: 130.00 E-value: 3.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1035 FKMVNFAYpSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLD--LKWLRLQTA 1112
Cdd:cd03229 1 LELKNVSK-RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGG-TIGENIRFGnpnaswseveeaakeayihnficglprgyetevgesgiqLSGGQKQRIAIARAIVKKSK 1191
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1192 VLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGK 1246
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
398-610 |
5.23e-34 |
|
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: 130.73 E-value: 5.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTI---FALLERfydPNKGLILLDGQDI--RTLQVKWL 472
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTIIIDGLKLtdDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 473 RSQMGMVGQEPVLFAD-TILENILMGK---ENATKKEAIDACIAvnahnficdlpqgYDTQVG--EKGT----QLSGGQK 542
Cdd:cd03262 75 RQKVGMVFQQFNLFPHlTVLENITLAPikvKGMSKAEAEERALE-------------LLEKVGlaDKADaypaQLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 543 QRIALARAMIKDPKILLLDEPTSALDPKsesLVQQAIDKI----SKGRTTIVIAHRLATVKN-AETIIVLEQG 610
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLDVMkdlaEEGMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
398-616 |
6.68e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 134.50 E-value: 6.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKST---IFALLERfydPNKGLILLDGQDIRT-LQVKwlR 473
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLNGRDLFTnLPPR--E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 474 SQMGMVGQEPVLFAD-TILENILMG-KENATKKEAIDACI-----AVNAHNFICDLPqgydtqvgekgTQLSGGQKQRIA 546
Cdd:COG1118 75 RRVGFVFQHYALFPHmTVAENIAFGlRVRPPSKAEIRARVeelleLVQLEGLADRYP-----------SQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 547 LARAMIKDPKILLLDEPTSALDPKS----ESLVQQAIDKIskGRTTIVIAH------RLatvknAETIIVLEQGSVIEIG 616
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDAKVrkelRRWLRRLHDEL--GGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVG 216
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
398-617 |
7.78e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.46 E-value: 7.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVkWLRsQMG 477
Cdd:COG3842 6 LELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKR-NVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENI-----LMGKENATKKEAIDACIAVnahnficdlpqgydTQVGEKG----TQLSGGQKQRIAL 547
Cdd:COG3842 81 MVFQDYALFPHlTVAENVafglrMRGVPKAEIRARVAELLEL--------------VGLEGLAdrypHQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 548 ARAMIKDPKILLLDEPTSALDPKS-ESLvQQAIDKISK--GRTTIVIAH------RLATvknaeTIIVLEQGSVIEIGD 617
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLrEEM-REELRRLQRelGITFIYVTHdqeealALAD-----RIAVMNDGRIEQVGT 219
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
715-990 |
1.81e-33 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 132.40 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 715 VGVIFGMLAGAILSLFPLVLGQALTVYFNPDK-----------------SKLQKDVGYLCLALVGLGFGCILTMMGQQGF 777
Cdd:cd18558 3 VGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMtnitgnssglnssagpfEKLEEEMTLYAYYYLIIGAIVLITAYIQGSF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 778 CGWAGTKLTKRVRDLLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWR 857
Cdd:cd18558 83 WGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 858 LALLATIVTP-FTLGASYFSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQ 936
Cdd:cd18558 161 LTLVILAISPvLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 937 ITGIALGISQGAMYSAYTLVLFFGAYLVKKDYTKFGDVYKIFLILVLSTFSVGQ 990
Cdd:cd18558 241 TFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQ 294
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
399-617 |
1.87e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.88 E-value: 1.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 399 ELKNVSFAYPSrMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGM 478
Cdd:PRK13632 9 KVENVSFSYPN-SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 479 VGQEP--VLFADTILENILMGKEN------ATKKEAIDACIAVNAHNFICDLPQgydtqvgekgtQLSGGQKQRIALARA 550
Cdd:PRK13632 88 IFQNPdnQFIGATVEDDIAFGLENkkvppkKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 551 MIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGR--TTIVIAHRLATVKNAETIIVLEQGSVIEIGD 617
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1034-1246 |
2.53e-33 |
|
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: 126.59 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1034 EFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTAL 1113
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1114 VGQepalfggtigenirfgnpnaswseveeaakeayihnficglprgyetevgesgiqLSGGQKQRIAIARAIVKKSKVL 1193
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1194 LLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKKA-NAIAVVQNGK 1246
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVtHDPELAELAaDRVIVLKDGK 157
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
398-617 |
3.05e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 132.12 E-value: 3.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRM-SVPILNSLNLVIPSQRISALVGASGAGKST---IFALLERfydPNKGLILLDGQDIRTLQVKWL- 472
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 473 --RSQMGMVGQEPVLFAD-TILENI-----LMGkenaTKKEAIDACIA-----VN----AHNFicdlPqgydtqvgekgT 535
Cdd:COG1135 79 aaRRKIGMIFQHFNLLSSrTVAENValpleIAG----VPKAEIRKRVAellelVGlsdkADAY----P-----------S 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 536 QLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSV 612
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
....*
gi 1770234124 613 IEIGD 617
Cdd:COG1135 220 VEQGP 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
396-630 |
4.62e-33 |
|
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: 129.26 E-value: 4.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 396 GRLELKNVSFAYPSRMSvPILNSLNLVI-PSQRIsALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRS 474
Cdd:cd03288 18 GEIKIHDLCVRYENNLK-PVLKHVKAYIkPGQKV-GICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFADTILENiLMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKD 554
Cdd:cd03288 96 RLSIILQDPILFSGSIRFN-LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 555 PKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFS 630
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1033-1259 |
1.50e-32 |
|
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: 126.93 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRP-DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQT 1111
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVG---QEPALFGG-TIGENIRFGNPNASWSEVEEAAKEAYIHNFIcglprGYETEVGESGIQLSGGQKQRIAIARAIV 1187
Cdd:cd03258 82 RRIGmifQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELV-----GLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1188 KKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT-TTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRELgLTIVLItHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1032-1252 |
2.64e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.83 E-value: 2.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1032 DLEFKMVNFAYPsrpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDL-------RDldl 1104
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekRN--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1105 kwlrlqTALVGQEPALFGG-TIGENIRFG--NPNASWSEVEEAAKEA------------YIHnficglprgyetevgesg 1169
Cdd:COG3842 79 ------VGMVFQDYALFPHlTVAENVAFGlrMRGVPKAEIRARVAELlelvglegladrYPH------------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1170 iQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLS---TIkkANAIAVVQN 1244
Cdd:COG3842 135 -QLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElgITFIYVTHDQEealAL--ADRIAVMND 211
|
....*...
gi 1770234124 1245 GKVSEYGT 1252
Cdd:COG3842 212 GRIEQVGT 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1033-1251 |
2.93e-32 |
|
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: 124.35 E-value: 2.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPDViVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDlKWLRLQTA 1112
Cdd:cd03247 1 LSINNVSFSYPEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGGTIGENIrfgnpnaswseveeaakeayihnficglprgyetevgesGIQLSGGQKQRIAIARAIVKKSKV 1192
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 1193 LLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYG 1251
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
100-371 |
3.44e-32 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 127.66 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 100 VNKIALDNDKDQMIKDVRELCVLmSALSGIVvigAYLQIACWRLVGERLGHRIRSKYLRAVLRQDVSFFDTDiSTSDIMH 179
Cdd:cd18572 23 IDAVVADGSREAFYRAVLLLLLL-SVLSGLF---SGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT-KTGELTS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 180 GISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFCGVAYkAVYVGLAAKEV-NSYKKAGS 258
Cdd:cd18572 98 RLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVY-GRYYRKLSKEIqDALAEANQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 259 IAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYSTWALAFWYGSILVSRNELSGGAAI 338
Cdd:cd18572 177 VAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLV 256
|
250 260 270
....*....|....*....|....*....|...
gi 1770234124 339 ACFFGVTIGGRGLALSLSYFAQFAQGTVAASKV 371
Cdd:cd18572 257 TFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
416-613 |
3.59e-32 |
|
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: 126.01 E-value: 3.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 416 LNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwLRSQMGMVG--QEPVLFAD-TILE 492
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 493 NILMG---------------KENATKKEAIDACIAvnahnfICDLPQGYDTQVGEkgtqLSGGQKQRIALARAMIKDPKI 557
Cdd:cd03219 95 NVMVAaqartgsglllararREEREARERAEELLE------RVGLADLADRPAGE----LSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 558 LLLDEPTSALDPKsesLVQQAIDKI----SKGRTTIVIAHRLATVKN-AETIIVLEQGSVI 613
Cdd:cd03219 165 LLLDEPAAGLNPE---ETEELAELIrelrERGITVLLVEHDMDVVMSlADRVTVLDQGRVI 222
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1050-1273 |
4.30e-32 |
|
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: 126.56 E-value: 4.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENI 1129
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1130 rfgNPNASWSE--VEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESE 1207
Cdd:cd03288 116 ---DPECKCTDdrLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1208 KHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTnHSNGVYATLVHSEM 1273
Cdd:cd03288 193 NILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA-QEDGVFASLVRTDK 257
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1033-1258 |
5.41e-32 |
|
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: 125.93 E-value: 5.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPAL-FGGTIGENIRFG-----NPNASWSE-----VEEAAKEAYIHNFIcglprgyETEVGEsgiqLSGGQKQRIA 1181
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlGLFGRPSAedreaVEEALERTGLEHLA-------DRPVDE----LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1182 IARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLS-TIKKANAIAVVQNGKVSEYGTHDTLLT 1258
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
125-371 |
1.06e-31 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 126.47 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 125 ALSGIVVIGA---YLQIACWRLVGERLGHRIRSKYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGDKMSQFIY 201
Cdd:cd18573 46 ALLGVFVVGAaanFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDK-NKTGELVSRLSSDTSVVGKSLTQNLSDGLR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 202 HIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAA 281
Cdd:cd18573 125 SLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 282 RYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYSTWALAFWYGSILVSRNELSGG-----AAIACFFGVTIGGrglaLSlS 356
Cdd:cd18573 205 RYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGdltsfLMYAVYVGSSVSG----LS-S 279
|
250
....*....|....*
gi 1770234124 357 YFAQFAQGTVAASKV 371
Cdd:cd18573 280 FYSELMKGLGASSRL 294
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
398-616 |
1.15e-31 |
|
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: 123.84 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMsvpILNSLNLVIPSQrISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTlQVKWLRSQMG 477
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILE-----NILMGKENATKKEAIDACI-AVNAHNFicdlpqgYDTQVGekgtQLSGGQKQRIALARA 550
Cdd:cd03264 76 YLPQEFGVYPNfTVREfldyiAWLKGIPSKEVKARVDEVLeLVNLGDR-------AKKKIG----SLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 551 MIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIG 616
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1033-1258 |
1.18e-31 |
|
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: 124.71 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLD---LKWLRL 1109
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 QTALVGQEPALFGG-TIGENIRFG---NPNASWSEVEEAAKEAyihnficgLprgyeTEVGESGI------QLSGGQKQR 1179
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLEK--------L-----ELVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1180 IAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTL 1256
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElgLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 1770234124 1257 LT 1258
Cdd:COG1127 230 LA 231
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
75-371 |
1.30e-31 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 126.13 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 75 IIIGCLGALINGGSQPWYSYLFGNFVNKIALDNDKDQMIKdvreLCVLMSALSGIVVIGAYLQIACWRLVGERLGHRIRS 154
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLW----IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 155 KYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFC 234
Cdd:cd07346 77 DLFRHLQRLSLSFFDR-NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 235 GVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYS 314
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 315 TWALAFWYGSILVSRNELSGGAAIACFFGVTIGGRGLALSLSYFAQFAQGTVAASKV 371
Cdd:cd07346 236 GTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
399-610 |
1.43e-31 |
|
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: 123.41 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 399 ELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLqvkwlRSQMGM 478
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 479 VGQEPVL---FADTILENILMG---------KENATKKEAIDACIA-VNAHNFIcdlpqgyDTQVGEkgtqLSGGQKQRI 545
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGlyghkglfrRLSKADKAKVDEALErVGLSELA-------DRQIGE----LSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 546 ALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRLATV-KNAETIIVLEQG 610
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1033-1262 |
1.44e-31 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 124.53 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRP-DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQT 1111
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVGQEPAL-------FGGTIGENIRFGNPNASWSEVEEAAKEayihnfiCGLPRGYETEVGEsgiQLSGGQKQRIAIAR 1184
Cdd:COG1124 82 QMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQ-------VGLPPSFLDRYPH---QLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1185 AIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTNHS 1261
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErgLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGPK 231
|
.
gi 1770234124 1262 N 1262
Cdd:COG1124 232 H 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
398-623 |
1.49e-31 |
|
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: 123.70 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVkWLRSQMG 477
Cdd:cd03224 1 LEVENLNAGYGK---SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPP-HERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 M--VGQEPVLFAD-TILENILMG---KENATKKEAIDAciavnahnfICDL-PQGYDTQvGEKGTQLSGGQKQRIALARA 550
Cdd:cd03224 77 IgyVPEGRRIFPElTVEENLLLGayaRRRAKRKARLER---------VYELfPRLKERR-KQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 551 MIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVI----AHRLATVknAETIIVLEQGSVIEIGDHNKLMA 623
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1033-1258 |
1.55e-31 |
|
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: 124.15 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDL---DLKWLRL 1109
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 QTALVGQEPALFGG-TIGENIRFG---NPNASWSEVEEAAKEAYihnficglprgyeTEVGESGI------QLSGGQKQR 1179
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLEKL-------------EAVGLRGAedlypaELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1180 IAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTL 1256
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 1770234124 1257 LT 1258
Cdd:cd03261 225 RA 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1033-1249 |
2.48e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 123.23 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPS-RPDVIVLREFCLKVKGGTMVAVVGGSGSGKST---VIWLMQRfydPIGGKVMMGGRDLRDLD---LK 1105
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1106 WLRLQT-ALVGQEPALFGG-TIGENIRFgnP----NASWSEVEEAAKEA--------YIHNFicglPRgyetevgesgiQ 1171
Cdd:COG1136 82 RLRRRHiGFVFQFFNLLPElTALENVAL--PlllaGVSRKERRERARELlervglgdRLDHR----PS-----------Q 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1172 LSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT-TTIVVV-HRLSTIKKANAIAVVQNGKVSE 1249
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
397-604 |
5.24e-31 |
|
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: 121.82 E-value: 5.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKST---IFALLERfydPNKGLILLDGQDIRTLQVKWlR 473
Cdd:COG4133 2 MLEAENLSCRRGER---LLFSGLSFTLAAGEALALTGPNGSGKTTllrILAGLLP---PSAGEVLWNGEPIRDAREDY-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 474 SQMGMVGQEPVLFAD-TILENILM---GKENATKKEAIDACIAvnahnfICDLPQGYDTQVGekgtQLSGGQKQRIALAR 549
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRFwaaLYGLRADREAIDEALE------AVGLAGLADLPVR----QLSAGQKRRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 550 AMIKDPKILLLDEPTSALDPKSESLVQQAI-DKISKGRTTIVIAHRLATVKNAETI 604
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIaAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
396-616 |
6.75e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.96 E-value: 6.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 396 GRLELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKST---IFALLErfyDPNKGLILLDGQDIRTLQVKwl 472
Cdd:COG3839 2 ASLELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTllrMIAGLE---DPTSGEILIGGRDVTDLPPK-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 473 RSQMGMVGQEPVLFAD-TILENILMGKENA-TKKEAIDACIAVNAHnfICDLpqgyDTQVGEKGTQLSGGQKQRIALARA 550
Cdd:COG3839 74 DRNIAMVFQSYALYPHmTVYENIAFPLKLRkVPKAEIDRRVREAAE--LLGL----EDLLDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 551 MIKDPKILLLDEPTSALDPKsesLVQQAIDKISK-----GRTTIVIAH------RLATvknaeTIIVLEQGSVIEIG 616
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAK---LRVEMRAEIKRlhrrlGTTTIYVTHdqveamTLAD-----RIAVMNDGRIQQVG 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
412-616 |
7.55e-31 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. 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: 213261 [Multi-domain] Cd Length: 269 Bit Score: 123.14 E-value: 7.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 412 SVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWL----RSQMGMVGQEPVLFA 487
Cdd:cd03294 36 QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 488 D-TILENILMGKE------NATKKEAIDACIAVNAHNFICDLPQgydtqvgekgtQLSGGQKQRIALARAMIKDPKILLL 560
Cdd:cd03294 116 HrTVLENVAFGLEvqgvprAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 561 DEPTSALDP------KSESLVQQAidkiSKGRTTIVIAHRLA-TVKNAETIIVLEQGSVIEIG 616
Cdd:cd03294 185 DEAFSALDPlirremQDELLRLQA----ELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
398-616 |
9.82e-31 |
|
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: 121.46 E-value: 9.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTlQVKWLRSQMG 477
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENI-----LMGKENATKKEAIDACIAVnahnfiCDLPQGYDTQVGekgtQLSGGQKQRIALARAM 551
Cdd:cd03263 79 YCPQFDALFDElTVREHLrfyarLKGLPKSEIKEEVELLLRV------LGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 552 IKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTI----------VIAHRLAtvknaetiiVLEQGSVIEIG 616
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIIltthsmdeaeALCDRIA---------IMSDGKLRCIG 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1033-1228 |
2.36e-30 |
|
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: 120.27 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSR-PDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLdlkwlRLQT 1111
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVGQEPALFG-GTIGENIRFG--NPNASWSEVEEAAkEAYIHnficglprgyetEVGESGI------QLSGGQKQRIAI 1182
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGleLQGVPKAEARERA-EELLE------------LVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1770234124 1183 ARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT--TTIVVVH 1228
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTH 190
|
|
| R-SNARE_SEC22 |
cd15866 |
SNARE motif of SEC22; SEC22 forms complexes with syntaxin 18 (Qa), Sec20 (Qb) and USE1 (Qc), ... |
1469-1532 |
3.49e-30 |
|
SNARE motif of SEC22; SEC22 forms complexes with syntaxin 18 (Qa), Sec20 (Qb) and USE1 (Qc), and with syntaxin 5 (Qa), GS27 (Qb) and Bet1 (Qc). These complexes are involved in the transport from cis-Golgi to the endoplasmic reticulum (ER) and in the transport from endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC), respectively. SEC22 is a member of the R-SNARE subfamily of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins which contain coiled-coil helices (called SNARE motifs) that mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.
Pssm-ID: 277219 [Multi-domain] Cd Length: 64 Bit Score: 114.15 E-value: 3.49e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1469 QRNISKLNDELYEVHQIMTRNVQEVLGVGEKLDQVSQMSSRLTSESRIYADKARDLNRQALIKK 1532
Cdd:cd15866 1 RRNLSKLNDELQDVQRIMTKNIDDVLGRGEKLDDLSDKSSNLSSESKKYKKDAKKLNLQALYRK 64
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
398-612 |
7.86e-30 |
|
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: 118.66 E-value: 7.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL---QVKWLRS 474
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFAD-TILENILMGKE------NATKKEAIDACIAVNAHNFICDLPQgydtqvgekgtQLSGGQKQRIAL 547
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtgvppREIRKRVPAALELVGLSHKHRALPA-----------ELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 548 ARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNA--ETIIVLEQGSV 612
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
398-617 |
7.98e-30 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 121.70 E-value: 7.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRM-SVPILNSLNLVIPSQRISALVGASGAGKSTI-FALLeRFYDPN---KGLILLDGQDIRTL---QV 469
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAIL-GLLPPPgitSGEILFDGEDLLKLsekEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 470 KWLR-SQMGMVGQE------PVL-----FADTILENILMGKENAtKKEAIDACIAV---NAHNFICDLPQgydtqvgekg 534
Cdd:COG0444 81 RKIRgREIQMIFQDpmtslnPVMtvgdqIAEPLRIHGGLSKAEA-RERAIELLERVglpDPERRLDRYPH---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 535 tQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPksesLVQ-QAIDKISK-----GRTTIVIAHRLATVKN-AETIIVL 607
Cdd:COG0444 150 -ELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNLLKDlqrelGLAILFITHDLGVVAEiADRVAVM 224
|
250
....*....|
gi 1770234124 608 EQGSVIEIGD 617
Cdd:COG0444 225 YAGRIVEEGP 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1033-1262 |
1.57e-29 |
|
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: 118.81 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRlQTA 1112
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR-QIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGG-TIGENIR-FGNPNASWSEVEEAAKEAYIHNFicGLPRGYETEVGEsgiqLSGGQKQRIAIARAIVKKS 1190
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRyFAELYGLFDEELKKRIEELIELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1191 KVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTNHSN 1262
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
398-613 |
1.87e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 118.99 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSfaypsrMS---VPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVkWLRS 474
Cdd:COG0411 5 LEVRGLT------KRfggLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMV--GQEPVLFAD-TILENILMG--------------------KENATKKEAIDACIAvnahnfICDLPQGYDTQVG 531
Cdd:COG0411 78 RLGIArtFQNPRLFPElTVLENVLVAaharlgrgllaallrlprarREEREARERAEELLE------RVGLADRADEPAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 532 EkgtqLSGGQKQRIALARAMIKDPKILLLDEPTSALDPK-SESLVqQAIDKISK--GRTTIVIAHRLATVKN-AETIIVL 607
Cdd:COG0411 152 N----LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEeTEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVL 226
|
....*.
gi 1770234124 608 EQGSVI 613
Cdd:COG0411 227 DFGRVI 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
419-616 |
1.97e-29 |
|
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: 117.21 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 419 LNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwlRSQMGMVGQEPVLFAD-TILENILMG 497
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 498 -----KENATKKEAIDACIA-VNAHNFICDLPQgydtqvgekgtQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKS 571
Cdd:cd03298 95 lspglKLTAEDRQAIEVALArVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1770234124 572 ESLVQQAIDKI--SKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIG 616
Cdd:cd03298 164 RAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
399-616 |
2.13e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 121.06 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 399 ELKNVSFAYP-SRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFA---LLERfydPNKGLILLDGQDIRTLQVKWLRS 474
Cdd:PRK11153 3 ELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRcinLLER---PTSGRVLVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 ---QMGMVGQE-PVLFADTILENILMGKENA-TKKEAIDAciAVNAhnfICDLpqgydtqVG--EKG----TQLSGGQKQ 543
Cdd:PRK11153 80 arrQIGMIFQHfNLLSSRTVFDNVALPLELAgTPKAEIKA--RVTE---LLEL-------VGlsDKAdrypAQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 544 RIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIG 616
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
718-964 |
2.24e-29 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 119.57 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 718 IFGMLAGAILSLF-PLVLGQAL-TVYFNPDKSKLQKDVGYLCLALVGLGfgcILTmmGQQGFC-GWAGTKLTKRVRDLLF 794
Cdd:cd18572 2 FVFLVVAALSELAiPHYTGAVIdAVVADGSREAFYRAVLLLLLLSVLSG---LFS--GLRGGCfSYAGTRLVRRLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 795 RSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLA-TIVTPFTLGAS 873
Cdd:cd18572 77 RSLLRQDIAFFD--ATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAfITVPVIALITK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 874 YFSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMYSAY 953
Cdd:cd18572 155 VYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQ 234
|
250
....*....|.
gi 1770234124 954 TLVLFFGAYLV 964
Cdd:cd18572 235 VLVLFYGGHLV 245
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
398-619 |
2.72e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 117.81 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDG------QDIRTLQVKW 471
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 472 LRSQMGMVGQE----PVLfadTILENIL---MGKENATKKEAIDACIAVNAHNFICDLPQGYDTQvgekgtqLSGGQKQR 544
Cdd:COG4161 80 LRQKVGMVFQQynlwPHL---TVMENLIeapCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLH-------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 545 IALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLATV-KNAETIIVLEQGSVIEIGDHN 619
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGDAS 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
398-616 |
2.76e-29 |
|
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: 117.83 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwlRSQMG 477
Cdd:cd03296 3 IEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENILMGKENATKKEAID-ACIAVNAHNFIcDLPQgYDTQVGEKGTQLSGGQKQRIALARAMIKDP 555
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPRSERPPeAEIRAKVHELL-KLVQ-LDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 556 KILLLDEPTSALDPKS----ESLVQQAIDKIskGRTTIVIAHRLA-TVKNAETIIVLEQGSVIEIG 616
Cdd:cd03296 156 KVLLLDEPFGALDAKVrkelRRWLRRLHDEL--HVTTVFVTHDQEeALEVADRVVVMNKGRIEQVG 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
398-616 |
3.60e-29 |
|
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: 117.34 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwlRSQMG 477
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENILMG------KENATKKEAIDACIAVNAHNFICDLPQgydtqvgekgtQLSGGQKQRIALARA 550
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 551 MIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLA---TVknAETIIVLEQGSVIEIG 616
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1047-1272 |
4.89e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 117.09 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRlQTALVGQEPALFGG-TI 1125
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR-RIGYVPQEPALYPDlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1126 GENIRFgnpNASWSEVEEAAKEAYIHNFI--CGLPRGYETEVGesgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSALD 1203
Cdd:COG1131 91 RENLRF---FARLYGLPRKEARERIDELLelFGLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1204 LESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTNHSNGVYATLVHSE 1272
Cdd:COG1131 164 PEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKARLLEDVFLELTGEE 234
|
|
| SNC1 |
COG5143 |
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion]; |
1346-1530 |
4.93e-29 |
|
Synaptobrevin/VAMP-like protein [Intracellular trafficking and secretion];
Pssm-ID: 227472 [Multi-domain] Cd Length: 190 Bit Score: 115.60 E-value: 4.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1346 VTDGLPLAEGLDDGRDMQDAEFYKQQVKALFKNLSRgqNEASRMSVETGPYVFHYIIEGR-VCYLTMCDRAYPKKLAFQY 1424
Cdd:COG5143 8 RVKGEPLRTLSDAESLSSFSFFHRSKVKEVLRFLSK--TSASRASIESGDYFFHYLKMSSgIVYVPISDKEYPNKLAYGY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1425 LEDLKNEFERGYGNQIET-AARPYAFIKFDTFIQKTkklYQDTRTQRNISKLNDELYEVHQIMTRNVQEVLGVGEKLDQV 1503
Cdd:COG5143 86 LNSIATEFLKSSALEQLIdDTVGIMRVNIDKVIEKG---YRDPSIQDKLDQLQQELEETKRVLNKNIEKVLYRDEKLDLL 162
|
170 180
....*....|....*....|....*..
gi 1770234124 1504 SQMSSRLTSESRIYADKARDLNRQALI 1530
Cdd:COG5143 163 VDLSSILLLSSKMFPKSAKKSNLCCLI 189
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1033-1262 |
4.99e-29 |
|
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: 117.02 E-value: 4.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPDVivLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:cd03295 1 IEFENVTKRYGGGKKA--VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGG-TIGENIRFGNPNASWSE--VEEAAKEAyIHnfICGL-PRGYeteVGESGIQLSGGQKQRIAIARAIVK 1188
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIALVPKLLKWPKekIRERADEL-LA--LVGLdPAEF---ADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1189 KSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRL-STIKKANAIAVVQNGKVSEYGTHDTLLTNHSN 1262
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1033-1227 |
5.60e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 117.50 E-value: 5.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRP-DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwlrlqT 1111
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVGQEPALFg-gTIGENIRFGNPNASWS--EVEEAAkEAYIHNFicGL-------PRgyetevgesgiQLSGGQKQRIA 1181
Cdd:COG1116 83 GVVFQEPALLpwlTVLDNVALGLELRGVPkaERRERA-RELLELV--GLagfedayPH-----------QLSGGMRQRVA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1770234124 1182 IARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT-TTIVVV 1227
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgKTVLFV 195
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1050-1269 |
7.74e-29 |
|
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: 116.28 E-value: 7.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLdlKWLRLQTALVGQEPALFGG-TIGEN 1128
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL--PPEKRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1129 IRFGNPNASWS------EVEEAAKEAYIHNFicgLPRGYETevgesgiqLSGGQKQRIAIARAIVKKSKVLLLDEATSAL 1202
Cdd:cd03299 92 IAYGLKKRKVDkkeierKVLEIAEMLGIDHL---LNRKPET--------LSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1203 DLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTNHSNGVYATLV 1269
Cdd:cd03299 161 DVRTKEKLREELKKIRKEfgVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1047-1259 |
1.04e-28 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 116.25 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDL--RDLDLKWLRLQTALVGQEPALFGG- 1123
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 TIGENIRFGnP----NASWSEVEEAAKE------------AYihnficglPRgyetevgesgiQLSGGQKQRIAIARAIV 1187
Cdd:COG1126 93 TVLENVTLA-PikvkKMSKAEAEERAMEllervgladkadAY--------PA-----------QLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1188 KKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:COG1126 153 MEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVtHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
398-613 |
1.72e-28 |
|
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: 112.91 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQdirtlqvkwlrsqmg 477
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 mvgqePVLFADTilenilmgkenatkKEAIDACIAVnAHnficdlpqgydtqvgekgtQLSGGQKQRIALARAMIKDPKI 557
Cdd:cd03216 63 -----EVSFASP--------------RDARRAGIAM-VY-------------------QLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 558 LLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRLATVKN-AETIIVLEQGSVI 613
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLrAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
399-593 |
2.25e-28 |
|
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: 113.89 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 399 ELKNVSFAYPSRMSvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTlqvKWLRSQMGM 478
Cdd:cd03226 1 RIENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 479 VGQEP--VLFADTILENILMGKENATKKEAIDACI--AVNAHNFICDLPQgydtqvgekgtQLSGGQKQRIALARAMIKD 554
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGLKELDAGNEQAETVlkDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1770234124 555 PKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAH 593
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITH 184
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1038-1251 |
2.42e-28 |
|
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: 112.91 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1038 VNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQE 1117
Cdd:cd03214 5 LSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1118 PALFGgtigenirfgnpnaswseveeaakeayIHNFicgLPRGYETevgesgiqLSGGQKQRIAIARAIVKKSKVLLLDE 1197
Cdd:cd03214 82 LELLG---------------------------LAHL---ADRPFNE--------LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1198 ATSALDLESEKHVQDAIRKIIKRT--TTIVVVHRLS-TIKKANAIAVVQNGKVSEYG 1251
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
398-617 |
4.11e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 115.60 E-value: 4.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEP--VLFADTILENILMGKENA--TKKE----AIDACIAVNAHNFICDLPQgydtqvgekgtQLSGGQKQRIALAR 549
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMglDKDEverrVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 550 AMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIA-HRLATVKN-AETIIVLEQGSVIEIGD 617
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGD 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
416-617 |
4.39e-28 |
|
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: 114.36 E-value: 4.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 416 LNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwlRSQMGMVGQEPVLFAD-TILENI 494
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 495 LMG-KENATKKEAIDACIavnaHNFICDLpqGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSES 573
Cdd:cd03299 93 AYGlKKRKVDKKEIERKV----LEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1770234124 574 LVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGD 617
Cdd:cd03299 167 KLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGK 213
|
|
| Longin |
pfam13774 |
Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for ... |
1379-1454 |
4.55e-28 |
|
Regulated-SNARE-like domain; Longin is one of the approximately 26 components required for transporting proteins from the ER to the plasma membrane, via the Golgi apparatus. It is necessary for the steps of the transfer from the ER to the Golgi complex. Longins are the only R-SNAREs that are common to all eukaryotes, and they are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain.
Pssm-ID: 463978 Cd Length: 81 Bit Score: 108.78 E-value: 4.55e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1379 LSRGQNEASRMSVETGPYVFHYIIEGRVCYLTMCDRAYPKKLAFQYLEDLKNEFERGYGNQIETAARPYAFIK-FDT 1454
Cdd:pfam13774 5 LEKIPQNPQRQTYEGDNYTFHYLIEDGLTYLVIADKSYPRRLAFAFLEEIKDEFLSTYGPWTASALRPYAFNKeFDT 81
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
398-625 |
6.50e-28 |
|
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: 113.54 E-value: 6.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKST----IFALLerfyDPNKGLILLDGQDIRTLQVkWLR 473
Cdd:COG0410 4 LEVENLHAGYGG---IHVLHGVSLEVEEGEIVALLGRNGAGKTTllkaISGLL----PPRSGSIRFDGEDITGLPP-HRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 474 SQMGM--VGQEPVLFAD-TILENILMGKENATKKEAIDACIAvnahnFICDL-PQgydtqVGE----KGTQLSGGQKQRI 545
Cdd:COG0410 76 ARLGIgyVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLE-----RVYELfPR-----LKErrrqRAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 546 ALARAMIKDPKILLLDEPTSALDPKsesLVQQ---AIDKISKGRTTIVI----AHRLATVknAETIIVLEQGSVIEIGDH 618
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGLAPL---IVEEifeIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTA 220
|
....*..
gi 1770234124 619 NKLMAQE 625
Cdd:COG0410 221 AELLADP 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
398-616 |
6.57e-28 |
|
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: 113.12 E-value: 6.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwlRSQMG 477
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENILMG-KENATKKEAIDACIAVNAHNFicdlpqGYDTQVGEKGTQLSGGQKQRIALARAMIKDP 555
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGlKLRKVPKDEIDERVREVAELL------QIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 556 KILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAH-RLATVKNAETIIVLEQGSVIEIG 616
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
420-617 |
8.00e-28 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 112.65 E-value: 8.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 420 NLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwlRSQMGMVGQEPVLFAD-TILENILMG- 497
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY--QRPVSMLFQENNLFAHlTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 498 ----KENATKKEAI-DACIAVNAHNFICDLPQgydtqvgekgtQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSE 572
Cdd:TIGR01277 96 hpglKLNAEQQEKVvDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1770234124 573 ----SLVQQAIDKisKGRTTIVIAHRLA-TVKNAETIIVLEQGSVIEIGD 617
Cdd:TIGR01277 165 eemlALVKQLCSE--RQRTLLMVTHHLSdARAIASQIAVVSQGKIKVVSD 212
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
431-630 |
8.13e-28 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 116.05 E-value: 8.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 431 LVGASGAGKSTIFALLERFYDPNKGLILLDGQDIrTLQVKWLRSqMGMVGQEPVLFAD-TILENILMG-KENATKKEAID 508
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-TNVPPHLRH-INMVFQSYALFPHmTVEENVAFGlKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 509 AciAVNAHNFICDLpQGYDTQvgeKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GR 586
Cdd:TIGR01187 79 P--RVLEALRLVQL-EEFADR---KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEqlGI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1770234124 587 TTIVIAH-RLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFS 630
Cdd:TIGR01187 153 TFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFV 197
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1033-1247 |
8.15e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 114.00 E-value: 8.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSrpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDL---DLKWLRL 1109
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 QTALVGQEPALFGG-TIGENI---RFGNPNA------SWSEVE-EAAKEAyihnficgLPRgyeteVGESGI------QL 1172
Cdd:COG3638 81 RIGMIFQQFNLVPRlSVLTNVlagRLGRTSTwrsllgLFPPEDrERALEA--------LER-----VGLADKayqradQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1173 SGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKV 1247
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdgITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1033-1262 |
8.33e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 113.31 E-value: 8.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdvivLReFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDlkwlrlqta 1112
Cdd:COG3840 2 LRLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 lVGQEPA--------LFGG-TIGENIRFG-NPN-----ASWSEVEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQK 1177
Cdd:COG3840 68 -PAERPVsmlfqennLFPHlTVAQNIGLGlRPGlkltaEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1178 QRIAIARAIVKKSKVLLLDEATSALD--LESEKHvqDAIRKIIKRT--TTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGT 1252
Cdd:COG3840 136 QRVALARCLVRKRPILLLDEPFSALDpaLRQEML--DLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGP 213
|
250
....*....|
gi 1770234124 1253 HDTLLTNHSN 1262
Cdd:COG3840 214 TAALLDGEPP 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
398-622 |
9.50e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 113.26 E-value: 9.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIR--TLQVKWLRSQ 475
Cdd:PRK09493 2 IEFKNVSKHFGP---TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MGMVGQEPVLFAD-TILENILMGK---ENATKKEAIDACIAVNAHnficdlpQGYDTQVGEKGTQLSGGQKQRIALARAM 551
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGPlrvRGASKEEAEKQARELLAK-------VGLAERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 552 IKDPKILLLDEPTSALDP--KSESL-VQQaiDKISKGRTTIVIAHRLATV-KNAETIIVLEQGSVIEIGDHNKLM 622
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPelRHEVLkVMQ--DLAEEGMTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
94-370 |
1.05e-27 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 114.89 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 94 YLFGNFVNKIALDndkdqmiKDVRELCVLMSALSGIVVIGA---YLQIACWRLVGERLGHRIRSKYLRAVLRQDVSFFDT 170
Cdd:cd18576 17 LLAGQLIDAALGG-------GDTASLNQIALLLLGLFLLQAvfsFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 171 DiSTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFCgvaykAVYVG-----L 245
Cdd:cd18576 90 R-RVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLV-----AVLFGrrirkL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 246 AAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYSTWALAFWYGSI 325
Cdd:cd18576 164 SKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGR 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1770234124 326 LVSRNELSGGAAIA-CFFGVTIGG--RGLAlslSYFAQFaQGTVAASK 370
Cdd:cd18576 244 LVLAGELTAGDLVAfLLYTLFIAGsiGSLA---DLYGQL-QKALGASE 287
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
398-617 |
1.07e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 113.72 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSvpiLNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPN-----KGLILLDGQDI---RTLQV 469
Cdd:PRK14239 6 LQVSDLSVYYNKKKA---LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 470 KwLRSQMGMVGQEPVLFADTILENILMG------KENATKKEAID-ACIAVNAHNFICDlpQGYDTQVGekgtqLSGGQK 542
Cdd:PRK14239 83 D-LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEAVEkSLKGASIWDEVKD--RLHDSALG-----LSGGQQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 543 QRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRL--ATVKNAETIIVLEqGSVIEIGD 617
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqASRISDRTGFFLD-GDLIEYND 230
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
718-997 |
1.46e-27 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 114.19 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 718 IFGMLAGAILSLF-PLVLGQAL-TVYFNPDKSKLQKDVGYLCLALVglgFGCILTMMGQQGFCGwAGTKLTKRVRDLLFR 795
Cdd:cd18557 2 LLFLLISSAAQLLlPYLIGRLIdTIIKGGDLDVLNELALILLAIYL---LQSVFTFVRYYLFNI-AGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 796 SILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLAL-LATIVTPFTLGASY 874
Cdd:cd18557 78 SLLRQEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLvLLLVIPLLLIASKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 875 FSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMYSAYT 954
Cdd:cd18557 156 YGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1770234124 955 LVLFFGAYLVKKDYTKFGDV--YKIFLILVlsTFSVGQFAGLAPD 997
Cdd:cd18557 236 LVLWYGGYLVLSGQLTVGELtsFILYTIMV--ASSVGGLSSLLAD 278
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
398-630 |
1.70e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 116.47 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSVpilNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRtlQVKWLRSQMG 477
Cdd:PRK11607 20 LEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENILMG-KENATKKEAIDACIA-----VNAHNFicdlpqgydtqVGEKGTQLSGGQKQRIALARA 550
Cdd:PRK11607 95 MMFQSYALFPHmTVEQNIAFGlKQDKLPKAEIASRVNemlglVHMQEF-----------AKRKPHQLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 551 MIKDPKILLLDEPTSALDPKSESLVQ-QAIDKISK-GRTTIVIAH-RLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGA 627
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTT 243
|
...
gi 1770234124 628 YFS 630
Cdd:PRK11607 244 RYS 246
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1048-1262 |
1.72e-27 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. 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: 213261 [Multi-domain] Cd Length: 269 Bit Score: 113.51 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1048 VIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWL----RLQTALVGQEPALFGG 1123
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 -TIGENIRFG--NPNASWSEVEEAAKEAY----IHNFICGLPRgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLLLD 1196
Cdd:cd03294 117 rTVLENVAFGleVQGVPRAEREERAAEALelvgLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 1197 EATSALDLESEKHVQDAIRKIIK--RTTTIVVVHRLS-TIKKANAIAVVQNGKVSEYGTHDTLLTNHSN 1262
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNPAN 254
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
398-569 |
2.10e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 111.42 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPN---KGLILLDGQDIRTLQVkwLRS 474
Cdd:COG4136 2 LSLENLTITLGGR---PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFAD-TILENILMGKENATKKEAIDACIAvNAhnficdLpqgydTQVGEKG------TQLSGGQKQRIAL 547
Cdd:COG4136 77 RIGILFQDDLLFPHlSVGENLAFALPPTIGRAQRRARVE-QA------L-----EEAGLAGfadrdpATLSGGQRARVAL 144
|
170 180
....*....|....*....|..
gi 1770234124 548 ARAMIKDPKILLLDEPTSALDP 569
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDA 166
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1046-1251 |
3.30e-27 |
|
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: 110.81 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1046 PDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwlRLQTALVGQEPALFGG-T 1124
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVFQNYALYPHmT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1125 IGENIRFG-----NPNASWSE-VEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLLLDEA 1198
Cdd:cd03301 89 VYDNIAFGlklrkVPKDEIDErVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1199 TSALDLESEKHVQDAIRKIIKR--TTTIVVVH-RLSTIKKANAIAVVQNGKVSEYG 1251
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1033-1247 |
6.02e-27 |
|
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: 110.27 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPD-VIVLREFCLKVKGGTMVAVVGGSGSGKST---VIWLMQRfydPIGGKVMMGGRDLRDLDLKWL- 1107
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1108 ---RLQTALVGQEPALFGG-TIGENIRF-----GNPNAswsEVEEAAKEA--YIhnficGLPRGYETEVGesgiQLSGGQ 1176
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVELplllaGVPKK---ERRERAEELleRV-----GLGDRLNHYPS----ELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1177 KQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIK--RTTTIVVVHRLSTIKKANAIAVVQNGKV 1247
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1050-1227 |
6.11e-27 |
|
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: 110.31 E-value: 6.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDL--RDLDLKWLRLQTALVGQEPALFGG-TIG 1126
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1127 ENIRFGnP----NASWSEVEEAAKEAyihnficgLPR-GYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSA 1201
Cdd:cd03262 95 ENITLA-PikvkGMSKAEAEERALEL--------LEKvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180
....*....|....*....|....*.
gi 1770234124 1202 LDLESEKHVQDAIRKIIKRTTTIVVV 1227
Cdd:cd03262 166 LDPELVGEVLDVMKDLAEEGMTMVVV 191
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
407-592 |
6.20e-27 |
|
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: 109.43 E-value: 6.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 407 YPSRMSVpiLNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDI---RTLQVKWlRSQMGMVGQEP 483
Cdd:TIGR01166 1 YPGGPEV--LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLER-RQRVGLVFQDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 484 --VLFADTILENILMGKENATKKEA------IDACIAVNAHNFICDLPQgydtqvgekgtQLSGGQKQRIALARAMIKDP 555
Cdd:TIGR01166 78 ddQLFAADVDQDVAFGPLNLGLSEAeverrvREALTAVGASGLRERPTH-----------CLSGGEKKRVAIAGAVAMRP 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 1770234124 556 KILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIA 592
Cdd:TIGR01166 147 DVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVIS 183
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1038-1259 |
7.56e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 113.70 E-value: 7.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1038 VNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLrDLDLKWLRLQTALVGQE 1117
Cdd:COG1118 8 ISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGFVFQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1118 PALFGG-TIGENIRFGNPNASWSEVEEAAK-EAYIHnficglprgyetEVGESGI------QLSGGQKQRIAIARAIVKK 1189
Cdd:COG1118 84 YALFPHmTVAENIAFGLRVRPPSKAEIRARvEELLE------------LVQLEGLadrypsQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1190 SKVLLLDEATSALDLESEKHVQDAIRKIIKRT--TTIVVVH------RLstikkANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
715-964 |
9.38e-27 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 111.87 E-value: 9.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 715 VGVIFGMLAGAILSLFPLVLGQALtvyfnpDKSKLQKDVGYL---CLALVGLGFGCILTMMGQQGFCGWAGTKLTKRVRD 791
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLLI------DDVIPAGDLSLLlwiALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 792 LLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPFT-L 870
Cdd:cd07346 77 DLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYvL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 871 GASYFSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMY 950
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250
....*....|....
gi 1770234124 951 SAYTLVLFFGAYLV 964
Cdd:cd07346 235 LGTALVLLYGGYLV 248
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1047-1252 |
9.58e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 113.63 E-value: 9.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwlRLQTALVGQEPALF-GGTI 1125
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAMVFQSYALYpHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1126 GENIRFGNPNASWSE------VEEAAKeayihnfICGL-------PRgyetevgesgiQLSGGQKQRIAIARAIVKKSKV 1192
Cdd:COG3839 93 YENIAFPLKLRKVPKaeidrrVREAAE-------LLGLedlldrkPK-----------QLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1193 LLLDEATSALD------LESEkhvqdaIRKIIKR--TTTIVVVHRLS---TIkkANAIAVVQNGKVSEYGT 1252
Cdd:COG3839 155 FLLDEPLSNLDaklrveMRAE------IKRLHRRlgTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGT 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
398-618 |
1.19e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 110.49 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDG------QDIRTLQVKW 471
Cdd:PRK11124 3 IQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 472 LRSQMGMVGQEPVLFAD-TILENIL--------MGKENAtKKEAIDACIAVNAHNFICDLPQgydtqvgekgtQLSGGQK 542
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPHlTVQQNLIeapcrvlgLSKDQA-LARAEKLLERLRLKPYADRFPL-----------HLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 543 QRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLATVKNAETIIV-LEQGSVIEIGDH 618
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVyMENGHIVEQGDA 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
398-617 |
1.19e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.89 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRtlqvkwLRS--- 474
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR------FRSprd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 --QMG--MVGQEPVLFAD-TILENILMGKE---------NATKKEAIDACIAVNAHnfiCDLpqgyDTQVGEkgtqLSGG 540
Cdd:COG1129 76 aqAAGiaIIHQELNLVPNlSVAENIFLGREprrgglidwRAMRRRARELLARLGLD---IDP----DTPVGD----LSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 541 QKQRIALARAMIKDPKILLLDEPTSALDPK-SESLVQQaIDKI-SKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGD 617
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLTEReVERLFRI-IRRLkAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGP 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1056-1252 |
1.24e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.68 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRD--LDLKWLRLQTALVGQEP--ALFGGTIGENIRF 1131
Cdd:PRK13637 28 IEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPeyQLFEETIEKDIAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1132 G--NPNASWSEVEEAAKEAYIhnfICGLPrgYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKH 1209
Cdd:PRK13637 108 GpiNLGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1770234124 1210 VQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGT 1252
Cdd:PRK13637 183 ILNKIKELHKEynMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
398-616 |
1.40e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 111.37 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSV--PILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL----QVKW 471
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 472 LRSQMGMVGQ--EPVLFADTILENILMGKEN--ATKKEAidACIAVNAHNFIcdlpqGYDTQVGEKGT-QLSGGQKQRIA 546
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEA--EALAREKLALV-----GISESLFEKNPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 547 LARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIV-IAHRLATVKN-AETIIVLEQGSVIEIG 616
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1047-1252 |
1.47e-26 |
|
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: 109.63 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwlRLQTALVGQEPALFGG-TI 1125
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPHlTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1126 GENIRFG------NPNASWSEVEEAAK----EAYIHNFICglprgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLLL 1195
Cdd:cd03300 90 FENIAFGlrlkklPKAEIKERVAEALDlvqlEGYANRKPS---------------QLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1196 DEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLS-TIKKANAIAVVQNGKVSEYGT 1252
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKElgITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1037-1262 |
1.87e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.80 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1037 MVNFAYPSRP--DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRD--LDLKWLRLQTA 1112
Cdd:PRK09493 1 MIEFKNVSKHfgPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGG-TIGENIRFGnP----NASWSEVEEAAKEAyihnficgLPR-GYETEVGESGIQLSGGQKQRIAIARAI 1186
Cdd:PRK09493 81 MVFQQFYLFPHlTALENVMFG-PlrvrGASKEEAEKQAREL--------LAKvGLAERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1187 VKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTNHSN 1262
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVtHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1033-1252 |
2.03e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 112.09 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRP-DVIVLREFCLKVKGGTMVAVVGGSGSGKST---VIWLMQRfydPIGGKVMMGGRDLRDLD---LK 1105
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSereLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1106 WLRLQTALVGQEPALFGG-TIGENIRFgnP--NASWSEVEEAAK--------------EAYihnficglPRgyetevges 1168
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVAL--PleIAGVPKAEIRKRvaellelvglsdkaDAY--------PS--------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1169 giQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT-TTIVVV-HRLSTIKK-ANAIAVVQNG 1245
Cdd:COG1135 140 --QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELgLTIVLItHEMDVVRRiCDRVAVLENG 217
|
....*..
gi 1770234124 1246 KVSEYGT 1252
Cdd:COG1135 218 RIVEQGP 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
398-607 |
2.64e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 108.65 E-value: 2.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:PRK10247 8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFADTILENILMGKENATKKEAIDAciavnahnFICDLPQ-GYDTQVGEKG-TQLSGGQKQRIALARAMIKDP 555
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAI--------FLDDLERfALPDTILTKNiAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 556 KILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAHRLATVKNAETIIVL 607
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1033-1252 |
3.59e-26 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 109.83 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKW-LRLQT 1111
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVGQEP--ALFGGTIGENIRFG------NPNASWSEVEEAAK----EAYIHnficglprgYETEvgesgiQLSGGQKQR 1179
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGlenlgvPREEMRKRVDEALKlvgmEDFRD---------REPH------LLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1180 IAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT--TTIVVVHRLSTIKKANAIAVVQNGKVSEYGT 1252
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
398-613 |
3.91e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.41 E-value: 3.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVS--FAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVkWLRSQ 475
Cdd:COG1101 2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 M-GMVGQEPVL--FAD-TILENILM----GKENATKkeaidacIAVNAHN---F---ICDLPQGY----DTQVGekgtQL 537
Cdd:COG1101 81 YiGRVFQDPMMgtAPSmTIEENLALayrrGKRRGLR-------RGLTKKRrelFrelLATLGLGLenrlDTKVG----LL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 538 SGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAHRL--AtVKNAETIIVLEQGSVI 613
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMeqA-LDYGNRLIMMHEGRII 228
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1033-1259 |
5.20e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.97 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIG-----GKVMMGGRDL--RDLDLK 1105
Cdd:COG1117 12 IEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPgarveGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1106 WLRLQTALVGQEPALFGGTIGENIRFG---NPNASWSE----VEEAAKEAYIHNficglprgyetEV----GESGIQLSG 1174
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlHGIKSKSEldeiVEESLRKAALWD-----------EVkdrlKKSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1175 GQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVH------RLS--TikkanaiAVVQNGK 1246
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVSdyT-------AFFYLGE 230
|
250
....*....|...
gi 1770234124 1247 VSEYGTHDTLLTN 1259
Cdd:COG1117 231 LVEFGPTEQIFTN 243
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1012-1266 |
6.26e-26 |
|
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: 116.97 E-value: 6.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1012 MNRNPLIDGKGKKIEqskpfdleFKMVNFAYpSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGK 1091
Cdd:TIGR00957 624 IERRTIKPGEGNSIT--------VHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1092 VMMGGrdlrdldlkwlrlQTALVGQEPALFGGTIGENIRFG---NPNASWSEVEEAAKEAYIHNficgLPRGYETEVGES 1168
Cdd:TIGR00957 695 VHMKG-------------SVAYVPQQAWIQNDSLRENILFGkalNEKYYQQVLEACALLPDLEI----LPSGDRTEIGEK 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1169 GIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAI---RKIIKRTTTIVVVHRLSTIKKANAIAVVQNG 1245
Cdd:TIGR00957 758 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGG 837
|
250 260
....*....|....*....|.
gi 1770234124 1246 KVSEYGTHDTLLTNhsNGVYA 1266
Cdd:TIGR00957 838 KISEMGSYQELLQR--DGAFA 856
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
396-616 |
6.31e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 109.71 E-value: 6.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 396 GRLELKNVSFAYPSRMSVPI--LNSLNLVIPSQRISALVGASGAGKSTIFALlerfydpNKGLILLD-GQDI-------- 464
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEFkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQL-------TNGLIISEtGQTIvgdyaipa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 465 ---RTLQVKWLRSQMGMVGQEP--VLFADTILENILMG-------KENATKK--EAIDaciavnahnfICDLPQGYdtqV 530
Cdd:PRK13645 78 nlkKIKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpvnlgenKQEAYKKvpELLK----------LVQLPEDY---V 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 531 GEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATV-KNAETIIVL 607
Cdd:PRK13645 145 KRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVM 224
|
....*....
gi 1770234124 608 EQGSVIEIG 616
Cdd:PRK13645 225 HEGKVISIG 233
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
398-625 |
7.25e-26 |
|
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: 107.63 E-value: 7.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwLRSQMG 477
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH-KRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 M--VGQEPVLFAD-TILENIL-----MGKENATKKEAIDAC-----IAVNAHNficdlpqgydtqvgeKGTQLSGGQKQR 544
Cdd:cd03218 77 IgyLPQEASIFRKlTVEENILavleiRGLSKKEREEKLEELleefhITHLRKS---------------KASSLSGGERRR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 545 IALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIA-HRL-ATVKNAETIIVLEQGSVIEIGDHNKLM 622
Cdd:cd03218 142 VEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
...
gi 1770234124 623 AQE 625
Cdd:cd03218 222 ANE 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
398-614 |
9.72e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.15 E-value: 9.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYP--SRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIrTLQ-----VK 470
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI-TPEtgnknLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 471 WLRSQMGMVGQ--EPVLFADTILENILMGKEN--ATKKEAIDAciavnAHNFICDLpqGYDTQVGEKGT-QLSGGQKQRI 545
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEK-----ALKWLKKV--GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 546 ALARAMIKDPKILLLDEPTSALDPKS-ESLVQQAIDKISKGRTTIVIAHRLATV-KNAETIIVLEQGSVIE 614
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIK 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
419-616 |
9.89e-26 |
|
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: 106.61 E-value: 9.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 419 LNLVIPSQRIsALVGASGAGKSTIFALLERFYDPNKGLILLDGqdirtlqVKWLRSQ-----------MGMVGQEPVLFA 487
Cdd:cd03297 17 IDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG-------TVLFDSRkkinlppqqrkIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 488 D-TILENILMG---KENATKKEAIDACIAVnahnficdlpQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEP 563
Cdd:cd03297 89 HlNVRENLAFGlkrKRNREDRISVDELLDL----------LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 564 TSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATV-KNAETIIVLEQGSVIEIG 616
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
381-630 |
9.90e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 116.42 E-value: 9.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 381 IDPYSTTGRKPETVH-GRLELKNVSFAYpsRMSVP-ILNSLNLVI-PSQRIsALVGASGAGKSTIFALLERFYDPNKGLI 457
Cdd:PTZ00243 1291 IEPASPTSAAPHPVQaGSLVFEGVQMRY--REGLPlVLRGVSFRIaPREKV-GIVGRTGSGKSTLLLTFMRMVEVCGGEI 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 458 LLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKEnATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQL 537
Cdd:PTZ00243 1368 RVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNY 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 538 SGGQKQRIALARAMIK-DPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIG 616
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMG 1526
|
250
....*....|....
gi 1770234124 617 DHNKLMAQEGAYFS 630
Cdd:PTZ00243 1527 SPRELVMNRQSIFH 1540
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
73-339 |
1.08e-25 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 108.94 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 73 FLIIIGCLGALINggsqPWYSylfGNFVNKIALDNDKDQMIKDVrelcVLMSALSGIVVIGAYLQIACWRLVGERLGHRI 152
Cdd:cd18784 3 FFLLAAAVGEIFI----PYYT---GQVIDGIVIEKSQDKFSRAI----IIMGLLAIASSVAAGIRGGLFTLAMARLNIRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 153 RSKYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFIcGYIVGFLK-SWKVSLAVLAVTPLT 231
Cdd:cd18784 72 RNLLFRSIVSQEIGFFDT-VKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAI-GVIVFMFKlSWQLSLVTLIGLPLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 232 MFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLV 311
Cdd:cd18784 150 AIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELT 229
|
250 260
....*....|....*....|....*...
gi 1770234124 312 TYSTWALAFWYGSILVSRNELSGGAAIA 339
Cdd:cd18784 230 ELALTVSTLYYGGHLVITGQISGGNLIS 257
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
395-613 |
1.15e-25 |
|
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: 105.71 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 395 HGRLELKNVSFAYPSRMS---VPILNSLNLVIPSQRISALVGASGAGKSTIFALL--ERFYDPNKGLILLDGQDIRTlqv 469
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 470 KWLRSQMGMVGQEPVLFAD-TILENILMGkenatkkeaidACIavnahnficdlpqgydtqvgeKGtqLSGGQKQRIALA 548
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTlTVRETLMFA-----------AKL---------------------RG--LSGGERKRVSIA 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 549 RAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLAT--VKNAETIIVLEQGSVI 613
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
398-616 |
1.18e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.56 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:PRK13635 6 IRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEP------------VLFAdtiLENILMGKENATKK--EAIDAciaVNAHNFICDLPQgydtqvgekgtQLSGGQKQ 543
Cdd:PRK13635 85 MVFQNPdnqfvgatvqddVAFG---LENIGVPREEMVERvdQALRQ---VGMEDFLNREPH-----------RLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 544 RIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIG 616
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1033-1247 |
1.22e-25 |
|
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: 107.27 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSrpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDL---DLKWLRL 1109
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 QTALVGQEPALFGG-TIGENI---RFGNPNASWSEVEEAAKEAYIHNFIC----GLPRGYETEVGesgiQLSGGQKQRIA 1181
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENVlsgRLGRRSTWRSLFGLFPKEEKQRALAAlervGLLDKAYQRAD----QLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 1182 IARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKV 1247
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1046-1254 |
1.44e-25 |
|
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: 107.04 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1046 PDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwlRLQTALVGQEPALFGG-T 1124
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRHmT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1125 IGENIRFG---NPNASwsEVEEAAKEAYIHNFI-----CGLPRGYETevgesgiQLSGGQKQRIAIARAIVKKSKVLLLD 1196
Cdd:cd03296 91 VFDNVAFGlrvKPRSE--RPPEAEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1197 EATSALDLESEKHVQDAIRKIIKRT--TTIVVVHRLS-TIKKANAIAVVQNGKVSEYGTHD 1254
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPD 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
397-616 |
1.48e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.31 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYD--PN---KGLILLDGQDIRTLQVKW 471
Cdd:PRK14247 3 KIEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 472 LRSQMGMVGQEPVLFAD-TILENILMG-KENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALAR 549
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNlSIFENVALGlKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 550 AMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLA-TVKNAETIIVLEQGSVIEIG 616
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQqAARISDYVAFLYKGQIVEWG 227
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
430-617 |
1.88e-25 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 107.19 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 430 ALVGASGAGKSTIFA---LLErfyDPNKGLILLDGQDIRTL-------------QVKWLRSQMGMVGQEPVLFAD-TILE 492
Cdd:COG4598 38 SIIGSSGSGKSTFLRcinLLE---TPDSGEIRVGGEEIRLKpdrdgelvpadrrQLQRIRTRLGMVFQSFNLWSHmTVLE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 493 NILMG-----KENatKKEAIDACIAvnahnficdlpqgYDTQVG--EKG----TQLSGGQKQRIALARAMIKDPKILLLD 561
Cdd:COG4598 115 NVIEApvhvlGRP--KAEAIERAEA-------------LLAKVGlaDKRdaypAHLSGGQQQRAAIARALAMEPEVMLFD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 562 EPTSALDPKsesLVQQAIDKISK----GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGD 617
Cdd:COG4598 180 EPTSALDPE---LVGEVLKVMRDlaeeGRTMLVVTHEMGFARDvSSHVVFLHQGRIEEQGP 237
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1046-1245 |
2.52e-25 |
|
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: 105.88 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1046 PDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWL----RLQTALVGQEPALF 1121
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1122 GGTIGENIRFGNP--NASWSEVEEAAKeayIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEAT 1199
Cdd:cd03290 92 NATVEENITFGSPfnKQRYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1770234124 1200 SALDLESEKHV-QDAIRKIIK--RTTTIVVVHRLSTIKKANAIAVVQNG 1245
Cdd:cd03290 169 SALDIHLSDHLmQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
398-616 |
2.68e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.58 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDP---NKGLILLDGQDIRTLQVKWLRS 474
Cdd:PRK13640 6 VEFKHVSFTYPDS-KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEP--VLFADTILENILMGKEN------ATKKEAIDACIAVNAHNFICDLPQgydtqvgekgtQLSGGQKQRIA 546
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENravprpEMIKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 547 LARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIG 616
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLkkKNNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1033-1260 |
2.68e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.33 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDldlKWLRL--- 1109
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR---ARRRIgyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 -QTALVGQE-PA-----LFGGTIGENIRFGNPNAS-WSEVEEAAK----EAYIHNFICglprgyetevgesgiQLSGGQK 1177
Cdd:COG1121 81 pQRAEVDWDfPItvrdvVLMGRYGRRGLFRRPSRAdREAVDEALErvglEDLADRPIG---------------ELSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1178 QRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVqNGKVSEYGTHDT 1255
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVtHDLGAVREyFDRVLLL-NRGLVAHGPPEE 224
|
....*
gi 1770234124 1256 LLTNH 1260
Cdd:COG1121 225 VLTPE 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
416-616 |
2.74e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.83 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 416 LNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKW--LRSQMGMVGQEP--VLFADTIL 491
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 492 ENILMG------KENATKKEAIDACIAVNahnficdLPqgYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTS 565
Cdd:PRK13637 103 KDIAFGpinlglSEEEIENRVKRAMNIVG-------LD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 566 ALDPKSESLVQQAIDKISK--GRTTIVIAHRLATV-KNAETIIVLEQGSVIEIG 616
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQG 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
398-625 |
5.19e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.05 E-value: 5.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAY---PSRMSVPilnslnlVIPSQRIsALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwlRS 474
Cdd:PRK10771 2 LKLTDITWLYhhlPMRFDLT-------VERGERV-AILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFAD-TILENILMG-----KENATKKEAIDAcIA--VNAHNFICDLPqgydtqvgekgTQLSGGQKQRIA 546
Cdd:PRK10771 72 PVSMLFQENNLFSHlTVAQNIGLGlnpglKLNAAQREKLHA-IArqMGIEDLLARLP-----------GQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 547 LARAMIKDPKILLLDEPTSALDP--KSE--SLVQQAIDKisKGRTTIVIAHRLA-TVKNAETIIVLEQGSVIEIGDHNKL 621
Cdd:PRK10771 140 LARCLVREQPILLLDEPFSALDPalRQEmlTLVSQVCQE--RQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDEL 217
|
....
gi 1770234124 622 MAQE 625
Cdd:PRK10771 218 LSGK 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
398-616 |
7.18e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.62 E-value: 7.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQvKWLRSQM- 476
Cdd:PRK13548 3 LEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWS-PAELARRr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQEPVL-FADTILENILMGK-----ENATKKEAIDACIAvnahnfICDLpQGYdtqVGEKGTQLSGGQKQRIALARA 550
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMGRaphglSRAEDDALVAAALA------QVDL-AHL---AGRDYPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 551 MI------KDPKILLLDEPTSALDPKSeslvQQAIDKISKGRTT------IVIAHRLA-TVKNAETIIVLEQGSVIEIG 616
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAH----QHHVLRLARQLAHerglavIVVLHDLNlAARYADRIVLLHQGRLVADG 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1033-1249 |
1.12e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.98 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPsrPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDL---DLKWLRL 1109
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 QTALVGQEPALFGG-TIGENIRF-----GnpnASWSEVEEAAKEAyihnficgLprgyeTEVGESG------IQLSGGQK 1177
Cdd:COG2884 80 RIGVVFQDFRLLPDrTVYENVALplrvtG---KSRKEIRRRVREV--------L-----DLVGLSDkakalpHELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1178 QRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKKANA-IAVVQNGKVSE 1249
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
413-611 |
1.25e-24 |
|
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: 103.56 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 413 VPILNSLNLVIPSQRISALVGASGAGKSTIF--------ALLERFYDPNKGLILLDGQDIRTLQvkwlRSQMGMVGQEPV 484
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLlailgemqTLEGKVHWSNKNESEPSFEATRSRN----RYSVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 485 LFADTILENILMGKE-NATK-KEAIDACiavNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDE 562
Cdd:cd03290 90 LLNATVEENITFGSPfNKQRyKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 563 PTSALDPK-SESLVQQAIDKISKG--RTTIVIAHRLATVKNAETIIVLEQGS 611
Cdd:cd03290 167 PFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
416-702 |
1.26e-24 |
|
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: 105.94 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 416 LNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIrTLQVKWLRSQMGMVGQEPVLFAD-TILENI 494
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV-VREPRKVRRSIGIVPQYASVDEDlTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 495 -LMGKENATKKEAIDACIAVNAHNFicDLPQGYDTQVGekgtQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSES 573
Cdd:TIGR01188 88 eMMGRLYGLPKDEAEERAEELLELF--ELGEAADRPVG----TYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 574 LVQQAIDKISK-GRTTIVIAHRLATV-KNAETIIVLEQGSVIEIGDHNKLMAQEGAyfsliklatEAISSNPVSKKGKTV 651
Cdd:TIGR01188 162 AIWDYIRALKEeGVTILLTTHYMEEAdKLCDRIAIIDHGRIIAEGTPEELKRRLGK---------DTLESRPRDIQSLKV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 652 INQETSSNC--DLLKQNHVYEISPSGYMKSIQDANQ-PESAKLNKIKSYKIREV 702
Cdd:TIGR01188 233 EVSMLIAELgeTGLGLLAVTVDSDRIKILVPDGDETvPEIVEAAIRNGIRIRSI 286
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
398-623 |
1.27e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.56 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEP--VLFADTILENILMGKENA--TKKEAI----DACIAVNAHNFICDLPqgydtqvgekgTQLSGGQKQRIALAR 549
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQgiPREEMIkrvdEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 550 AMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGR--TTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMA 623
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
398-616 |
1.71e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.43 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:COG4559 2 LEAENLSVRLGGR---TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVL-FADTILENILMG-----KENATKKEAIDACIAvnahnfICDLpQGYdtqVGEKGTQLSGGQKQRIALARAM 551
Cdd:COG4559 79 VLPQHSSLaFPFTVEEVVALGraphgSSAAQDRQIVREALA------LVGL-AHL---AGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 552 I-------KDPKILLLDEPTSALDPKSeslvQQAIDKI-----SKGRTTIVIAHRLatvkN-----AETIIVLEQGSVIE 614
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDLAH----QHAVLRLarqlaRRGGGVVAVLHDL----NlaaqyADRILLLHQGRLVA 220
|
..
gi 1770234124 615 IG 616
Cdd:COG4559 221 QG 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1034-1252 |
1.82e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 106.42 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1034 EFKMVNFAYP-SRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRL--- 1109
Cdd:PRK11153 3 ELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 QTALVGQEPALFGG-TIGENIRFGNPNASWSEVEEAAKEAYIhnficgLPRgyeteVGESG------IQLSGGQKQRIAI 1182
Cdd:PRK11153 83 QIGMIFQHFNLLSSrTVFDNVALPLELAGTPKAEIKARVTEL------LEL-----VGLSDkadrypAQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1183 ARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR-TTTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYGT 1252
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLItHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1038-1227 |
1.99e-24 |
|
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: 102.72 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1038 VNFAYPSRPDVivLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRdldlKWLRLQTA-LVGQ 1116
Cdd:cd03226 5 ISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK----AKERRKSIgYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1117 EP--ALFGGTIGENIRFGNPNASWS--EVEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIAIARAIVKKSKV 1192
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190
....*....|....*....|....*....|....*
gi 1770234124 1193 LLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV 1227
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVI 182
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
835-1304 |
2.37e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 111.61 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 835 SVLFMGLSSAAVGLSVSFYLEWRL--------ALLATIVTPFTlgasyfSLIINIGSKLDNDSF---DKASGIASAAVSN 903
Cdd:PLN03232 415 AEQLHGLWSAPFRIIVSMVLLYQQlgvaslfgSLILFLLIPLQ------TLIVRKMRKLTKEGLqwtDKRVGIINEILAS 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 904 IRTVTTLAtQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMYSAYTLVlFFGAYLVKKdytkfGDVYKIFLILVL 983
Cdd:PLN03232 489 MDTVKCYA-WEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLV-SFGVFVLLG-----GDLTPARAFTSL 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 984 STFSVGQFAgLAPDTSMASTAIPAVFEIMNRNPLIDGKGKKIEQSKPFD-----LEFKMVNFAYPSRPDVIVLREFCLKV 1058
Cdd:PLN03232 562 SLFAVLRSP-LNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQpgapaISIKNGYFSWDSKTSKPTLSDINLEI 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1059 KGGTMVAVVGGSGSGKSTVIwlmqrfydpiggKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGN---PN 1135
Cdd:PLN03232 641 PVGSLVAIVGGTGEGKTSLI------------SAMLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSdfeSE 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1136 ASWSEVEEAAKEAYIHNFicglPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDA-I 1214
Cdd:PLN03232 709 RYWRAIDVTALQHDLDLL----PGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScM 784
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1215 RKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTNhsngvyATLVHSEMEaNADHFSLVQQPVTDPE--- 1291
Cdd:PLN03232 785 KDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS------GSLFKKLME-NAGKMDATQEVNTNDEnil 857
|
490
....*....|...
gi 1770234124 1292 FLASEAKMNRSDR 1304
Cdd:PLN03232 858 KLGPTVTIDVSER 870
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
398-612 |
3.37e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 103.60 E-value: 3.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLiLLDGQ--------DIRtlqv 469
Cdd:PRK11247 13 LLLNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTaplaeareDTR---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 470 kwlrsqmgMVGQEPVLFA-DTILENILMGKENATKKEAIDACIAVnahnficdlpqGYDTQVGEKGTQLSGGQKQRIALA 548
Cdd:PRK11247 85 --------LMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAV-----------GLADRANEWPAALSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 549 RAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAHRLA-TVKNAETIIVLEQGSV 612
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
398-616 |
3.43e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.06 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSVpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEP------------VLFAdtiLENILMGKENaTKKEAIDACIAVNAHNFICDLPQGydtqvgekgtqLSGGQKQRI 545
Cdd:PRK13648 87 IVFQNPdnqfvgsivkydVAFG---LENHAVPYDE-MHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 546 ALARAMIKDPKILLLDEPTSALDPKSE----SLVQQAidKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIG 616
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARqnllDLVRKV--KSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1034-1228 |
3.48e-24 |
|
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: 102.23 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1034 EFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDldlKWLRL---- 1109
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKRIgyvp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 QTALV-------GQEPALFGGTIGENIRFGNPNASWSEVEEAAKEayihnficglprgyeteVGESGI------QLSGGQ 1176
Cdd:cd03235 75 QRRSIdrdfpisVRDVVLMGLYGHKGLFRRLSKADKAKVDEALER-----------------VGLSELadrqigELSGGQ 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1177 KQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVH 1228
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVT 189
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1033-1247 |
3.50e-24 |
|
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: 100.94 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRlQTA 1112
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGG-TIGENIRfgnpnaswseveeaakeayihnficglprgyetevgesgiqLSGGQKQRIAIARAIVKKSK 1191
Cdd:cd03230 77 YLPEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1192 VLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKV 1247
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
398-570 |
3.73e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.18 E-value: 3.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRtlQVKWLRSQMG 477
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENILMG-KENATKKEAI-----DACIAVNAHNFIcdlpqgydtqvGEKGTQLSGGQKQRIALARA 550
Cdd:PRK09452 90 TVFQSYALFPHmTVFENVAFGlRMQKTPAAEItprvmEALRMVQLEEFA-----------QRKPHQLSGGQQQRVAIARA 158
|
170 180
....*....|....*....|
gi 1770234124 551 MIKDPKILLLDEPTSALDPK 570
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYK 178
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
75-371 |
4.08e-24 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 104.43 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 75 IIIGCLGALINGGSQPWYSYLFGNFVNKIALDNDKDQMIKdvreLCVLMSALSGIVVIGAYLQIACWRLVGERLGHRIRS 154
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLL----VPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 155 KYLRAVLRQDVSFFDtDISTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFC 234
Cdd:cd18552 77 DLFDKLLRLPLSFFD-RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 235 gvaykAVYVG-----LAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIY 309
Cdd:cd18552 156 -----IRRIGkrlrkISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLME 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 310 LVTYSTWALAFWYGSILVSRNELSGGAAIAcFFGvtiggrglALSLSY---------FAQFAQGTVAASKV 371
Cdd:cd18552 231 LLGAIAIALVLWYGGYQVISGELTPGEFIS-FIT--------ALLLLYqpikrlsnvNANLQRGLAAAERI 292
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
415-624 |
4.19e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.51 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 415 ILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL-------------QVKWLRSQMGMVGQ 481
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 482 EPVLFAD-TILENILMGKENA---TKKEAIDACIAVNAHNFICDLPQGydtqvgEKGTQLSGGQKQRIALARAMIKDPKI 557
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPIQVlglSKQEARERAVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 558 LLLDEPTSALDPKSESLVQQAIDKIS-KGRTTIVIAHRLATVKNAET-IIVLEQGSVIEIGDHNKLMAQ 624
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1054-1251 |
5.84e-24 |
|
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: 101.42 E-value: 5.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1054 FCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwlRLQTALVGQEPALFGG-TIGENIRFG 1132
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1133 -NPNASWSE-----VEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLES 1206
Cdd:cd03298 95 lSPGLKLTAedrqaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1770234124 1207 EKHVQDAIRKIIKRT--TTIVVVHRLSTIKK-ANAIAVVQNGKVSEYG 1251
Cdd:cd03298 164 RAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
398-616 |
5.95e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 103.23 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSVpiLNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWL--RSQ 475
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MGMVGQEP--VLFADTILENILMG------KENATKKEAIDACIAVNAHNFICDLPQgydtqvgekgtQLSGGQKQRIAL 547
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 548 ARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIA-HRLATV-KNAETIIVLEQGSVIEIG 616
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEG 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
420-624 |
6.34e-24 |
|
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: 105.18 E-value: 6.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 420 NLVIPSQRISALVGASGAGKSTIF---ALLERfydPNKGLILLDGqdiRTLQ----VKWL---RSQMGMVGQEPVLFAD- 488
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLraiAGLER---PDSGRIRLGG---EVLQdsarGIFLpphRRRIGYVFQEARLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 489 TILENILMGKENATK---KEAIDAciavnahnfICDL----------PQgydtqvgekgtQLSGGQKQRIALARAMIKDP 555
Cdd:COG4148 93 SVRGNLLYGRKRAPRaerRISFDE---------VVELlgighlldrrPA-----------TLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 556 KILLLDEPTSALDPKS--------ESLVQQ----------AIDKISkgrttiviahRLATvknaeTIIVLEQGSVIEIGD 617
Cdd:COG4148 153 RLLLMDEPLAALDLARkaeilpylERLRDEldipilyvshSLDEVA----------RLAD-----HVVLLEQGRVVASGP 217
|
....*..
gi 1770234124 618 HNKLMAQ 624
Cdd:COG4148 218 LAEVLSR 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1033-1226 |
6.81e-24 |
|
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: 101.33 E-value: 6.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPsrPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLD---LKWLRL 1109
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 QTALVGQEPALFGG-TIGENIRF-----GNPNASWSEVEEAAKEayihnfICGLpRGYETEVGEsgiQLSGGQKQRIAIA 1183
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFalevtGVPPREIRKRVPAALE------LVGL-SHKHRALPA---ELSGGEQQRVAIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1770234124 1184 RAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVV 1226
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVV 191
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1047-1262 |
7.65e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.82 E-value: 7.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRF---YDP---IGGKVMMGGRDLRDLDLKWLRLQTALVGQEPAL 1120
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1121 FGG-TIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEAT 1199
Cdd:PRK14246 102 FPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1200 SALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTNHSN 1262
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1044-1226 |
7.82e-24 |
|
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: 101.02 E-value: 7.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1044 SRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRlQTALVGQEPALFGG 1123
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRR-RLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 -TIGENIRF----GNPNASWSEVEEAAKEAyihnficGLPRGYETEVGesgiQLSGGQKQRIAIARAIVKKSKVLLLDEA 1198
Cdd:COG4133 90 lTVRENLRFwaalYGLRADREAIDEALEAV-------GLAGLADLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180
....*....|....*....|....*...
gi 1770234124 1199 TSALDLESEKHVQDAIRKIIKRTTTIVV 1226
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1050-1256 |
1.02e-23 |
|
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: 103.01 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRdlrdldlkwlrlqTALVGQEPALFGGTIGENI 1129
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1130 RFGnpnASWSEV--EEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESE 1207
Cdd:cd03291 119 IFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1208 KHVQDA-IRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTL 1256
Cdd:cd03291 196 KEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
398-635 |
1.48e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.37 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL-QVKWLRSQM 476
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQEP--VLFADTILENILMGKEN-----ATKKEAIDACIAvnahnficdlPQGYDTQVGEKGTQLSGGQKQRIALAR 549
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENlclppIEIRKRVDRALA----------EIGLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 550 AMIKDPKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAY 628
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQ 229
|
250
....*....|...
gi 1770234124 629 F------SLIKLA 635
Cdd:PRK13644 230 TlgltppSLIELA 242
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1050-1252 |
1.60e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 104.64 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTalVGQEPALFGG-TIGEN 1128
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNT--VFQSYALFPHmTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1129 IRFG-----NPNASWSE-VEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSAL 1202
Cdd:PRK09452 107 VAFGlrmqkTPAAEITPrVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1203 DLESEKHVQDAIrKIIKRT---TTIVVVH-RLSTIKKANAIAVVQNGKVSEYGT 1252
Cdd:PRK09452 176 DYKLRKQMQNEL-KALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
398-625 |
1.63e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQ--DIRTLQVKWLRSQ 475
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MGMVGQEP--VLFADTILENILMGKENAT--KKEAIDACIAVNAHNFICDLPqgydtqvgEKGTQ-LSGGQKQRIALARA 550
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLK--------DKPTHcLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 551 MIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGR-TTIVIA-HRLATVK-NAETIIVLEQGSVIEIGDHNKLMAQE 625
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELgLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
398-616 |
1.64e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.41 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYpsRMSVPI----LNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDI----RTLQV 469
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 470 KWLRSQMGMVGQ--EPVLFADTILENILMGKEN---------ATKKEAIDACiavnahnficdlpqGYDTQVGEKGT-QL 537
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgvseedakQKAREMIELV--------------GLPEELLARSPfEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 538 SGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAHRLATVKN-AETIIVLEQGSVIE 614
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFL 226
|
..
gi 1770234124 615 IG 616
Cdd:PRK13634 227 QG 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
387-617 |
2.07e-23 |
|
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: 106.31 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 387 TGRKPETVHGR---LELKNVSFAYPSRMS--------VPILNSLNLVIPSQRISALVGASGAGKSTI-FALLeRFyDPNK 454
Cdd:COG4172 262 RGDPRPVPPDApplLEARDLKVWFPIKRGlfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RL-IPSE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 455 GLILLDGQDIRTL---QVKWLRSQMGMVGQEPvlFA---------DTILENILMGKENATKKE----AIDACIAVnahnf 518
Cdd:COG4172 340 GEIRFDGQDLDGLsrrALRPLRRRMQVVFQDP--FGslsprmtvgQIIAEGLRVHGPGLSAAErrarVAEALEEV----- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 519 icdlpqGYDTQVGEK-GTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDpKSeslVQ-QAID---KISK--GRTTIVI 591
Cdd:COG4172 413 ------GLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VS---VQaQILDllrDLQRehGLAYLFI 482
|
250 260
....*....|....*....|....*..
gi 1770234124 592 AHRLATVKN-AETIIVLEQGSVIEIGD 617
Cdd:COG4172 483 SHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
415-623 |
2.40e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 100.98 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 415 ILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDI---RTL-----QVKWLRSQMGMVGQEPVLF 486
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLsqqkgLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 487 AD-TILENILMGKEnATKKEAIDACIAvnahnficdLPQGYDTQVGEKGTQ------LSGGQKQRIALARAMIKDPKILL 559
Cdd:PRK11264 98 PHrTVLENIIEGPV-IVKGEPKEEATA---------RARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 560 LDEPTSALDPKsesLVQQAIDKI----SKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGDHNKLMA 623
Cdd:PRK11264 168 FDEPTSALDPE---LVGEVLNTIrqlaQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
398-617 |
2.54e-23 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 100.29 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWL-RSQM 476
Cdd:TIGR03410 1 LEVSNLNVYYGQSH---ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQEPVLFAD-TILENILMGKEN-ATKKEAIDAciavnahnFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKD 554
Cdd:TIGR03410 78 AYVPQGREIFPRlTVEENLLTGLAAlPRRSRKIPD--------EIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 555 PKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGD 617
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGA 215
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
398-613 |
2.64e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 101.70 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAY---PSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKW-LR 473
Cdd:PRK13633 5 IKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 474 SQMGMVGQEP--VLFADTILENILMGKEN-ATKKEAI-----DACIAVNAHNFICDLPQgydtqvgekgtQLSGGQKQRI 545
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlGIPPEEIrervdESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 546 ALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKNAETIIVLEQGSVI 613
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
398-624 |
2.74e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.73 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEP--VLFADTILENILMGKEN-----ATKKEAIDACIA-VNAHNFICDLPqgydtqvgekgTQLSGGQKQRIALAR 549
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgiphEEMKERVNEALElVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 550 AMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQ 624
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
430-624 |
3.66e-23 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 102.50 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 430 ALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL---QVKWLRSQMGMVGQEPvlFA---------DTILE----- 492
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDP--YAslnprmtvgDIIAEplrih 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 493 NILMGKEnatKKEAIDACIAvnahnficdlpqgydtQVGEKGT-------QLSGGQKQRIALARAMIKDPKILLLDEPTS 565
Cdd:COG4608 126 GLASKAE---RRERVAELLE----------------LVGLRPEhadryphEFSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 566 ALDpKSeslVQ-QAID-----KISKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGDHNKLMAQ 624
Cdd:COG4608 187 ALD-VS---IQaQVLNlledlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
398-629 |
3.96e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.88 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDI--RTLQvkwlRSQ 475
Cdd:PRK11432 7 VVLKNITKRFGSNT---VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQ----QRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MGMVGQEPVLFAD-TILENI-----LMGKENATKKEAIDACIAvnahnfICDLPQGYDTQVgekgTQLSGGQKQRIALAR 549
Cdd:PRK11432 80 ICMVFQSYALFPHmSLGENVgyglkMLGVPKEERKQRVKEALE------LVDLAGFEDRYV----DQISGGQQQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 550 AMIKDPKILLLDEPTSALDPkseSLVQQAIDKISKGRTTIVIAHRLATVKNAE------TIIVLEQGSVIEIGDHNKLMA 623
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDA---NLRRSMREKIRELQQQFNITSLYVTHDQSEafavsdTVIVMNKGKIMQIGSPQELYR 226
|
....*.
gi 1770234124 624 QEGAYF 629
Cdd:PRK11432 227 QPASRF 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1033-1252 |
5.59e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.86 E-value: 5.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYP--SRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQ 1110
Cdd:PRK13635 6 IRVEHISFRYPdaATY---ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1111 TALVGQEP--ALFGGTIGENIRFG--NPNASWSE----VEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIAI 1182
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGleNIGVPREEmverVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1183 ARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKII--KRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGT 1252
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1019-1256 |
7.47e-23 |
|
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: 106.92 E-value: 7.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1019 DGKGKKIEQSKPFDLEFKMVN------FAYPSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKV 1092
Cdd:TIGR01271 404 EGIGELFEKIKQNNKARKQPNgddglfFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1093 MMGGRdlrdldlkwlrlqTALVGQEPALFGGTIGENIRFGnpnASWSEVE--EAAKEAYIHNFICGLPRGYETEVGESGI 1170
Cdd:TIGR01271 484 KHSGR-------------ISFSPQTSWIMPGTIKDNIIFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGI 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1171 QLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHV-QDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSE 1249
Cdd:TIGR01271 548 TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYF 627
|
....*..
gi 1770234124 1250 YGTHDTL 1256
Cdd:TIGR01271 628 YGTFSEL 634
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
398-624 |
7.87e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 100.62 E-value: 7.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYpsRMSVPI----LNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDI----RTLQV 469
Cdd:PRK13646 3 IRFDNVSYTY--QKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 470 KWLRSQMGMVGQ--EPVLFADTILENILMGKENAtkKEAIDAcIAVNAHNFICDLpqGYDTQVGEKGT-QLSGGQKQRIA 546
Cdd:PRK13646 81 RPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNF--KMNLDE-VKNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 547 LARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKIS--KGRTTIVIAHRLATV-KNAETIIVLEQGSVIEIGDHNKLMA 623
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
.
gi 1770234124 624 Q 624
Cdd:PRK13646 236 D 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
398-568 |
8.08e-23 |
|
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: 99.05 E-value: 8.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRM-SVPILNSLNLVIPSQRISALVGASGAGKSTIFAL---LERfydPNKGLILLDGQDIRTL---QVK 470
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALdedARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 471 WLRSQ-MGMVGQE----PVLfadTILENILMGKENATKKEAIDACIAVNAhnficdlpqgydtQVGEKG------TQLSG 539
Cdd:COG4181 86 RLRARhVGFVFQSfqllPTL---TALENVMLPLELAGRRDARARARALLE-------------RVGLGHrldhypAQLSG 149
|
170 180
....*....|....*....|....*....
gi 1770234124 540 GQKQRIALARAMIKDPKILLLDEPTSALD 568
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1034-1259 |
1.07e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 99.68 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1034 EFKMVNFAYPSRpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTAL 1113
Cdd:PRK13632 9 KVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1114 VGQEP--ALFGGTIGENIRFG------NPNASWSEVEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIAIARA 1185
Cdd:PRK13632 88 IFQNPdnQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1186 IVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT--TTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1050-1259 |
1.17e-22 |
|
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: 98.28 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDL-KWLRLQTALVGQEPALFGG-TIGE 1127
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1128 NIRFGNPNASWSEVEEAAKEAYiHNFicglPRGYE---TEVGesgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDL 1204
Cdd:cd03224 95 NLLLGAYARRRAKRKARLERVY-ELF----PRLKErrkQLAG----TLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1205 ESEKHVQDAIRKIIKRTTTIVVV-HRLstiKKANAIA----VVQNGKVSEYGTHDTLLTN 1259
Cdd:cd03224 166 KIVEEIFEAIRELRDEGVTILLVeQNA---RFALEIAdrayVLERGRVVLEGTAAELLAD 222
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
415-610 |
1.44e-22 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 97.78 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 415 ILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL---QVKWLRSQMGMVGQEPVLF-ADTI 490
Cdd:TIGR02982 20 VLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGAskkQLVQLRRRIGYIFQAHNLLgFLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 491 LENILMGKE---NATKKEAIDACIAVnahnficdLPQ-GYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSA 566
Cdd:TIGR02982 100 RQNVQMALElqpNLSYQEARERARAM--------LEAvGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1770234124 567 LDPKSESLVQQAIDKISK--GRTTIVIAH--RLATVknAETIIVLEQG 610
Cdd:TIGR02982 172 LDSKSGRDVVELMQKLAKeqGCTILMVTHdnRILDV--ADRILQMEDG 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
400-568 |
1.55e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 400 LKNVSFAYPSRmsvPILNSLNLVI-PSQRIsALVGASGAGKSTIFALLERFYDPNKGLILLDGqDIRtlqvkwlrsqMGM 478
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSInPGDRI-GLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 479 VGQEPVLFAD-TILENILMG----------KENATKK------------EAIDACIAVNAHNF------ICD---LPQG- 525
Cdd:COG0488 66 LPQEPPLDDDlTVLDTVLDGdaelraleaeLEELEAKlaepdedlerlaELQEEFEALGGWEAearaeeILSglgFPEEd 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1770234124 526 YDTQVGEkgtqLSGGQKQRIALARAMIKDPKILLLDEPTSALD 568
Cdd:COG0488 146 LDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-621 |
1.65e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.96 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPN-----KGLILLDGQDI--RTLQVK 470
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 471 WLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARA 550
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 551 MIKDPKILLLDEPTSALDP----KSESLVQQAidKISKGRTTIVIAHRLATVKNAETIIVLEQGS------VIEIGDHNK 620
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPiasmKVESLIQSL--RLRSELTMVIVSHNLHQVSRLSDFTAFFKGNenrigqLVEFGLTKK 242
|
.
gi 1770234124 621 L 621
Cdd:PRK14258 243 I 243
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1056-1259 |
1.95e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 100.13 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDP---IGGKVMMGGRDLRDLD---LKWLRLQT-ALVGQEP--AL-----F 1121
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekeLRKIRGREiQMIFQDPmtSLnpvmtV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1122 GGTIGENIRFGNPnASWSEVEEAAKEA---------------YIHnficglprgyetevgesgiQLSGGQKQRIAIARAI 1186
Cdd:COG0444 106 GDQIAEPLRIHGG-LSKAEARERAIELlervglpdperrldrYPH-------------------ELSGGMRQRVMIARAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1187 VKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT-TTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:COG0444 166 ALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLAILFItHDLGVVAEiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-621 |
2.25e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 98.38 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPN-----KGLILLDGQDIRTLQVKWL 472
Cdd:PRK14267 5 IETVNLRVYYGSNH---VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 473 --RSQMGMVGQEPVLFAD-TILENILMG-KEN--ATKKEAIDACIAVNAHNfiCDLPQGYDTQVGEKGTQLSGGQKQRIA 546
Cdd:PRK14267 82 evRREVGMVFQYPNPFPHlTIYDNVAIGvKLNglVKSKKELDERVEWALKK--AALWDEVKDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 547 LARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLA-TVKNAETIIVLEQGSVIEIGDHNKL 621
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAqAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
402-621 |
2.71e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.20 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 402 NVSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERF---YDPN---KGLILLDGQDIRTLQVKWLRSQ 475
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MGMVGQEPVLFAD-TILENILMG------KENATKKEAIDACIavnahNFICDLPQGYDtQVGEKGTQLSGGQKQRIALA 548
Cdd:PRK14246 92 VGMVFQQPNPFPHlSIYDNIAYPlkshgiKEKREIKKIVEECL-----RKVGLWKEVYD-RLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 549 RAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATV-KNAETIIVLEQGSVIEIGDHNKL 621
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
402-632 |
3.31e-22 |
|
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: 98.39 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 402 NVSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLrsqmgMVGq 481
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWI-----MPG- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 482 epvlfadTILENILMG--KENATKKEAIDACiavNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILL 559
Cdd:cd03291 113 -------TIKENIIFGvsYDEYRYKSVVKAC---QLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 560 LDEPTSALDPKSESLV-QQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSLI 632
Cdd:cd03291 183 LDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
398-595 |
4.36e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.55 E-value: 4.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSVpilNSLNLVIPSQRISALVGASGAGKSTIFALLERFYD--PN---KGLILLDGQDIRTLQVK-- 470
Cdd:PRK14243 11 LRTENLNVYYGSFLAV---KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYAPDVDpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 471 WLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDACIAVNahnficdLPQG--YDtQVGEK----GTQLSGGQKQR 544
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGARINGYKGDMDELVERS-------LRQAalWD-EVKDKlkqsGLSLSGGQQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 545 IALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRL 595
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1056-1259 |
5.06e-22 |
|
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: 102.07 E-value: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKST----VIWLMqrfydPIGGKVMMGGRDLRDLD---LKWLRLQTALVGQEPalFGG----- 1123
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSlsprm 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 ----TIGENIRFGNPNASWSEVEEAAKEA-------------YIHNFicglprgyetevgesgiqlSGGQKQRIAIARAI 1186
Cdd:COG4172 380 tvgqIIAEGLRVHGPGLSAAERRARVAEAleevgldpaarhrYPHEF-------------------SGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1187 VKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT--TTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:COG4172 441 ILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
398-625 |
5.36e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.01 E-value: 5.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:PRK11231 3 LRTENLTVGYGTK---RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVlfadtILENI---------------LMGKENATKKEAIDACIAvnahnficdlpqgyDTQVGE----KGTQLS 538
Cdd:PRK11231 80 LLPQHHL-----TPEGItvrelvaygrspwlsLWGRLSAEDNARVNQAME--------------QTRINHladrRLTDLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 539 GGQKQRIALARAMIKDPKILLLDEPTSALDPKSE----SLVQQAIDkisKGRTTIVIAHRL-ATVKNAETIIVLEQGSVI 613
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQvelmRLMRELNT---QGKTVVTVLHDLnQASRYCDHLVVLANGHVM 217
|
250
....*....|..
gi 1770234124 614 EIGDHNKLMAQE 625
Cdd:PRK11231 218 AQGTPEEVMTPG 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
397-568 |
6.67e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 97.24 E-value: 6.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAYP-SRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwlRsq 475
Cdd:COG4525 3 MLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 mGMVGQEPVLFA-DTILENI-----LMGKENATKKEAIDACIAvnahnficdlpqgydtQVGEKGT------QLSGGQKQ 543
Cdd:COG4525 79 -GVVFQKDALLPwLNVLDNVafglrLRGVPKAERRARAEELLA----------------LVGLADFarrriwQLSGGMRQ 141
|
170 180
....*....|....*....|....*
gi 1770234124 544 RIALARAMIKDPKILLLDEPTSALD 568
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALD 166
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1032-1252 |
7.73e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 97.78 E-value: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1032 DLEFKMVNFAY-PSRP-DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDL----RDLDLK 1105
Cdd:PRK13634 2 DITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1106 WLRLQTALVGQ--EPALFGGTIGENIRFGNPNASWSEvEEAAKEAYIHNFICGLPrgyETEVGESGIQLSGGQKQRIAIA 1183
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLP---EELLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1184 RAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT--TTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGT 1252
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
420-622 |
7.75e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 99.72 E-value: 7.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 420 NLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRS----QMGMVGQEPVLFAD-TILENI 494
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 495 LMGKENA------TKKEAIDACIAVNAHNFICDLPQgydtqvgekgtQLSGGQKQRIALARAMIKDPKILLLDEPTSALD 568
Cdd:PRK10070 128 AFGMELAginaeeRREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 569 PKSESLVQQAIDKISKG--RTTIVIAHRL-ATVKNAETIIVLEQGSVIEIGDHNKLM 622
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
121-354 |
8.32e-22 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 97.55 E-value: 8.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 121 VLMSALSGIVVIGAYLQIACWRLVGERLGHRIRSKYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGDKMSQFI 200
Cdd:cd18575 40 LLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFET-TRTGEVLSRLTTDTTLIQTVVGSSLSIAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 201 YHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFCGVAYkAVYVGLAAKEV-NSYKKAGSIAEQAIGSIRTVFSFVAEDSL 279
Cdd:cd18575 119 RNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILF-GRRVRRLSRASqDRLADLSAFAEETLSAIKTVQAFTREDAE 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 280 AARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYSTWALAFWYGSILVSRNELSGGAAIA-CFFGVTIGGRGLALS 354
Cdd:cd18575 198 RQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQfVFYAVLAAGSVGALS 273
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
398-616 |
1.07e-21 |
|
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: 95.92 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVI-PSQRIsALVGASGAGKSTIFALLERFYDPNKG--LILLD----GQDIRtlqvk 470
Cdd:COG1119 4 LELRNVTVRRGGK---TILDDISWTVkPGEHW-AILGPNGAGKSTLLSLITGDLPPTYGndVRLFGerrgGEDVW----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 471 WLRSQMGMVG---QEPVLFADTILENILMGKENATkkeaidaciavnahnficDLPQGYDTQ-------------VGEKG 534
Cdd:COG1119 75 ELRKRIGLVSpalQLRFPRDETVLDVVLSGFFDSI------------------GLYREPTDEqrerarellellgLAHLA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 535 ----TQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIV-IAHRL----ATVKNAeti 604
Cdd:COG1119 137 drpfGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVlVTHHVeeipPGITHV--- 213
|
250
....*....|..
gi 1770234124 605 IVLEQGSVIEIG 616
Cdd:COG1119 214 LLLKDGRVVAAG 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1051-1251 |
1.66e-21 |
|
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: 94.67 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1051 LREFCLKVK---GGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRD----LDLKWLRLQTALVGQEPALFGG 1123
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 -TIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETevgesgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSAL 1202
Cdd:cd03297 90 lNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPA-------QLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1203 DLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYG 1251
Cdd:cd03297 163 DRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
398-617 |
2.10e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.23 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSVPI--LNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLI----LLDGQDIRTLQV-- 469
Cdd:PRK13631 22 LRVKNLYCVFDEKQENELvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 470 ----------KWLRSQMGMVGQEP--VLFADTILENILMG-------KENATKKEAIdaciavnahnficdlpqgYDTQV 530
Cdd:PRK13631 102 npyskkiknfKELRRRVSMVFQFPeyQLFKDTIEKDIMFGpvalgvkKSEAKKLAKF------------------YLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 531 GEKGT-------QLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAI-DKISKGRTTIVIAHRLATV-KNA 601
Cdd:PRK13631 164 GLDDSylerspfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHVlEVA 243
|
250
....*....|....*.
gi 1770234124 602 ETIIVLEQGSVIEIGD 617
Cdd:PRK13631 244 DEVIVMDKGKILKTGT 259
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1033-1300 |
2.13e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.44 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAY-PSRP-DVIVLREFCLKVKGGTMVAVVGGSGSGKSTviwLMQRF---YDPIGGKVMMGGRDLR----DLD 1103
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKST---LMQHFnalLKPSSGTITIAGYHITpetgNKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1104 LKWLRLQTALVGQ--EPALFGGTIGENIRFGNPNASWSEvEEAAKEAYIHNFICGLPrgyETEVGESGIQLSGGQKQRIA 1181
Cdd:PRK13641 80 LKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE-DEAKEKALKWLKKVGLS---EDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1182 IARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT-TTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGhTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSD 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1770234124 1260 -------HSNGVYATLVHSEMEANAdhFSLVQQPVTDPEfLASEAKMN 1300
Cdd:PRK13641 236 kewlkkhYLDEPATSRFASKLEKGG--FKFSEMPLTIDE-LVDGIKNN 280
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
398-614 |
2.30e-21 |
|
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: 93.82 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWlrSQMG 477
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENI-LMGKENATKKEAIDACIAVnahnficdlpQGYDTQVGEKGTQLSGGQKQRIALARAMIKDP 555
Cdd:cd03268 76 ALIEAPGFYPNlTARENLrLLARLLGIRKKRIDEVLDV----------VGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 556 KILLLDEPTSALDPKSESLVQQAI-DKISKGRTTIVIAHRLATV-KNAETIIVLEQGSVIE 614
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIE 206
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
398-617 |
2.50e-21 |
|
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: 93.75 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFaypSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERF--YDPNKGLILLDGQDIRTLQVKwLRSQ 475
Cdd:cd03217 1 LEIKDLHV---SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MG--MVGQEPVLFAdtilenilmgkenatkkeaidaciAVNAHNFICDLPQGydtqvgekgtqLSGGQKQRIALARAMIK 553
Cdd:cd03217 77 LGifLAFQYPPEIP------------------------GVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 554 DPKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAH--RLATVKNAETIIVLEQGSVIEIGD 617
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKLrEEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD 188
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
417-616 |
2.66e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.06 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 417 NSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL---QVkwlrSQMGMVG--QEPVLFAD-TI 490
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghQI----ARMGVVRtfQHVRLFREmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 491 LENILMGKENATK-----------------KEAIDaciavNAHNFIcdlpqgydTQVG-------EKGTqLSGGQKQRIA 546
Cdd:PRK11300 98 IENLLVAQHQQLKtglfsgllktpafrraeSEALD-----RAATWL--------ERVGllehanrQAGN-LAYGQQRRLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 547 LARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIG 616
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANG 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1046-1255 |
2.80e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 99.32 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1046 PDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLD-LKWLRLQTALVGQEPALFGG- 1123
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 TIGENIRFGNPNAS-----WSEVEEAAKEAyIHNFicGLPRGYETEVGEsgiqLSGGQKQRIAIARAIVKKSKVLLLDEA 1198
Cdd:COG1129 95 SVAENIFLGREPRRgglidWRAMRRRAREL-LARL--GLDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1199 TSALDlESE-KHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGK-VSEYGTHDT 1255
Cdd:COG1129 168 TASLT-EREvERLFRIIRRLKAQGVAIIYIsHRLDEVFEiADRVTVLRDGRlVGTGPVAEL 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
400-625 |
2.90e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 95.24 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 400 LKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL-------QVKWL 472
Cdd:PRK10575 14 LRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWsskafarKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 473 RSQM----GMVGQEPVLFADTILENILmGKENATKKEAIDACIAVN-----AHNFIcdlpqgydtqvgekgTQLSGGQKQ 543
Cdd:PRK10575 91 PQQLpaaeGMTVRELVAIGRYPWHGAL-GRFGAADREKVEEAISLVglkplAHRLV---------------DSLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 544 RIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKIS--KGRTTIVIAHRL-ATVKNAETIIVLEQGSVIEIGDHNK 620
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqeRGLTVIAVLHDInMAARYCDYLVALRGGEMIAQGTPAE 234
|
....*
gi 1770234124 621 LMAQE 625
Cdd:PRK10575 235 LMRGE 239
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
718-964 |
2.97e-21 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 96.16 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 718 IFGMLAGAILSLF-PLVLGQ---ALTVYFNPDKSKLQKDVGYLCLALVGLGF-GCILTMMgqQGFC-GWAGTKLTKRVRD 791
Cdd:cd18780 2 TIALLVSSGTNLAlPYFFGQvidAVTNHSGSGGEEALRALNQAVLILLGVVLiGSIATFL--RSWLfTLAGERVVARLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 792 LLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPF-TL 870
Cdd:cd18780 80 RLFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPlSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 871 GASYFSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMY 950
Cdd:cd18780 158 GAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQ 237
|
250
....*....|....
gi 1770234124 951 SAYTLVLFFGAYLV 964
Cdd:cd18780 238 LAIVLVLWYGGRLV 251
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
398-616 |
3.08e-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: 93.50 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQvkwlRSQMG 477
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENIL-------MGKENAtKKEAIDACIAVnahnficDLpQGYDTQVGEkgtQLSGGQKQRIALAR 549
Cdd:cd03269 74 YLPEERGLYPKmKVIDQLVylaqlkgLKKEEA-RRRIDEWLERL-------EL-SEYANKRVE---ELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 550 AMIKDPKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIG 616
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1033-1247 |
3.19e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.57 E-value: 3.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEP--ALFGGTIGENIRFG--NPNASWSEVEEAAKEAYIhnfICGLPRGYETEVGesgiQLSGGQKQRIAIARAIVK 1188
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGleNKGIPHEEMKERVNEALE---LVGMQDFKEREPA----RLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1189 KSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKKANAIAVVQNGKV 1247
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDyqMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
397-616 |
4.73e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 4.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLI----LLDGQDIRTLQVKWL 472
Cdd:PRK13643 3 KFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 473 RSQMGMVGQEP--VLFADTILENILMGKEN--ATKKEAIDacIAVNAHNFIcdlpqGYDTQVGEKGT-QLSGGQKQRIAL 547
Cdd:PRK13643 83 RKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEK--IAAEKLEMV-----GLADEFWEKSPfELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 548 ARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIG 616
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
414-623 |
4.87e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.69 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 414 PILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQ--DIRTLQVKWLRSQMGMVGQEP---VLFAD 488
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqqIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 489 T------ILENILMGKENATKKeAIDACIAVNAHNFicdlpqgydtqvGEKGTQ-LSGGQKQRIALARAMIKDPKILLLD 561
Cdd:PRK13638 95 IdsdiafSLRNLGVPEAEITRR-VDEALTLVDAQHF------------RHQPIQcLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 562 EPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGDHNKLMA 623
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
415-623 |
6.78e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.39 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 415 ILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGL-----ILLDGQDIRTLQ-VKWLRSQMGMVGQEPVLFAD 488
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRdVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 489 TILENILMGkenatkkeaidaciaVNAHNFIC-----DLPQGYDTQVG----------EKGTQLSGGQKQRIALARAMIK 553
Cdd:PRK14271 116 SIMDNVLAG---------------VRAHKLVPrkefrGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 554 DPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLA-TVKNAETIIVLEQGSVIEIGDHNKLMA 623
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1046-1247 |
6.81e-21 |
|
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: 90.95 E-value: 6.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1046 PDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDlrdldlkwlrlqtalvgqepalfggti 1125
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE--------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1126 genIRFGNPNASWseveeAAKEAYIHnficglprgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLE 1205
Cdd:cd03216 64 ---VSFASPRDAR-----RAGIAMVY-------------------QLSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1770234124 1206 SEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKV 1247
Cdd:cd03216 117 EVERLFKVIRRLRAQGVAVIFIsHRLDEVFEiADRVTVLRDGRV 160
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1049-1252 |
8.85e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 94.38 E-value: 8.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1049 IVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKW-LRLQTALVGQEP--ALFGGTI 1125
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNPdnQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1126 GENIRFG------NPNASWSEVEEAAKEAYIHNFicglpRGYETEVgesgiqLSGGQKQRIAIARAIVKKSKVLLLDEAT 1199
Cdd:PRK13633 104 EEDVAFGpenlgiPPEEIRERVDESLKKVGMYEY-----RRHAPHL------LSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1200 SALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKKANAIAVVQNGKVSEYGT 1252
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
397-613 |
9.33e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.79 E-value: 9.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRtlqvkwLRSQM 476
Cdd:COG3845 5 ALELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR------IRSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 -------GMVGQEPVLFAD-TILENILMGKENAT-----KKEAIDACIAV-NAHNFICDLpqgyDTQVGekgtQLSGGQK 542
Cdd:COG3845 76 daialgiGMVHQHFMLVPNlTVAENIVLGLEPTKggrldRKAARARIRELsERYGLDVDP----DAKVE----DLSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 543 QRIALARAMIKDPKILLLDEPTSALDPkseslvqQAIDK--------ISKGRTTIVIAHRLATVK-NAETIIVLEQGSVI 613
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTP-------QEADElfeilrrlAAEGKSIIFITHKLREVMaIADRVTVLRRGKVV 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
399-616 |
1.10e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.22 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 399 ELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGM 478
Cdd:COG4604 3 EIKNVSKRYGGK---VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 479 VGQEPVLFAD-TILEniLM---------GKENATKKEAIDACIA-VN----AHNFIcdlpqgydtqvgekgTQLSGGQKQ 543
Cdd:COG4604 80 LRQENHINSRlTVRE--LVafgrfpyskGRLTAEDREIIDEAIAyLDledlADRYL---------------DELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 544 RIALARAMIKDPKILLLDEPTSALDPK-SESLVQQ---AIDKisKGRTTIVIAHRLatvkN-----AETIIVLEQGSVIE 614
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKhSVQMMKLlrrLADE--LGKTVVIVLHDI----NfascyADHIVAMKDGRVVA 216
|
..
gi 1770234124 615 IG 616
Cdd:COG4604 217 QG 218
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
398-617 |
1.24e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.82 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFaypsrmSV---PILNSLNLVIPSQRISALVGASGAGKSTIFALL---ERfYDPNKGLILLDGQDIRTLQVKw 471
Cdd:COG0396 1 LEIKNLHV------SVegkEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 472 LRSQMGM-VG-QEPVLFADTILENILMGKENATKKEAIDAciaVNAHNFICD------LPQGY-DTQVGEKgtqLSGGQK 542
Cdd:COG0396 73 ERARAGIfLAfQYPVEIPGVSVSNFLRTALNARRGEELSA---REFLKLLKEkmkelgLDEDFlDRYVNEG---FSGGEK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 543 QRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAH--RLATVKNAETIIVLEQGSVIEIGD 617
Cdd:COG0396 147 KRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1049-1252 |
1.76e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 92.92 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1049 IVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIG-----GKVMMGGRDL--RDLDLKWLRLQTALVGQEPALF 1121
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1122 GGTIGENIRFG----NPNASWSE-VEEAAKEAYIHNFIcglprgyETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLD 1196
Cdd:PRK14243 104 PKSIYDNIAYGarinGYKGDMDElVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1197 EATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGT 1252
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
415-568 |
1.81e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 415 ILNSLNLVIPSQRISALVGASGAGKST---IFALLERFydpNKGLILLDGQDIRTLQVKwlRSQMGMVGQEPVLFAD-TI 490
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTllrIIAGLEHQ---TSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRHmTV 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 491 LENILMGKENATKKEAIDACIAVNAHNFICDLPQgYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALD 568
Cdd:PRK10851 92 FDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQ-LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1051-1262 |
1.97e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.49 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1051 LREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDL---RDLDLKWLRLQT-ALVGQEPALFGG-TI 1125
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakiSDAELREVRRKKiAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1126 GENIRFGNPNASWSEVE------EAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLLLDEAT 1199
Cdd:PRK10070 124 LDNTAFGMELAGINAEErrekalDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1200 SALDLESEKHVQDAIRKIIKR--TTTIVVVHRL-STIKKANAIAVVQNGKVSEYGTHDTLLTNHSN 1262
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAN 258
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1033-1259 |
2.26e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.79 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYD-----PIGGKVMMGGRDL--RDLDLK 1105
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1106 WLRLQTALVGQEPALFGGTIGENIRFGNPNASWSE-------VEEAAKEAYIHNFIcglprgyETEVGESGIQLSGGQKQ 1178
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPkleiddiVESALKDADLWDEI-------KHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1179 RIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT--TTIVVVHRLSTIKKANAIAVV------QNGKVSEY 1250
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSelTMVIVSHNLHQVSRLSDFTAFfkgnenRIGQLVEF 237
|
....*....
gi 1770234124 1251 GTHDTLLTN 1259
Cdd:PRK14258 238 GLTKKIFNS 246
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1056-1256 |
2.35e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.40 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDL-------RDLdlkwlrlqtALVGQEPALFGG-TIGE 1127
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthrsiqqRDI---------CMVFQSYALFPHmSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1128 NIRFG--NPNASWSEVEEAAKEAYIHNFICGLPRGYETevgesgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLE 1205
Cdd:PRK11432 98 NVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRYVD-------QISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1206 SEKHVQDAIRKIIKR--TTTIVVVHRLS-TIKKANAIAVVQNGKVSEYGTHDTL 1256
Cdd:PRK11432 171 LRRSMREKIRELQQQfnITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
398-633 |
2.40e-20 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 91.31 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDirtlqvkWLRSQMG 477
Cdd:TIGR03740 1 LETKNLSKRFGKQT---AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP-------WTRKDLH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVG---QEPVLFAD-TILENILMGKEN-ATKKEAIDACIAvnahnfICDLpqgydTQVGEK-GTQLSGGQKQRIALARAM 551
Cdd:TIGR03740 71 KIGsliESPPLYENlTARENLKVHTTLlGLPDSRIDEVLN------IVDL-----TNTGKKkAKQFSLGMKQRLGIAIAL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 552 IKDPKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGDHNKLMAQEGAYF 629
Cdd:TIGR03740 140 LNHPKLLILDEPTNGLDPIGIQELRELIRSFpEQGITVILSSHILSEVQQlADHIGIISEGVLGYQGKINKSENLEKLFV 219
|
....
gi 1770234124 630 SLIK 633
Cdd:TIGR03740 220 EVVK 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1252 |
2.78e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.83 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSrpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLrDLDLKWL---RL 1109
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 QTALVGQEP--ALFGGTIGENIRFG--NPNASWSEVEEAAKEAYihnficglprgyeTEVGESGIQ------LSGGQKQR 1179
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEAL-------------KAVGMEGFEnkpphhLSGGQKKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1180 IAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVV-VHRLSTIKK-ANAIAVVQNGKVSEYGT 1252
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIsTHDVDLVPVyADKVYVMSDGKIIKEGT 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1256 |
3.09e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.51 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSrPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEP--ALFGGTIGENIRFGNPNAS------WSEVEEAAKEAYIHNFicglpRGYETEvgesgiQLSGGQKQRIAIAR 1184
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENHAvpydemHRRVSEALKQVDMLER-----ADYEPN------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1185 AIVKKSKVLLLDEATSALDLESEKHVQDAIRKI--IKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTL 1256
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
406-607 |
3.44e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.99 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 406 AYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwlRSQMgmvgqePVL 485
Cdd:NF040873 1 GYGGR---PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--RSEV------PDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 486 FADTILENILMGK----------ENATKKEAIDACIAVNAHNFIcdlpqgyDTQVGEkgtqLSGGQKQRIALARAMIKDP 555
Cdd:NF040873 70 LPLTVRDLVAMGRwarrglwrrlTRDDRAAVDDALERVGLADLA-------GRQLGE----LSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 556 KILLLDEPTSALDPKSESLVQQAIDKIS-KGRTTIVIAHRLATVKNAETIIVL 607
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
398-613 |
4.86e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.72 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPS-RMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWL---- 472
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 473 RSQMGMVGQEPVLFAD-TILEN-----ILMGKENATKKEaidaciavNAHNFICDLpqGYDTQVGEKGTQLSGGQKQRIA 546
Cdd:PRK10535 85 REHFGFIFQRYHLLSHlTAAQNvevpaVYAGLERKQRLL--------RAQELLQRL--GLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 547 LARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRLATVKNAETIIVLEQGSVI 613
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1033-1264 |
5.80e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.54 E-value: 5.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGGTIGENIRFgnpnaSWS----EVEEAAKEAYIHNFicGLPrgyETEVGESGIQLSGGQKQRIAIARAIVK 1188
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIF-----PWQirnqQPDPAIFLDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1189 KSKVLLLDEATSALDLESEKHVQDairkiikrtttivVVHRLSTIKKanaIAVVqngkvseYGTHDTLLTNHSNGV 1264
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNE-------------IIHRYVREQN---IAVL-------WVTHDKDEINHADKV 207
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
398-598 |
5.99e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 91.36 E-value: 5.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFaypSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWL---RS 474
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFAD-TILENILMG-KENATKKEAI---DACIAVNAhnficdlpqgydtqVGEKG------TQLSGGQKQ 543
Cdd:PRK11831 85 RMSMLFQSGALFTDmNVFDNVAYPlREHTQLPAPLlhsTVMMKLEA--------------VGLRGaaklmpSELSGGMAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 544 RIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATV 598
Cdd:PRK11831 151 RAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEV 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1048-1247 |
6.60e-20 |
|
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: 90.57 E-value: 6.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1048 VIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwlrlQTALVG-----QEPALFG 1122
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH----EIARLGigrtfQIPRLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1123 G-TIGENIRFG-------NPNASWSEVEEAAKEAYIHNFI--CGLPRGYETEVGEsgiqLSGGQKQRIAIARAIVKKSKV 1192
Cdd:cd03219 89 ElTVLENVMVAaqartgsGLLLARARREEREARERAEELLerVGLADLADRPAGE----LSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1193 LLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKV 1247
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRELRERGITVLLVeHDMDVVMSlADRVTVLDQGRV 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
398-639 |
7.99e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.59 E-value: 7.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTlQVKWLRSQMG 477
Cdd:PRK13536 42 IDLAGVSKSYGDK---AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENILM-GKENATKKEAIDACIAvNAHNFiCDLPQGYDTQVGEkgtqLSGGQKQRIALARAMIKDP 555
Cdd:PRK13536 118 VVPQFDNLDLEfTVRENLLVfGRYFGMSTREIEAVIP-SLLEF-ARLESKADARVSD----LSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 556 KILLLDEPTSALDPKSESLVQQAIDK-ISKGRTTIVIAHRLATVKN-AETIIVLEQG------------------SVIEI 615
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGrkiaegrphalidehigcQVIEI 271
|
250 260
....*....|....*....|....*.
gi 1770234124 616 --GDHNKLMAQEGAYFSLIKLATEAI 639
Cdd:PRK13536 272 ygGDPHELSSLVKPYARRIEVSGETL 297
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1038-1261 |
8.10e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.20 E-value: 8.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1038 VNFAYPSrpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLD-LKWLRLQTALVGQ 1116
Cdd:PRK13644 7 VSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1117 EP--ALFGGTIGENIRFGNPNASWSEVE----------EAAKEAYIHNficglprgyetevgeSGIQLSGGQKQRIAIAR 1184
Cdd:PRK13644 85 NPetQFVGRTVEEDLAFGPENLCLPPIEirkrvdralaEIGLEKYRHR---------------SPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1185 AIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIV-VVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTNHS 1261
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1050-1259 |
8.70e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 90.58 E-value: 8.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMG------GRDLRDLD--LKWLRLQTALVGQEPALF 1121
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtARSLSQQKglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1122 GG-TIGENIRFGnPNASWSEVEEAAKEayihnficgLPRGYETEVGESGIQ------LSGGQKQRIAIARAIVKKSKVLL 1194
Cdd:PRK11264 98 PHrTVLENIIEG-PVIVKGEPKEEATA---------RARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1195 LDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVtHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
993-1247 |
8.90e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 96.77 E-value: 8.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 993 GLAPDTSMASTAIPAVFEIMNRNPLIDGKGKKIEQSkPFDLEFKMVNFaYPSRPDVIvLREFCLKVKGGTMVAVVGGSGS 1072
Cdd:PTZ00243 621 VVVEDTDYGSPSSASRHIVEGGTGGGHEATPTSERS-AKTPKMKTDDF-FELEPKVL-LRDVSVSVPRGKLTVVLGATGS 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1073 GKSTVIWLMQRFYDPIGGKVmmggrdlrdldlkWLRLQTALVGQEPALFGGTIGENIRFGNPNASwSEVEEAAKEAYIHN 1152
Cdd:PTZ00243 698 GKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNILFFDEEDA-ARLADAVRVSQLEA 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1153 FICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLE-SEKHVQDAIRKIIKRTTTIVVVHRLS 1231
Cdd:PTZ00243 764 DLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVH 843
|
250
....*....|....*.
gi 1770234124 1232 TIKKANAIAVVQNGKV 1247
Cdd:PTZ00243 844 VVPRADYVVALGDGRV 859
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1054-1261 |
9.52e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 90.03 E-value: 9.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1054 FCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwlRLQTALVGQEPALFGG-TIGENIRFG 1132
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1133 -NPN-----ASWSEVEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSALD--L 1204
Cdd:PRK10771 96 lNPGlklnaAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDpaL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1205 ESE--KHVQDAIRKiiKRTTTIVVVHRLStikKANAIA----VVQNGKVSEYGTHDTLLTNHS 1261
Cdd:PRK10771 165 RQEmlTLVSQVCQE--RQLTLLMVSHSLE---DAARIAprslVVADGRIAWDGPTDELLSGKA 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
398-625 |
1.15e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.02 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYpsRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEP--VLFADTILENILMGKENATKKEAIDACIAVNAHNFIcdlpqGYDTQVGEKGTQLSGGQKQRIALARAMIKDP 555
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 556 KILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGDHNKLMAQE 625
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
405-662 |
1.44e-19 |
|
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: 96.13 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 405 FAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLrsqmgMVGqepv 484
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWI-----MPG---- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 485 lfadTILENILMG--KENATKKEAIDACiavNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDE 562
Cdd:TIGR01271 502 ----TIKDNIIFGlsYDEYRYTSVIKAC---QLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 563 PTSALDPKSE-SLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQEGAYFSLIkLATEAISS 641
Cdd:TIGR01271 575 PFTHLDVVTEkEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL-LGLEAFDN 653
|
250 260
....*....|....*....|.
gi 1770234124 642 npVSKKGKTVINQETSSNCDL 662
Cdd:TIGR01271 654 --FSAERRNSILTETLRRVSI 672
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1033-1251 |
1.49e-19 |
|
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: 88.38 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRP---DVIVLREFCLKVKGGTMVAVVGGSGSGKSTV--IWLMQRFYDPIGGKVMMGGRDLrdlDLKWL 1107
Cdd:cd03213 4 LSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1108 RLQTALVGQEPALFGG-TIGENIRFgnpnaswseveeAAKeayihnficgLpRGyetevgesgiqLSGGQKQRIAIARAI 1186
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMF------------AAK----------L-RG-----------LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1187 VKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR-TTTIVVVHRLST--IKKANAIAVVQNGKVSEYG 1251
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
95-371 |
1.69e-19 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 90.68 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 95 LFGNFVNKIA--LDNDKDQMIKDVRE----LCVLMSALSgivvIGAYLQIACWRLVGERLGHRIRSKYLRAVLRQDVSFF 168
Cdd:cd18574 18 LLGDLVNVISrsLKETNGDFIEDLKKpalkLLGLYLLQS----LLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 169 DTDiSTSDIMHGISSDVaqiQEVMGD-KM--SQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFCGVAYKAVYVGL 245
Cdd:cd18574 94 DTH-RTGELVNRLTADV---QEFKSSfKQcvSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 246 --AAKEVNSykKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFakGIG---------LGVIYLVTYs 314
Cdd:cd18574 170 srRAQAQVA--KATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGL--GIGifqglsnlaLNGIVLGVL- 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 315 twalafWYGSILVSRNELSGGAAIACFFGVTIGGRGLAlSLSY-FAQFAQGTVAASKV 371
Cdd:cd18574 245 ------YYGGSLVSRGELTAGDLMSFLVATQTIQRSLA-QLSVlFGQYVKGKSAGARV 295
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
419-623 |
1.78e-19 |
|
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: 92.10 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 419 LNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDG---QDIRT-LQVKWLRSQMGMVGQEPVLFAD-TILEN 493
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgIFLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 494 ILMGKENATKKEAI---DACIAVnahnficdlpQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPK 570
Cdd:TIGR02142 96 LRYGMKRARPSERRisfERVIEL----------LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 571 SESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGDHNKLMA 623
Cdd:TIGR02142 166 RKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1044-1258 |
2.09e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.60 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1044 SRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPAL-FG 1122
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1123 GTIGENIRFG-NPNAS----WSEVEEAAKEAyihnficGLPRGYETEVGESGI-QLSGGQKQRIAIARAIVKKSKVLLLD 1196
Cdd:PRK09536 92 FDVRQVVEMGrTPHRSrfdtWTETDRAAVER-------AMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1197 EATSALDLESEKHVQDAIRKIIKRTTTIV-VVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLT 1258
Cdd:PRK09536 165 EPTASLDINHQVRTLELVRRLVDDGKTAVaAIHDLDLAARyCDELVLLADGRVRAAGPPADVLT 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
396-571 |
2.28e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.93 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 396 GRLELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFAL---LERfydPNKGLILLDGQDIRTLQVkWL 472
Cdd:COG1137 2 MTLEAENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMivgLVK---PDSGRIFLDGEDITHLPM-HK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 473 RSQMGMvG---QEPVLFAD-TILENILM-----GKENATKKEAIDAC-----IAVNAHNficdlpqgydtqvgeKGTQLS 538
Cdd:COG1137 75 RARLGI-GylpQEASIFRKlTVEDNILAvlelrKLSKKEREERLEELleefgITHLRKS---------------KAYSLS 138
|
170 180 190
....*....|....*....|....*....|...
gi 1770234124 539 GGQKQRIALARAMIKDPKILLLDEPTSALDPKS 571
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVDPIA 171
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
398-616 |
2.33e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.21 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFaypSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:PRK09536 4 IDVSDLSV---EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVL-FADTILENILMGKEN-----ATKKEAIDACI--AVNAhnfiCDLPQGYDTQVgekgTQLSGGQKQRIALAR 549
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMGRTPhrsrfDTWTETDRAAVerAMER----TGVAQFADRPV----TSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 550 AMIKDPKILLLDEPTSALD----PKSESLVQQAIDkisKGRTTIVIAHRL-ATVKNAETIIVLEQGSVIEIG 616
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDinhqVRTLELVRRLVD---DGKTAVAAIHDLdLAARYCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1033-1252 |
2.67e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.86 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDP---IGGKVMMGGRDLRDLDLKWLRL 1109
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 QTALVGQEP--ALFGGTIGENIRFGNPNASWSE------VEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIA 1181
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRpemikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1182 IARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT--TTIVVVHRLSTIKKANAIAVVQNGKVSEYGT 1252
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
716-964 |
2.90e-19 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 90.27 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 716 GVIFGMLAGAILSLFPLVLGQALTVYFNPDKSKLQ--KDVGYLCLALVGLGFGCILTMMGQQGFCGWAGTKLTKRVRDLL 793
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIfgLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 794 FRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLA-TIVTPFTLGA 872
Cdd:cd18573 81 FKSILRQDAAFFD--KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMlLVVPPIAVGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 873 SYFSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMYSA 952
Cdd:cd18573 159 VFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLS 238
|
250
....*....|..
gi 1770234124 953 YTLVLFFGAYLV 964
Cdd:cd18573 239 LLSVLYYGGSLV 250
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
416-612 |
3.51e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 89.30 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 416 LNSLNLVIPSQRISALVGASGAGKSTIFALLErfydpnkGLILLD---GQDI----RTLQ--------VKWLRSQMGMVG 480
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS-------GLITGDksaGSHIellgRTVQregrlardIRKSRANTGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 481 QEPVLFAD-TILENILMGKENAT--------------KKEAIDACIAVNAHNFicdlpqgydtqVGEKGTQLSGGQKQRI 545
Cdd:PRK09984 93 QQFNLVNRlSVLENVLIGALGSTpfwrtcfswftreqKQRALQALTRVGMVHF-----------AHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 546 ALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRL-ATVKNAETIIVLEQGSV 612
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVdYALRYCERIVALRQGHV 231
|
|
| longin-like |
cd14818 |
Longin-like domains; Longin-like domains are small protein domains present in a variety of ... |
1339-1459 |
4.00e-19 |
|
Longin-like domains; Longin-like domains are small protein domains present in a variety of proteins and members of protein complexes involved in or required for different steps during the transport of proteins from the ribosome to the ER to the plasma membrane, via the Golgi apparatus. Examples are mu and sigma subunits of the heterotetrameric adaptor protein (AP) complex, zeta and delta subunits of the heterotetrameric F-COPI complex, a subgroup of R-SNARE proteins, a subfamily of the transport protein particle (TRAPP), and the signal recognition particle receptor subunit alpha (SR-alpha).
Pssm-ID: 341426 Cd Length: 117 Bit Score: 84.50 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1339 KLTMIARVtDGLPLAEGLDDGRDmQDAEFYKQQVKALFKNLSRGQNEasRMSVETGPYVFHYIIEGRVCYLTMCDRAYPK 1418
Cdd:cd14818 1 LQLAVFDP-QGQVLAASNWLGKK-PSVKFSLIQIKSFFSKLITSGFD--FLTLTIGSYTFHYYLNKGLYFVVITDEQELR 76
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1770234124 1419 KLAFQYLEDLKNEFERGYGNQIETAARPYAFIKFDTFIQKT 1459
Cdd:cd14818 77 QELFQTLNLLLKEFNSLHGSEVITKNIEDDLEEFESYLDIK 117
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1047-1259 |
4.80e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.43 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYD-----PIGGKVMMGGRDLRDLDLKWLRLQTALVGQEP-AL 1120
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1121 FGGTIGENIRFG----NPNASWSEVEEAAKEAYIHnfiCGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLD 1196
Cdd:PRK14247 95 PNLSIFENVALGlklnRLVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1197 EATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
430-624 |
5.64e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.02 E-value: 5.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 430 ALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIR---TLQVKWLRSQMGMVGQEPvlFAD--------TILENILMGK 498
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNP--YGSlnprkkvgQILEEPLLIN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 499 ENATKKEAIDACIAVNAhnficdlpqgydtQVGEKGTQ-------LSGGQKQRIALARAMIKDPKILLLDEPTSALDPKS 571
Cdd:PRK11308 123 TSLSAAERREKALAMMA-------------KVGLRPEHydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 572 ESLV-------QQAIdkiskGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGDHNKLMAQ 624
Cdd:PRK11308 190 QAQVlnlmmdlQQEL-----GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
414-595 |
8.50e-19 |
|
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: 93.54 E-value: 8.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 414 PILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTlQVKWLRSQMGMVGQEPVLFAD-TILE 492
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 493 NILM-----GKENATKKEAIDACIAvnahnficdlPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSAL 567
Cdd:TIGR01257 1023 HILFyaqlkGRSWEEAQLEMEAMLE----------DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180
....*....|....*....|....*...
gi 1770234124 568 DPKSESLVQQAIDKISKGRTTIVIAHRL 595
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRSGRTIIMSTHHM 1120
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
413-616 |
1.04e-18 |
|
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: 86.82 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 413 VPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGqdirtlQVKWLrsqMGM-VGQEPVLfadTIL 491
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSL---LGLgGGFNPEL---TGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 492 ENI-----LMGKENATKKEAIDACIAvnahnfICDLPQGYDTQVGEkgtqLSGGQKQRIALARAMIKDPKILLLDEPTSA 566
Cdd:cd03220 103 ENIylngrLLGLSRKEIDEKIDEIIE------FSELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 567 LDpksESLVQQAIDKI----SKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIG 616
Cdd:cd03220 173 GD---AAFQEKCQRRLrellKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
398-625 |
1.09e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 87.24 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQV-KWLRSQM 476
Cdd:PRK11614 6 LSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQEPVLFAD-TILENILMGKENATKKEAIDACIAVNAHnficdLPQGYDTQVGEKGTqLSGGQKQRIALARAMIKDP 555
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWVYEL-----FPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 556 KILLLDEPTSALDPkseSLVQQAIDKISKGRT---TIVIAHRLA--TVKNAETIIVLEQGSVIEIGDHNKLMAQE 625
Cdd:PRK11614 157 RLLLLDEPSLGLAP---IIIQQIFDTIEQLREqgmTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1059-1203 |
1.30e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 89.02 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1059 KGGTmVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDL---DLKWLRLQTALVGQEPalFGG-----TIGENIR 1130
Cdd:COG4608 43 RGET-LGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDP--YASlnprmTVGDIIA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1131 FG---NPNASWSEVEEAAKEA-------------YIHnficglprgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLL 1194
Cdd:COG4608 120 EPlriHGLASKAERRERVAELlelvglrpehadrYPH-------------------EFSGGQRQRIGIARALALNPKLIV 180
|
....*....
gi 1770234124 1195 LDEATSALD 1203
Cdd:COG4608 181 CDEPVSALD 189
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1065-1259 |
1.49e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.14 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1065 AVVGGSGSGKSTVIWLMQRFYD-----PIGGKVMMGGRDL--RDLDLKWLRLQTALVGQEPALFGGTIGENIRFG----- 1132
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGlrlkg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1133 -NPNASWSE-VEEAAKEAYIHNFIcglprgyETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHV 1210
Cdd:PRK14239 115 iKDKQVLDEaVEKSLKGASIWDEV-------KDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKI 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1211 QDAIRKIIKRTTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:PRK14239 188 EETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMN 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
398-625 |
1.60e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.32 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSVpilNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTlQVKWLRSQMG 477
Cdd:PRK13537 8 IDFRNVEKRYGDKLVV---DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENILM-----GKENATKKEAIDACIAvnahnfICDLPQGYDTQVGEkgtqLSGGQKQRIALARAM 551
Cdd:PRK13537 84 VVPQFDNLDPDfTVRENLLVfgryfGLSAAAARALVPPLLE------FAKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 552 IKDPKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGDHNKLMAQE 625
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1056-1252 |
1.61e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.49 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLR----DLDLKWLRLQTALVGQ--EPALFGGTIGENI 1129
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNKDIKQIRKKVGLVFQfpESQLFEETVLKDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1130 RFGNPNASWSEvEEAAKEAYIHNFICGLPrgyETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKH 1209
Cdd:PRK13649 108 AFGPQNFGVSQ-EEAEALAREKLALVGIS---ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1770234124 1210 VQDAIRKIIKRTTTIVVVHRL--STIKKANAIAVVQNGKVSEYGT 1252
Cdd:PRK13649 184 LMTLFKKLHQSGMTIVLVTHLmdDVANYADFVYVLEKGKLVLSGK 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1025-1229 |
1.62e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.41 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1025 IEQSKPFDLEFKMVNFAYPSrpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTV------IWlmqrfydPIG-GKVMMGGR 1097
Cdd:COG4178 355 IETSEDGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKSTLlraiagLW-------PYGsGRIARPAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1098 DlrdldlkwlrlQTALVGQEPALFGGTIGENIRFGNPNASWS--EVEEAAKEayihnfiCGLPRgYETEVGES---GIQL 1172
Cdd:COG4178 426 A-----------RVLFLPQRPYLPLGTLREALLYPATAEAFSdaELREALEA-------VGLGH-LAERLDEEadwDQVL 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1173 SGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHR 1229
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
398-610 |
1.68e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 83.65 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFallerfydpnkglilldgqdirtlqvkwlrsqmg 477
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLL---------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 mvgqepvlfadtileNILMGKENATKKEaidacIAVNAHNFICDLPQgydtqvgekgtqLSGGQKQRIALARAMIKDPKI 557
Cdd:cd03221 44 ---------------KLIAGELEPDEGI-----VTWGSTVKIGYFEQ------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 558 LLLDEPTSALDPKSESLVQQAIDKISkgRTTIVIAH-R--LATVknAETIIVLEQG 610
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP--GTVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
398-617 |
1.91e-18 |
|
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: 90.90 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKN--VSFAYPSRMsVPILNSLNLVIPSQRISALVGASGAGKS----TIFALLERFYDPNKGLILLDGQDIRTLQVKW 471
Cdd:COG4172 7 LSVEDlsVAFGQGGGT-VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 472 LR----SQMGMVGQEPV-----LFadTILENI---LMGKENATKKEAIDACIAV-------NAHNFICDLPQgydtqvge 532
Cdd:COG4172 86 LRrirgNRIAMIFQEPMtslnpLH--TIGKQIaevLRLHRGLSGAAARARALELlervgipDPERRLDAYPH-------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 533 kgtQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPksesLVQQAI----DKISK--GRTTIVIAHRLATVKN-AETII 605
Cdd:COG4172 156 ---QLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQAQIldllKDLQRelGMALLLITHDLGVVRRfADRVA 228
|
250
....*....|..
gi 1770234124 606 VLEQGSVIEIGD 617
Cdd:COG4172 229 VMRQGEIVEQGP 240
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1056-1251 |
2.40e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.12 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDlKWLRlQTALVGQEPALFGG-TIGENIRFG-- 1132
Cdd:PRK11607 40 LTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQR-PINMMFQSYALFPHmTVEQNIAFGlk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1133 ---NPNASW-SEVEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEK 1208
Cdd:PRK11607 118 qdkLPKAEIaSRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1770234124 1209 HVQDAIRKIIKR--TTTIVVVH-RLSTIKKANAIAVVQNGKVSEYG 1251
Cdd:PRK11607 187 RMQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
398-612 |
2.67e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwLRSQMG 477
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 --MVGQEPVLFAD-TILENILMG--KENATKKEAIDACIAVNAHnfiCDLpqgyDTQVGekgtQLSGGQKQRIALARAMI 552
Cdd:PRK15439 88 iyLVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDL----DSSAG----SLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 553 KDPKILLLDEPTSALDP-KSESLVQQAIDKISKGRTTIVIAHRLATVKN-AETIIVLEQGSV 612
Cdd:PRK15439 157 RDSRILILDEPTASLTPaETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
398-617 |
3.07e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.15 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSV--------PILNSLNLVIPSQRISALVGASGAGKSTI-FALLERFydPNKGLILLDGQDIRTLQ 468
Cdd:PRK15134 276 LDVEQLQVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 469 VKWL---RSQMGMVGQEPVLFAD---TILENILMGKE------NATKKEA--IDACIAVnahnficdlpqGYDTQVGEK- 533
Cdd:PRK15134 354 RRQLlpvRHRIQVVFQDPNSSLNprlNVLQIIEEGLRvhqptlSAAQREQqvIAVMEEV-----------GLDPETRHRy 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 534 GTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDpKSeslVQQAIDKISKGRTT------IVIAHRLATVKN-AETIIV 606
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KT---VQAQILALLKSLQQkhqlayLFISHDLHVVRAlCHQVIV 498
|
250
....*....|.
gi 1770234124 607 LEQGSVIEIGD 617
Cdd:PRK15134 499 LRQGEVVEQGD 509
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
398-627 |
3.15e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.09 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNV--SFAypsrmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQvkwlRSQ 475
Cdd:COG4152 2 LELKGLtkRFG-----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MGMVGQEPVLFAD-TILENIL-------MGKENAtKKEAIDACIAVnahnficDLPQGYDTQVGEkgtqLSGGQKQRIAL 547
Cdd:COG4152 73 IGYLPEERGLYPKmKVGEQLVylarlkgLSKAEA-KRRADEWLERL-------GLGDRANKKVEE----LSKGNQQKVQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 548 ARAMIKDPKILLLDEPTSALDPKSESLVQQAI-DKISKGRTTIVIAHRLATV-KNAETIIVLEQGSVIEIGDHNKLMAQE 625
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQF 220
|
..
gi 1770234124 626 GA 627
Cdd:COG4152 221 GR 222
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
398-614 |
3.24e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 86.40 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPS------RMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL---Q 468
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 469 VKWLRSQMGMVGQE------PVLFADTI----LENILMGKENATKKEAIDACIAVNAHNFICD-LPQgydtqvgekgtQL 537
Cdd:TIGR02769 83 RRAFRRDVQLVFQDspsavnPRMTVRQIigepLRHLTSLDESEQKARIAELLDMVGLRSEDADkLPR-----------QL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 538 SGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIE 614
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
397-625 |
4.80e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.81 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQM 476
Cdd:PRK10253 7 RLRGEQLTLGYGKYT---VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQEPVLFAD-TILENILMGKE------NATKKEAIDACIAVNAHNFICDLP-QGYDTqvgekgtqLSGGQKQRIALA 548
Cdd:PRK10253 84 GLLAQNATTPGDiTVQELVARGRYphqplfTRWRKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 549 RAMIKDPKILLLDEPTSALDPKSESLVQQAIDKIS--KGRTTIVIAHRL-ATVKNAETIIVLEQGSVIEIGDHNKLMAQE 625
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNreKGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
400-616 |
4.90e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.78 E-value: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 400 LKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQdiRTLQVKWLRSQMGMV 479
Cdd:PRK11000 6 LRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 480 GQEPVLFAD-TILENILMG-KENATKKEAIDAciAVNAHNFICDLPQGYDtqvgEKGTQLSGGQKQRIALARAMIKDPKI 557
Cdd:PRK11000 81 FQSYALYPHlSVAENMSFGlKLAGAKKEEINQ--RVNQVAEVLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 558 LLLDEPTSALDPKSEslVQQAIDkISK-----GRTTIVIAH-RLATVKNAETIIVLEQGSVIEIG 616
Cdd:PRK11000 155 FLLDEPLSNLDAALR--VQMRIE-ISRlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
398-614 |
6.05e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 6.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVI-PSQRIsALVGASGAGKSTIFALLERFYDPNKGLILLdGQdirTLQVKWLrSQM 476
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIdRGDRI-GLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE---TVKIGYF-DQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 gmvgQEPVLFADTILENILMGKENATKKEAIDACiavNAHNFicdlpQGYD--TQVGEkgtqLSGGQKQRIALARAMIKD 554
Cdd:COG0488 387 ----QEELDPDKTVLDELRDGAPGGTEQEVRGYL---GRFLF-----SGDDafKPVGV----LSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 555 PKILLLDEPTSALDPKSESLVQQAIDKIsKGrTTIVIAH------RLATvknaeTIIVLEQGSVIE 614
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdryfldRVAT-----RILEFEDGGVRE 509
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
147-335 |
6.12e-18 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 85.99 E-value: 6.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 147 RLGHRIRSKYLRAVLRQDVSFFDTDiSTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLA 226
Cdd:cd18589 66 RIHSRLQGLVFAAVLRQEIAFFDSN-QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 227 VTPLTMFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLg 306
Cdd:cd18589 145 GLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSM- 223
|
170 180 190
....*....|....*....|....*....|..
gi 1770234124 307 viYLVTYSTWALA---FWYGSILVSRNELSGG 335
Cdd:cd18589 224 --WTSSFSGLALKvgiLYYGGQLVTAGTVSSG 253
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1050-1259 |
6.50e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.41 E-value: 6.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDL---RDLD----------LKWLRLQTALVGQ 1116
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvRDKDgqlkvadknqLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1117 EPALFGG-TIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPrgyETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLL 1195
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGID---ERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1196 DEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEGKTMVVVtHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1056-1259 |
6.79e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 6.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGG----RDLRDL-DLKWLRLQTALVGQEP--ALFGGTIGEN 1128
Cdd:PRK13645 32 LTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIkEVKRLRKEIGLVFQFPeyQLFQETIEKD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1129 IRFGNPNASwSEVEEAAKEAYIHNFICGLPRGYeteVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEK 1208
Cdd:PRK13645 112 IAFGPVNLG-ENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEE 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1209 HVQDAIRKIIK--RTTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:PRK13645 188 DFINLFERLNKeyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1051-1203 |
9.43e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 83.69 E-value: 9.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1051 LREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDP---IGGKVMMGGRDLRDLDLkwLRLQTALVGQEPALFGG-TIG 1126
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA--EQRRIGILFQDDLLFPHlSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1127 ENIRFGNPNA-SWSEVEEAAKEAYihnficglprgyeTEVGESGI------QLSGGQKQRIAIARAIVKKSKVLLLDEAT 1199
Cdd:COG4136 95 ENLAFALPPTiGRAQRRARVEQAL-------------EEAGLAGFadrdpaTLSGGQRARVALLRALLAEPRALLLDEPF 161
|
....
gi 1770234124 1200 SALD 1203
Cdd:COG4136 162 SKLD 165
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1050-1259 |
1.04e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.15 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGG-----KVMMGGRDLRDL-DLKWLRLQTALVGQEPALFGG 1123
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 TIGENIRFGNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALD 1203
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1204 LESEKHVQDAIRKIIKRTTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
367-624 |
1.15e-17 |
|
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: 89.58 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 367 AASKVFAIIDrIPAIDPYSTTGRKP---------ETVH--------GRLELKNVSFAYPSRMSVpILNSLNLVI-PSQRI 428
Cdd:TIGR01271 1171 SVSRVFKFID-LPQEEPRPSGGGGKyqlstvlviENPHaqkcwpsgGQMDVQGLTAKYTEAGRA-VLQDLSFSVeGGQRV 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 429 sALVGASGAGKSTIFALLERFYDpNKGLILLDG--QDIRTLQvKWlRSQMGMVGQEPVLFADTILENiLMGKENATKKEA 506
Cdd:TIGR01271 1249 -GLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvsWNSVTLQ-TW-RKAFGVIPQKVFIFSGTFRKN-LDPYEQWSDEEI 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 507 IDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGR 586
Cdd:TIGR01271 1324 WKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC 1403
|
250 260 270
....*....|....*....|....*....|....*...
gi 1770234124 587 TTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQ 624
Cdd:TIGR01271 1404 TVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
397-617 |
1.23e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.52 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAYPSRMSVPI--LNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL------- 467
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTELkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 468 -----------------QVKWLRSQMGMVGQ--EPVLFADTILENILMG-------KENATK--KEAIDaciavnahnfI 519
Cdd:PRK13651 82 kvleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvsmgvsKEEAKKraAKYIE----------L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 520 CDLPQGYdtqVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLATV 598
Cdd:PRK13651 152 VGLDESY---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNV 228
|
250 260
....*....|....*....|
gi 1770234124 599 -KNAETIIVLEQGSVIEIGD 617
Cdd:PRK13651 229 lEWTKRTIFFKDGKIIKDGD 248
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
713-973 |
1.25e-17 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 85.17 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 713 LCVGVIFGMLAGAILSLFPLVLGQAL-TVYFNPDKSKLQkdvgYLCLALVGLGFGCILTMMGQQGFCGWAGTKLTKRVRD 791
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLdDIFVEKDLEALL----LVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 792 LLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPFTLG 871
Cdd:cd18552 77 DLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 872 asyfsLIINIGSKLDN---DSFDKASGIASA---AVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGIS 945
Cdd:cd18552 155 -----PIRRIGKRLRKisrRSQESMGDLTSVlqeTLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLM 229
|
250 260
....*....|....*....|....*...
gi 1770234124 946 QGAMYSAYTLVLFFGAYLVKKDYTKFGD 973
Cdd:cd18552 230 ELLGAIAIALVLWYGGYQVISGELTPGE 257
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
396-624 |
1.29e-17 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; 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: 213256 [Multi-domain] Cd Length: 275 Bit Score: 84.91 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 396 GRLELKNVSFAYpSRMSVPILNSLNLVI-PSQRIsALVGASGAGKSTIFALLERFYDpNKGLILLDGQDIRTLQVKWLRS 474
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSIsPGQRV-GLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFADTILENiLMGKENATKKEAIDACIAVNAHNFICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKD 554
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKN-LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 555 PKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIGDHNKLMAQ 624
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1033-1247 |
1.33e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.63 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPS-RPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLD---LKWLR 1108
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1109 LQ---------------TALVGQE-PALFGGtigenirfgnpnaswseVEEAAKEAYIHNFICGLprGYETEVGESGIQL 1172
Cdd:PRK10535 85 REhfgfifqryhllshlTAAQNVEvPAVYAG-----------------LERKQRLLRAQELLQRL--GLEDRVEYQPSQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1173 SGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT-TTIVVVHRLSTIKKANAIAVVQNGKV 1247
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGhTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
398-613 |
1.71e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.68 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYdPN---KGLILLDGQDIRTLQVKWL-R 473
Cdd:PRK13549 6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 474 SQMGMVGQEPVLFAD-TILENILMGKEnATKKEAID-ACIAVNAHNFICDLpqGYDTQVGEKGTQLSGGQKQRIALARAM 551
Cdd:PRK13549 82 AGIAIIHQELALVKElSVLENIFLGNE-ITPGGIMDyDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 552 IKDPKILLLDEPTSALdpkSESLVQQAIDKI----SKGRTTIVIAHRLATVKN-AETIIVLEQGSVI 613
Cdd:PRK13549 159 NKQARLLILDEPTASL---TESETAVLLDIIrdlkAHGIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1051-1289 |
1.72e-17 |
|
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: 85.93 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1051 LREFCLKVK----GGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRD----LDLKWLRLQTALVGQEPALFG 1122
Cdd:TIGR02142 9 LGDFSLDADftlpGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1123 G-TIGENIRFG-------NPNASWSEVEEAAkeayihnficglprGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLL 1194
Cdd:TIGR02142 89 HlSVRGNLRYGmkrarpsERRISFERVIELL--------------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1195 LDEATSALDLESEKHVQDAIRKIIK--RTTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLtnhSNGVYATLVHS 1271
Cdd:TIGR02142 155 MDEPLAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW---ASPDLPWLARE 231
|
250 260
....*....|....*....|....*.
gi 1770234124 1272 E--------MEANADHFSLVQQPVTD 1289
Cdd:TIGR02142 232 DqgsliegvVAEHDQHYGLTALRLGG 257
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1050-1249 |
1.73e-17 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 84.09 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLD---LKWLRLQTALVGQE-PALFGG-- 1123
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDsPSAVNPrm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 TIGENIrfGNPNASWSEVEEAAKEAYIHNFI--CGLPRGYETEVGEsgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSA 1201
Cdd:TIGR02769 106 TVRQII--GEPLRHLTSLDESEQKARIAELLdmVGLRSEDADKLPR---QLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1202 LDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKVSE 1249
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQAfgTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1051-1228 |
2.03e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 83.28 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1051 LREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLrlqtaLVGQEPALFGG-TIGENI 1129
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1130 RFG----NPNASWSEVEEAAKEayiHNFICGLPRGYETEVGesgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLE 1205
Cdd:TIGR01184 76 ALAvdrvLPDLSKSERRAIVEE---HIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180
....*....|....*....|....*
gi 1770234124 1206 SEKHVQDAIRKIIK--RTTTIVVVH 1228
Cdd:TIGR01184 149 TRGNLQEELMQIWEehRVTVLMVTH 173
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
354-611 |
2.11e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.94 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 354 SLSYFAqFAQGTVAASKvfAIIDRI--------PAIDPYSTTGRKPETVHGRLELKNVSFAYPSRMsvPILNSLNLVI-P 424
Cdd:COG4178 314 ALSWFV-DNYQSLAEWR--ATVDRLagfeealeAADALPEAASRIETSEDGALALEDLTLRTPDGR--PLLEDLSLSLkP 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 425 SQRIsALVGASGAGKSTIF-AL--LERFYDpnkGLILLDgQDIRTLqvkwlrsqmgMVGQEPVLFADTILENIL--MGKE 499
Cdd:COG4178 389 GERL-LITGPSGSGKSTLLrAIagLWPYGS---GRIARP-AGARVL----------FLPQRPYLPLGTLREALLypATAE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 500 NATKKEAIDACIAVNAHNFICDLPQGYD-TQVgekgtqLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQA 578
Cdd:COG4178 454 AFSDAELREALEAVGLGHLAERLDEEADwDQV------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL 527
|
250 260 270
....*....|....*....|....*....|...
gi 1770234124 579 IDKISKGRTTIVIAHRLATVKNAETIIVLEQGS 611
Cdd:COG4178 528 LREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
72-339 |
3.31e-17 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 84.02 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 72 LFLIIIGCLGALInggsQPWysyLFGNFVNKIALDNDKDQMIkdvrelcvlmSALSGIVVIGAYLQIACWRL---VGERL 148
Cdd:cd18551 5 LLLSLLGTAASLA----QPL---LVKNLIDALSAGGSSGGLL----------ALLVALFLLQAVLSALSSYLlgrTGERV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 149 GHRIRSKYLRAVLRQDVSFFDTDiSTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVT 228
Cdd:cd18551 68 VLDLRRRLWRRLLRLPVSFFDRR-RSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 229 PLTMFcgvaykaVYVGLAAKEVNSYKKA-------GSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAK 301
Cdd:cd18551 147 PLAFL-------IILPLGRRIRKASKRAqdalgelSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIE 219
|
250 260 270
....*....|....*....|....*....|....*...
gi 1770234124 302 GIGLGVIYLVTYSTWALAFWYGSILVSRNELSGGAAIA 339
Cdd:cd18551 220 ALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVA 257
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
122-357 |
3.45e-17 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 83.93 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 122 LMSALSGIVVIGAYLQIACWRLVGERLGHRIRSKYLRAVLRQDVSFFDtDISTSDIMHGISSDVaqiqevmgDKMSQFI- 200
Cdd:cd18590 41 LMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE-KTKTGDLTSRLSTDT--------TLMSRSVa 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 201 --YHIF--TFI--CG-YIVGFLKSWKVSLAVLAVTPLTMFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSF 273
Cdd:cd18590 112 lnANVLlrSLVktLGmLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 274 VAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYSTWALAFWYGSILVSRNELSGGAAIACFFGVTIGGRGL-A 352
Cdd:cd18590 192 KAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVrT 271
|
....*
gi 1770234124 353 LSLSY 357
Cdd:cd18590 272 LVYIY 276
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
716-994 |
3.57e-17 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 83.69 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 716 GVIFGMLAGAILSLFPLVLGQALtvyfnpDKSKLQKDVGylCLALVGLGFGCILTM-----MGQQGFCGWAGTKLTKRVR 790
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLI------DAALGGGDTA--SLNQIALLLLGLFLLqavfsFFRIYLFARVGERVVADLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 791 DLLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTP-FT 869
Cdd:cd18576 73 KDLYRHLQRLPLSFFH--ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPvVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 870 LGASYFSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAM 949
Cdd:cd18576 151 LVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1770234124 950 YSAYTLVLFFGAYLVKKDYTKFGDVYKIFLILVLSTFSVGQFAGL 994
Cdd:cd18576 231 FGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADL 275
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
400-595 |
3.81e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.56 E-value: 3.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 400 LKNVSFAypsrmsvpilnslnlvIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKW---LRSQ- 475
Cdd:PRK11629 25 LHNVSFS----------------IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MGMVGQEPVLFAD-TILENILM-----GKENATKKE-AIDACIAVnahnficdlpqGYDTQVGEKGTQLSGGQKQRIALA 548
Cdd:PRK11629 89 LGFIYQFHHLLPDfTALENVAMplligKKKPAEINSrALEMLAAV-----------GLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1770234124 549 RAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAHRL 595
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDL 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
980-1261 |
4.32e-17 |
|
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: 88.04 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 980 ILVLSTFSVGQFAGLAPDTSMAStaIPAVFEIMN---RNPLIDGKGKKIEQSKPFDLEFKMVNFAYPSRPDVIV------ 1050
Cdd:TIGR01271 1149 MNILSTLQWAVNSSIDVDGLMRS--VSRVFKFIDlpqEEPRPSGGGGKYQLSTVLVIENPHAQKCWPSGGQMDVqgltak 1226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1051 --------LREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDpIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFG 1122
Cdd:TIGR01271 1227 yteagravLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFS 1305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1123 GTIGENIrfgNPNASWS--EVEEAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATS 1200
Cdd:TIGR01271 1306 GTFRKNL---DPYEQWSdeEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1201 ALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTNHS 1261
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETS 1443
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1033-1293 |
4.57e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAY-PSRPDVI-VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGG----RDLRDLDLKW 1106
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1107 LRLQTALVGQEP--ALFGGTIGENIRFGNPNASWSEvEEAAKEAYIHNFICGLPRGYETEvgeSGIQLSGGQKQRIAIAR 1184
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPK-EKAEKIAAEKLEMVGLADEFWEK---SPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1185 AIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRL--STIKKANAIAVVQNGKVSEYGTHDTL------ 1256
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLmdDVADYADYVYLLEKGHIISCGTPSDVfqevdf 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 1770234124 1257 LTNHSNGVYATLVHSEMEANADHFSLVQQPVTDPEFL 1293
Cdd:PRK13643 238 LKAHELGVPKATHFADQLQKTGAVTFEKLPITRAELV 274
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
398-593 |
4.66e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.83 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQdirtlQVKWLRSQMG 477
Cdd:PRK11248 2 LQISHLYADYGGK---PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQ-EPVLFADTILENILMGKENA----TKKEAIdaciavnAHNFIcdlpqgydTQVGEKGT------QLSGGQKQRIA 546
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQLAgvekMQRLEI-------AHQML--------KKVGLEGAekryiwQLSGGQRQRVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1770234124 547 LARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAH 593
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITH 187
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
398-616 |
4.70e-17 |
|
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: 81.65 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAY-PSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRT--LQVkwlRS 474
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKepAEA---RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFAD-TILENIL-MGKENATKKEAIDACIAVNAHNFicDLPQGYDTQVGEkgtqLSGGQKQRIALARAMI 552
Cdd:cd03266 79 RLGFVSDSTGLYDRlTARENLEyFAGLYGLKGDELTARLEELADRL--GMEELLDRRVGG----FSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 553 KDPKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIG 616
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1050-1261 |
5.17e-17 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; 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: 213256 [Multi-domain] Cd Length: 275 Bit Score: 82.98 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDpIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGGTIGENI 1129
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1130 rfgNPNASWSEVE--EAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESE 1207
Cdd:cd03289 98 ---DPYGKWSDEEiwKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1208 KHVQDAIRKIIKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHDTLLTNHS 1261
Cdd:cd03289 175 QVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKS 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1050-1247 |
5.94e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.42 E-value: 5.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLdlkwlRLQTALVGQEPALFG-GTIGEN 1128
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1129 IRFGnPNASWSEVEEAAKEAYihnficglprGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEK 1208
Cdd:PRK11247 102 VGLG-LKGQWRDAALQALAAV----------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1770234124 1209 HVQDAIRKIIKRT--TTIVVVHRLS-TIKKANAIAVVQNGKV 1247
Cdd:PRK11247 171 EMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
753-965 |
5.98e-17 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 83.16 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 753 VGYLCLALVG--LGFGCiltmmgQQGFCGWAGTKLTKRVRDLLFRSILNQEPGWFdsDQNSPGSLVSKLSVNCTSFRSIL 830
Cdd:cd18590 39 IGLMCLFSLGssLSAGL------RGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFF--EKTKTGDLTSRLSTDTTLMSRSV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 831 GDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPFTLGAS--YFSLIINIGSKLdNDSFDKASGIASAAVSNIRTVT 908
Cdd:cd18590 111 ALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQkvYNTYHQKLSQAV-QDSIAKAGELAREAVSSIRTVR 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 909 TLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMYSAYTLVLFFGAYLVK 965
Cdd:cd18590 190 SFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQ 246
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
416-616 |
6.91e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 81.74 E-value: 6.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 416 LNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIrtlqvkwlrsqmgmvgQEP-----VLFAD-- 488
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----------------TEPgpdrmVVFQNys 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 489 -----TILENI------LMGKENATKKEAIdaciaVNAHNFICDLPQGYDtqvgEKGTQLSGGQKQRIALARAMIKDPKI 557
Cdd:TIGR01184 65 llpwlTVRENIalavdrVLPDLSKSERRAI-----VEEHIALVGLTEAAD----KRPGQLSGGMKQRVAIARALSIRPKV 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 558 LLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRL-ATVKNAETIIVLEQGSVIEIG 616
Cdd:TIGR01184 136 LLLDEPFGALDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1042-1256 |
7.05e-17 |
|
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: 81.40 E-value: 7.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1042 YPSRPDVIVlREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDlDLKWLRLQTALVGQEPALF 1121
Cdd:cd03263 10 YKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1122 GG-TIGENIRF-----GNPNASwsevEEAAKEAYIHnfICGLPRGYETEVGesgiQLSGGQKQRIAIARAIVKKSKVLLL 1195
Cdd:cd03263 88 DElTVREHLRFyarlkGLPKSE----IKEEVELLLR--VLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1196 DEATSALDLESEKHVQDAIRKIIKRTTTIVVVHrlsTIKKANA----IAVVQNGKVSEYGTHDTL 1256
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGRSIILTTH---SMDEAEAlcdrIAIMSDGKLRCIGSPQEL 219
|
|
| Synaptobrevin |
pfam00957 |
Synaptobrevin; |
1469-1548 |
8.13e-17 |
|
Synaptobrevin;
Pssm-ID: 395764 Cd Length: 89 Bit Score: 76.81 E-value: 8.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1469 QRNISKLNDELYEVHQIMTRNVQEVLGVGEKLDQVSQMSSRLTSESRIYADKARDLNRQALIKKWAPVAIVLGVVILLFW 1548
Cdd:pfam00957 2 NDKLAKIQAEVDEVKDIMTENIDKVLERGEKLDLLVDKTENLQSSAQQFRRQARKLKRKMWWKNMKLYIILGLVVLILIL 81
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1056-1258 |
8.85e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.74 E-value: 8.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPAL-FGGTIGENIRFGnp 1134
Cdd:PRK13548 23 LTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVVAMG-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1135 NASWSEVEEAAKEayihnficgLPRGYETEVGESGI------QLSGGQKQRIAIARAIV------KKSKVLLLDEATSAL 1202
Cdd:PRK13548 101 RAPHGLSRAEDDA---------LVAAALAQVDLAHLagrdypQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 1203 DLESEKHVQDAIRKIIKR--TTTIVVVHRLS-TIKKANAIAVVQNGKVSEYGTHDTLLT 1258
Cdd:PRK13548 172 DLAHQHHVLRLARQLAHErgLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
415-571 |
9.04e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.36 E-value: 9.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 415 ILNSLNLVI-PSQRIsALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL---QVKWLRSQ-MGMVGQE----PVL 485
Cdd:PRK10584 25 ILTGVELVVkRGETI-ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhVGFVFQSfmliPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 486 FAdtiLENI-----LMGK-ENATKKEAIDACIAVNAHNFICDLPqgydtqvgekgTQLSGGQKQRIALARAMIKDPKILL 559
Cdd:PRK10584 104 NA---LENVelpalLRGEsSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLF 169
|
170
....*....|..
gi 1770234124 560 LDEPTSALDPKS 571
Cdd:PRK10584 170 ADEPTGNLDRQT 181
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
423-616 |
9.20e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.24 E-value: 9.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 423 IPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRtlqvKWLRSQM-GMVGQE-------PVLFADTILeni 494
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLvAYVPQSeevdwsfPVLVEDVVM--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 495 lMGK---------ENATKKEAIDACIAVnahnfiCDLPQGYDTQVGEkgtqLSGGQKQRIALARAMIKDPKILLLDEPTS 565
Cdd:PRK15056 103 -MGRyghmgwlrrAKKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 566 ALDPKSESLVQQAIDKI-SKGRTTIVIAHRLATVKNAETIIVLEQGSVIEIG 616
Cdd:PRK15056 172 GVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1041-1227 |
9.27e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.97 E-value: 9.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1041 AYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGrdlrDLDLKWLRLQTALVGQEPAL 1120
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1121 FG-----GTIGENIRFGNPNASWSEVEEAAKEAYihnficGLPRGYETEVGEsgiqLSGGQKQRIAIARAIVKKSKVLLL 1195
Cdd:NF040873 74 VRdlvamGRWARRGLWRRLTRDDRAAVDDALERV------GLADLAGRQLGE----LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190
....*....|....*....|....*....|..
gi 1770234124 1196 DEATSALDLESEKHVQDAIRKIIKRTTTIVVV 1227
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVV 175
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
119-562 |
9.42e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 85.62 E-value: 9.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 119 LCVLMsalsgiVVIGAYLQIACWRLvGERLGHRIRSKYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGDkMSQ 198
Cdd:COG4615 57 LLVLL------LLSRLASQLLLTRL-GQHAVARLRLRLSRRILAAPLERLER-IGAARLLAALTEDVRTISQAFVR-LPE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 199 FIYHIFTFICGYI-VGFLkSWKVSLAVLAVTPLTMFcgvaykaVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFS----- 272
Cdd:COG4615 128 LLQSVALVLGCLAyLAWL-SPPLFLLTLVLLGLGVA-------GYRLLVRRARRHLRRAREAEDRLFKHFRALLEgfkel 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 273 --------FVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYSTWALAFWYGSIlvSRNELSGGAAIACFFgv 344
Cdd:COG4615 200 klnrrrrrAFFDEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWA--DPAVLSGFVLVLLFL-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 345 tiggRG-LALSLSYFAQFAQGTVAASKVFAIIDRIPAIDPYSTTGRKPETVHG--RLELKNVSFAYPSR--MSVPILNSL 419
Cdd:COG4615 276 ----RGpLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEdgDEGFTLGPI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 420 NLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADtileniLMGKE 499
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLD 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 500 NATKKEAIDAciavnahnficdlpqgY------DTQVGEKG-----TQLSGGQKQRIALARAMIKDPKILLLDE 562
Cdd:COG4615 426 GEADPARARE----------------LlerlelDHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1033-1247 |
1.09e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.06 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEP--ALFGGTIGENIRFGNPNASW------SEVEEAAKEAYIHNFICGLPrgyetevgesgIQLSGGQKQRIAIAR 1184
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIpreemiKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1185 AIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKKANAIAVVQNGKV 1247
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
416-613 |
1.13e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 81.32 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 416 LNSLNLVIPSQRISALVGASGAGKSTifallerFYD-------PNKGLILLDGQDIRTL---QVkwlrSQMGmVG---QE 482
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTT-------LMDvitgktrPDSGSVLFGGTDLTGLdehEI----ARLG-IGrkfQK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 483 PVLFAD-TILENI-------------LMGKENATKKEAIDACIAvnahnfICDLPQGYDTQVGEkgtqLSGGQKQRIALA 548
Cdd:COG4674 94 PTVFEElTVFENLelalkgdrgvfasLFARLTAEERDRIEEVLE------TIGLTDKADRLAGL----LSHGQKQWLEIG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 549 RAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKN-AETIIVLEQGSVI 613
Cdd:COG4674 164 MLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQiARKVTVLHQGSVL 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
397-625 |
1.18e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.09 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQV-KWLRSQ 475
Cdd:PRK10895 3 TLTAKNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MGMVGQEPVLFADTILENILMG----KENATKKEAIDACIAVNAHNFICDLPQGYdtqvgekGTQLSGGQKQRIALARAM 551
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAvlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 552 IKDPKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRL-ATVKNAETIIVLEQGSVIEIGDHNKLMAQE 625
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLrDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1033-1254 |
1.24e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.21 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGG------RDLRDLDLKW 1106
Cdd:COG4161 3 IQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1107 LRLQTALVGQE----PALfggTIGENIrfgnpNASWSEVEEAAKEAYIHNFICGLPRGYETEVGES-GIQLSGGQKQRIA 1181
Cdd:COG4161 80 LRQKVGMVFQQynlwPHL---TVMENL-----IEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRfPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1182 IARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKiIKRT--TTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHD 1254
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRE-LSQTgiTQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1050-1254 |
1.41e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.21 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwlRLQTALVGQEPALFGG-TIGEN 1128
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1129 IRFG--------NPNAswseveeaakeAYIHNFICGL----------PRgYETevgesgiQLSGGQKQRIAIARAIVKKS 1190
Cdd:PRK10851 95 IAFGltvlprreRPNA-----------AAIKAKVTQLlemvqlahlaDR-YPA-------QLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1191 KVLLLDEATSALDLESEKHVQDAIRKI---IKRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGTHD 1254
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLheeLKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1050-1249 |
1.46e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.66 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLD---LKWLRLQTALVGQEPalFGG--- 1123
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDS--ISAvnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 --TIGENIRfgNPNASWSEVEEAAKEAYIHNFI--CGLPrgyETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEAT 1199
Cdd:PRK10419 105 rkTVREIIR--EPLRHLLSLDKAERLARASEMLraVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1200 SALDLESEKHVQDAIRKIIKRTTT--IVVVHRLSTIKK-ANAIAVVQNGKVSE 1249
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
398-624 |
1.52e-16 |
|
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: 84.85 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPS--RMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLI-------LLDGQDIRTLQ 468
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 469 VKWLRSQMGMVGQEPVLFAD-TILENIL------MGKENATKKeaidACIAVNAHNFicdlPQGYDTQVGEKGT-QLSGG 540
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPHrTVLDNLTeaigleLPDELARMK----AVITLKMVGF----DEEKAEEILDKYPdELSEG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 541 QKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGD 617
Cdd:TIGR03269 432 ERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGD 511
|
....*..
gi 1770234124 618 HNKLMAQ 624
Cdd:TIGR03269 512 PEEIVEE 518
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
121-371 |
1.73e-16 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 82.17 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 121 VLMSALSGIVvigAYLQIACWRLVGERLGHRIRSKYLRAVLRQDVSFFDTDiSTSDIMHGISSDVAQIQEVMGDKMSQFI 200
Cdd:cd18564 61 VGIALLRGLA---SYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRR-RTGDLLSRLTGDVGAIQDLLVSGVLPLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 201 YHIFTFIcGYI-VGFLKSWKVSLAVLAVTPLtMFCGVAYKAVYVGLAAKEVNsyKKAGSIA---EQAIGSIRTVFSFVAE 276
Cdd:cd18564 137 TNLLTLV-GMLgVMFWLDWQLALIALAVAPL-LLLAARRFSRRIKEASREQR--RREGALAsvaQESLSAIRVVQAFGRE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 277 DSLAARYDAVLDESVPIG---KKL--GFAKGIGLgviyLVTYSTwALAFWYGSILVSRNELSGGAAIAcfFGVTIGG--- 348
Cdd:cd18564 213 EHEERRFARENRKSLRAGlraARLqaLLSPVVDV----LVAVGT-ALVLWFGAWLVLAGRLTPGDLLV--FLAYLKNlyk 285
|
250 260
....*....|....*....|....*
gi 1770234124 349 --RGLAlslSYFAQFAQGTVAASKV 371
Cdd:cd18564 286 pvRDLA---KLTGRIAKASASAERV 307
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
416-621 |
1.84e-16 |
|
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: 80.11 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 416 LNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTlQVKWLRSQMGMVGQEPVLfaDTIL---E 492
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV--DDELtgwE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 493 NILM-----GKENATKKEAIDACIAvnahnFIcDLPQGYDTQVGekgtQLSGGQKQRIALARAMIKDPKILLLDEPTSAL 567
Cdd:cd03265 93 NLYIharlyGVPGAERRERIDELLD-----FV-GLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 568 DPKSESLVQQAIDKISK--GRTTIVIAHRLATV-KNAETIIVLEQGSVIEIGDHNKL 621
Cdd:cd03265 163 DPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
72-339 |
1.90e-16 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 81.71 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 72 LFLIIIGCLGALINggsqPWysyLFGNFVNKIALDNDKDQMIKdvreLCVLMSALSGIVVIGAYLQIACWRLVGERLGHR 151
Cdd:cd18542 5 ILALLLATALNLLI----PL---LIRRIIDSVIGGGLRELLWL----LALLILGVALLRGVFRYLQGYLAEKASQKVAYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 152 IRSKYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLt 231
Cdd:cd18542 74 LRNDLYDHLQRLSFSFHDK-ARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPF- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 232 mfcgVAYKAVYVGLAAKEVnsYKKA-------GSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIG 304
Cdd:cd18542 152 ----IALFSYVFFKKVRPA--FEEIreqegelNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKY 225
|
250 260 270
....*....|....*....|....*....|....*
gi 1770234124 305 LGVIYLVTYSTWALAFWYGSILVSRNELSGGAAIA 339
Cdd:cd18542 226 WPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVA 260
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1259 |
2.15e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 81.32 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSrpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEP--ALFGGTIGENIRFG--NPNASWSEVEEAAKEAY----IHNFICGLPRgyetevgesgiQLSGGQKQRIAIAR 1184
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERRVEEALkavrMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1185 AIVKKSKVLLLDEATSALDLESekhvQDAIRKIIKR-----TTTIVVVHRLS-TIKKANAIAVVQNGKVSEYGThDTLLT 1258
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRG----QETLMEILDRlhnqgKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLT 226
|
.
gi 1770234124 1259 N 1259
Cdd:PRK13647 227 D 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
398-624 |
2.70e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 80.65 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMS------VPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKW 471
Cdd:COG4167 5 LEVRNLSKTFKYRTGlfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 472 lRSQ-MGMVGQEPV------LFADTILE-----NILMgkENATKKEAIdaciavnahnficdlpqgYDT--QVGEKGTQ- 536
Cdd:COG4167 85 -RCKhIRMIFQDPNtslnprLNIGQILEeplrlNTDL--TAEEREERI------------------FATlrLVGLLPEHa 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 537 ------LSGGQKQRIALARAMIKDPKILLLDEPTSALDPkseSLVQQAIDKI-----SKGRTTIVIAHRLATVKN-AETI 604
Cdd:COG4167 144 nfyphmLSSGQKQRVALARALILQPKIIIADEALAALDM---SVRSQIINLMlelqeKLGISYIYVSQHLGIVKHiSDKV 220
|
250 260
....*....|....*....|
gi 1770234124 605 IVLEQGSVIEIGDHNKLMAQ 624
Cdd:COG4167 221 LVMHQGEVVEYGKTAEVFAN 240
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
432-621 |
3.04e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 81.68 E-value: 3.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 432 VGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL-QVKWL--RSQMGMVGQEPV-------LFADTILENILMGKENA 501
Cdd:PRK15079 53 VGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkDDEWRavRSDIQMIFQDPLaslnprmTIGEIIAEPLRTYHPKL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 502 TKKEAIDACIAVNAH-----NFICDLPQgydtqvgekgtQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQ 576
Cdd:PRK15079 133 SRQEVKDRVKAMMLKvgllpNLINRYPH-----------EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVV 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1770234124 577 QAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGDHNKL 621
Cdd:PRK15079 202 NLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
430-611 |
3.58e-16 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 79.40 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 430 ALVGASGAGKSTIFALLERFYDPNKGLILLDGQ----DIRTL---QVKWLRSQ-MGMVGQ---------------EPVLf 486
Cdd:COG4778 41 ALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAsprEILALRRRtIGYVSQflrviprvsaldvvaEPLL- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 487 adtileniLMGKENAT-KKEAIDACIAVNahnficdLPqgydtqvgEKGTQL-----SGGQKQRIALARAMIKDPKILLL 560
Cdd:COG4778 120 --------ERGVDREEaRARARELLARLN-------LP--------ERLWDLppatfSGGEQQRVNIARGFIADPPLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 561 DEPTSALDPKSESLVQQAI-DKISKGRTTIVIAHRLATVKN-AETIIVLEQGS 611
Cdd:COG4778 177 DEPTASLDAANRAVVVELIeEAKARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
398-617 |
4.07e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.30 E-value: 4.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwLRSQMG 477
Cdd:PRK09700 6 ISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 --MVGQE-PVLFADTILENILMGKENATKKEAIDAC------IAVNAHNFICDLPQGYDTQVGEkgtqLSGGQKQRIALA 548
Cdd:PRK09700 82 igIIYQElSVIDELTVLENLYIGRHLTKKVCGVNIIdwremrVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 549 RAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLATVKN-AETIIVLEQGSVIEIGD 617
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGM 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1048-1228 |
4.39e-16 |
|
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: 79.40 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1048 VIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLD---LkwLRLQTALVG---QE---- 1117
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedaR--ARLRARHVGfvfQSfqll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1118 PALfggTIGENI-----RFGNPNAswsevEEAAKEAyihnficgLPRgyeteVGESG------IQLSGGQKQRIAIARAI 1186
Cdd:COG4181 103 PTL---TALENVmlpleLAGRRDA-----RARARAL--------LER-----VGLGHrldhypAQLSGGEQQRVALARAF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1770234124 1187 VKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVH 1228
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRErgTTLVLVTH 205
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
719-964 |
4.98e-16 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 80.43 E-value: 4.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 719 FGMLAGAILSLF-PLVLGQAL-TVYFNPDKSKLQKDVGYLCLALVGLGF-----GCILTMmgqqgfcgwAGTKLTKRVRD 791
Cdd:cd18784 3 FFLLAAAVGEIFiPYYTGQVIdGIVIEKSQDKFSRAIIIMGLLAIASSVaagirGGLFTL---------AMARLNIRIRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 792 LLFRSILNQEPGWFDSdqNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPFTLG 871
Cdd:cd18784 74 LLFRSIVSQEIGFFDT--VKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 872 AS-YFSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMY 950
Cdd:cd18784 152 VSkVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTEL 231
|
250
....*....|....
gi 1770234124 951 SAYTLVLFFGAYLV 964
Cdd:cd18784 232 ALTVSTLYYGGHLV 245
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1039-1252 |
5.50e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 80.23 E-value: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1039 NFAYPSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEP 1118
Cdd:PRK13652 8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1119 --ALFGGTIGENIRFGNPNASWSE------VEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIAIARAIVKKS 1190
Cdd:PRK13652 88 ddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1191 KVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGT 1252
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGT 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1033-1258 |
5.59e-16 |
|
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: 79.36 E-value: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPI-GGKVMMGGRDLRDLDLKWLR--- 1108
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTyGNDVRLFGERRGGEDVWELRkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1109 ------LQTALVGQEPAL------FGGTIGeniRFGNPNAswsEVEEAAKEAyIHNFicGLP----RGYETevgesgiqL 1172
Cdd:COG1119 81 glvspaLQLRFPRDETVLdvvlsgFFDSIG---LYREPTD---EQRERAREL-LELL--GLAhladRPFGT--------L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1173 SGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRL----STIKKAnaiAVVQNGK 1246
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVeeipPGITHV---LLLKDGR 220
|
250
....*....|..
gi 1770234124 1247 VSEYGTHDTLLT 1258
Cdd:COG1119 221 VVAAGPKEEVLT 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1033-1225 |
5.76e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.52 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYP-SRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLR--DLDlkwlRl 1109
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpGAD----R- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 qtALVGQEPALFGG-TIGENIRFGNPNASwseVEEAAKEAYIHNFI--CGLprgyeTEVGESGI-QLSGGQKQRIAIARA 1185
Cdd:COG4525 79 --GVVFQKDALLPWlNVLDNVAFGLRLRG---VPKAERRARAEELLalVGL-----ADFARRRIwQLSGGMRQRVGIARA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1770234124 1186 IVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIV 1225
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGV 188
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
431-610 |
6.10e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.76 E-value: 6.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 431 LVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL---QVKWLRSQMGMVGQEPVLFAD-TILEN-----ILMGKENA 501
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQIGMIFQDHHLLMDrTVYDNvaiplIIAGASGD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 502 TKKEAIDACIAV-----NAHNFicdlpqgydtqvgekGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQ 576
Cdd:PRK10908 113 DIRRRVSAALDKvglldKAKNF---------------PIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 1770234124 577 QAIDKISK-GRTTIVIAHRLATV-KNAETIIVLEQG 610
Cdd:PRK10908 178 RLFEEFNRvGVTVLMATHDIGLIsRRSYRMLTLSDG 213
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
397-621 |
6.32e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAypsRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVkwlRSQM 476
Cdd:PRK13539 2 MLEGEDLACV---RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQ----EPVLfadTILENILMGKE-NATKKEAIDACI-AVNAHNfICDLPQGYdtqvgekgtqLSGGQKQRIALARA 550
Cdd:PRK13539 76 HYLGHrnamKPAL---TVAENLEFWAAfLGGEELDIAAALeAVGLAP-LAHLPFGY----------LSAGQKRRVALARL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 551 MIKDPKILLLDEPTSALDPKSESLVqqaidkiskgrTTIVIAHrlatvknaetiivLEQGSVIEIGDHNKL 621
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAAAVALF-----------AELIRAH-------------LAQGGIVIAATHIPL 188
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1047-1256 |
8.92e-16 |
|
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: 78.18 E-value: 8.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDlDLKWLRLQTALVGQEPALFGGTIG 1126
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1127 -ENIR-----FGNPNASWSE-VEEAAKEAYIHNFICGLPRGYetevgesgiqlSGGQKQRIAIARAIVKKSKVLLLDEAT 1199
Cdd:cd03265 91 wENLYiharlYGVPGAERRErIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1200 SALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTL 1256
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEfgMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
398-646 |
9.61e-16 |
|
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: 82.16 E-value: 9.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERF--YDPNKGLIL----------------- 458
Cdd:TIGR03269 1 IEVKNLTKKFDG---KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 459 -----------LDGQDI------RTLQVKWLRSQMGMVGQEPVLFAD-TILENILMGKENA--TKKEAIDACIavnahnf 518
Cdd:TIGR03269 78 vgepcpvcggtLEPEEVdfwnlsDKLRRRIRKRIAIMLQRTFALYGDdTVLDNVLEALEEIgyEGKEAVGRAV------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 519 icDLPQgyDTQVGEKGTQ----LSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDK--ISKGRTTIVIA 592
Cdd:TIGR03269 151 --DLIE--MVQLSHRITHiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTS 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 593 HRLATVKN-AETIIVLEQGSVIEIGDHNKLMAQEGAYFSLIKLATEAISSNPVSK 646
Cdd:TIGR03269 227 HWPEVIEDlSDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIK 281
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1039-1251 |
1.65e-15 |
|
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: 77.19 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1039 NFAYPSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwlrlqtalVGQEP 1118
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG--------GGFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1119 ALfggTIGENIRFgnpNASW---SEVEEAAKEAYIHNFiCGLPRGYETEVGEsgiqLSGGQKQRIAIARAIVKKSKVLLL 1195
Cdd:cd03220 98 EL---TGRENIYL---NGRLlglSRKEIDEKIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1196 DEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYG 1251
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1033-1254 |
1.85e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 77.75 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGR--DLR----DLDLKW 1106
Cdd:PRK11124 3 IQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSktpsDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1107 LRLQTALVGQE----PALfggTIGENIRFGNPNASWSEVEEAAKEAYIHnficgLPRGYETEVGES-GIQLSGGQKQRIA 1181
Cdd:PRK11124 80 LRRNVGMVFQQynlwPHL---TVQQNLIEAPCRVLGLSKDQALARAEKL-----LERLRLKPYADRfPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1182 IARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKiIKRT--TTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHD 1254
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE-LAETgiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1051-1252 |
2.64e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.28 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1051 LREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDL----RDLDLKWLRLQTALVGQ--EPALFGGT 1124
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRPVRKRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1125 IGENIRFGNPNASWsEVEEAAKEAYIHNFICGLPRGYeteVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDL 1204
Cdd:PRK13646 103 VEREIIFGPKNFKM-NLDEVKNYAHRLLMDLGFSRDV---MSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1205 ESEKHVQDAIRKI-IKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYGT 1252
Cdd:PRK13646 179 QSKRQVMRLLKSLqTDENKTIILVsHDMNEVARyADEVIVMKEGSIVSQTS 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
415-593 |
2.98e-15 |
|
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: 76.54 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 415 ILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNK---GLILLDGQDIRTLQVKwlrSQMGMVGQ---------- 481
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQ---KCVAYVRQddillpgltv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 482 -EPVLFADTILENILMGKENATKKEAIDACIAVNahnficdlpqgyDTQVG-EKGTQLSGGQKQRIALARAMIKDPKILL 559
Cdd:cd03234 99 rETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLA------------LTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190
....*....|....*....|....*....|....*
gi 1770234124 560 LDEPTSALDPKSE-SLVQQAIDKISKGRTTIVIAH 593
Cdd:cd03234 167 LDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
398-594 |
3.44e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.76 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWlRSQMG 477
Cdd:PRK13540 2 LDVIELDFDYHDQ---PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQE----PVLfadTILENILMGKENATKKEAIDACIAVNAHNFICDLPQGYdtqvgekgtqLSGGQKQRIALARAMIK 553
Cdd:PRK13540 78 FVGHRsginPYL---TLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1770234124 554 DPKILLLDEPTSALDPKS-ESLVQQAIDKISKGRTTIVIAHR 594
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
398-625 |
3.67e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.80 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAypSRmsvpiLNSLNLVIPSQRISALVGASGAGKSTIFALLERFYdPNKGLILLDGQDIRTLQVKWLRSQMG 477
Cdd:COG4138 1 LQLNDVAVA--GR-----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQE-PVLFADTILENILMGKENATKKEAIDACIAVNAHNF-ICDLpqgYDTQVgekgTQLSGGQKQRIALARAMIK-- 553
Cdd:COG4138 73 YLSQQqSPPFAMPVFQYLALHQPAGASSEAVEQLLAQLAEALgLEDK---LSRPL----TQLSGGEWQRVRLAAVLLQvw 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 554 -----DPKILLLDEPTSALDpksesLVQQ-AIDKI-----SKGRTTIVIAHRLA-TVKNAETIIVLEQGSVIEIGDHNKL 621
Cdd:COG4138 146 ptinpEGQLLLLDEPMNSLD-----VAQQaALDRLlrelcQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEV 220
|
....
gi 1770234124 622 MAQE 625
Cdd:COG4138 221 MTPE 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1048-1230 |
5.15e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.66 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1048 VIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDlKWLRlqTALVG---QEPALfgGT 1124
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKR--AKYIGrvfQDPMM--GT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1125 -----IGEN------------IRFGNPNAswseveeaaKEAYIHNFICGLPRGYE----TEVGesgiQLSGGQKQRIAIA 1183
Cdd:COG1101 94 apsmtIEENlalayrrgkrrgLRRGLTKK---------RRELFRELLATLGLGLEnrldTKVG----LLSGGQRQALSLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1770234124 1184 RAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT--TTIVVVHRL 1230
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNM 209
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1056-1256 |
5.21e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.82 E-value: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDL------------------------DLKWLRLQT 1111
Cdd:PRK13651 28 VEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqktrfkkikKIKEIRRRV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVGQ--EPALFGGTIGENIRFGnPNASWSEVEEAAKEA--YIHnfICGLPRGYeteVGESGIQLSGGQKQRIAIARAIV 1187
Cdd:PRK13651 108 GVVFQfaEYQLFEQTIEKDIIFG-PVSMGVSKEEAKKRAakYIE--LVGLDESY---LQRSPFELSGGQKRRVALAGILA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1188 KKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRL-STIKKANAIAVVQNGKVSEYG-THDTL 1256
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVtHDLdNVLEWTKRTIFFKDGKIIKDGdTYDIL 253
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1056-1259 |
5.90e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.82 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLR---------LQTALVGQEPAL-FGGTI 1125
Cdd:PRK15079 42 LRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavrsdiqmiFQDPLASLNPRMtIGEII 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1126 GENIRFGNPNASWSEVEEAAKE-----AYIHNFICGLPRgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLLLDEATS 1200
Cdd:PRK15079 122 AEPLRTYHPKLSRQEVKDRVKAmmlkvGLLPNLINRYPH-----------EFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1201 ALDLESEKHVQDAIRKIIKRT--TTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1048-1247 |
6.62e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 76.23 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1048 VIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRdldlkwlRLQTALV---G-----QEPA 1119
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT-------GLPPHRIarlGiartfQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1120 LFGG-TIGENIRFG--------------NPNASWSEVEEAAKEAY--IHnfICGLPRGYETEVGEsgiqLSGGQKQRIAI 1182
Cdd:COG0411 90 LFPElTVLENVLVAaharlgrgllaallRLPRARREEREARERAEelLE--RVGLADRADEPAGN----LSYGQQRRLEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1183 ARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT-TTIVVV-HRLSTIKK-ANAIAVVQNGKV 1247
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgITILLIeHDMDLVMGlADRIVVLDFGRV 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
398-604 |
6.77e-15 |
|
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: 75.09 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRsQMG 477
Cdd:TIGR01189 1 LAARNLACSRGERM---LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENI-----LMGKENATKKEAIDAcIAVNAHNficDLPQGydtqvgekgtQLSGGQKQRIALARAM 551
Cdd:TIGR01189 77 YLGHLPGLKPElSALENLhfwaaIHGGAQRTIEDALAA-VGLTGFE---DLPAA----------QLSAGQQRRLALARLW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 552 IKDPKILLLDEPTSALDPKSESLVQQAIDK-ISKGRTTIVIAHRLATVKNAETI 604
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDLGLVEAREL 196
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
389-613 |
6.98e-15 |
|
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: 75.83 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 389 RKPETVHGRLElknvSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQ 468
Cdd:cd03267 14 SKEPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 469 VKWLRsQMGMV-GQEPVLFAD-TILENILMGK-----ENATKKEAIDACIAvnahnfICDLPQGYDTQVgekgTQLSGGQ 541
Cdd:cd03267 90 KKFLR-RIGVVfGQKTQLWWDlPVIDSFYLLAaiydlPPARFKKRLDELSE------LLDLEELLDTPV----RQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 542 KQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVI--AHRLATV-KNAETIIVLEQGSVI 613
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLL 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
398-610 |
7.30e-15 |
|
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: 79.48 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYdPN---KGLILLDGQDIRTLQVKWL-R 473
Cdd:TIGR02633 2 LEMKGIVKTFGG---VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 474 SQMGMVGQEPVLFAD-TILENILMGKENATKKEAID-ACIAVNAHNFICDLpQGYDTQVGEKGTQLSGGQKQRIALARAM 551
Cdd:TIGR02633 78 AGIVIIHQELTLVPElSVAENIFLGNEITLPGGRMAyNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 552 IKDPKILLLDEPTSALDPKSESLVQQAI-DKISKGRTTIVIAHRLATVKN-AETIIVLEQG 610
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIrDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
398-614 |
7.92e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.06 E-value: 7.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYdPN---KGLILLDGQdirTLQVKWLRS 474
Cdd:NF040905 2 LEMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGE---VCRFKDIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 --QMGMV--GQE----PVLfadTILENILMGKE---------NATKKEAIDACIAVNAHnficDLPqgyDTQVGEKGTql 537
Cdd:NF040905 75 seALGIViiHQElaliPYL---SIAENIFLGNErakrgvidwNETNRRARELLAKVGLD----ESP---DTLVTDIGV-- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 538 sgGQKQRIALARAMIKDPKILLLDEPTSAL-DPKSESLVQQAIDKISKGRTTIVIAHRLATV-KNAETIIVLEQGSVIE 614
Cdd:NF040905 143 --GKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
398-614 |
8.58e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.26 E-value: 8.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPS------RMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL---Q 468
Cdd:PRK10419 4 LNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 469 VKWLRSQMGMVGQEPVLFAD---TILENI------LMGKENATKKEAIDACI-AVNAHNFICD-LPQgydtqvgekgtQL 537
Cdd:PRK10419 84 RKAFRRDIQMVFQDSISAVNprkTVREIIreplrhLLSLDKAERLARASEMLrAVDLDDSVLDkRPP-----------QL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 538 SGGQKQRIALARAMIKDPKILLLDEPTSALDpksesLVQQA--IDKISK-----GRTTIVIAHRLATVKN-AETIIVLEQ 609
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLD-----LVLQAgvIRLLKKlqqqfGTACLFITHDLRLVERfCQRVMVMDN 227
|
....*
gi 1770234124 610 GSVIE 614
Cdd:PRK10419 228 GQIVE 232
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1049-1229 |
9.46e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 73.73 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1049 IVLREFCLKVKGGTMVAVVGGSGSGKSTV------IWlmqrfydPIG-GKVMMGGRDlrdldlkwlrlQTALVGQEPALF 1121
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLfralagLW-------PWGsGRIGMPEGE-----------DLLFLPQRPYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1122 GGTIGENIRFgnPnasWSEVeeaakeayihnficglprgyetevgesgiqLSGGQKQRIAIARAIVKKSKVLLLDEATSA 1201
Cdd:cd03223 77 LGTLREQLIY--P---WDDV------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180
....*....|....*....|....*...
gi 1770234124 1202 LDLESEKHVQDAIRKiiKRTTTIVVVHR 1229
Cdd:cd03223 122 LDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1056-1277 |
9.54e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.20 E-value: 9.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLM----------QRFYDPIGGKVMMGGRDLRdlDLKWLRLQTALVGQEPALFGG-T 1124
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksaGSHIELLGRTVQREGRLAR--DIRKSRANTGYIFQQFNLVNRlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1125 IGENIRFGNPNAS--WSEVEEAAKEAYIHNFICGLPR-GYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSA 1201
Cdd:PRK09984 103 VLENVLIGALGSTpfWRTCFSWFTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 1202 LDLESEKHVQDAIRKIIKR--TTTIVVVHRLS-TIKKANAIAVVQNGKVSEYGTHDTLLTNHSNGVYATLVHSEMEANA 1277
Cdd:PRK09984 183 LDPESARIVMDTLRDINQNdgITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERFDHLYRSINRVEENAKA 261
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1047-1259 |
1.36e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.81 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTV--------------IWLmQRFYdpIGGKVMMGGRDLRDL-----DLKWL 1107
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLvthfnglikskygtIQV-GDIY--IGDKKNNHELITNPYskkikNFKEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1108 RLQTALVGQEP--ALFGGTIGENIRFGnPNASWSEVEEAAKEAYIHNFICGLPRGYeteVGESGIQLSGGQKQRIAIARA 1185
Cdd:PRK13631 115 RRRVSMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1186 IVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT-TTIVVVHRLSTI-KKANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTD 266
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
398-570 |
1.44e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.19 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsVPILNSLNLVIPSQRISALVGASGAGKSTIF---ALLERFYDpnkGLILLDGQDIRTLQVKwLRS 474
Cdd:PRK11650 4 LKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLrmvAGLERITS---GEIWIGGRVVNELEPA-DRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 qMGMVGQEPVLFAD-TILENILMGKENA-TKKEAIDACIAVNAHnfICDLPQGYDtqvgEKGTQLSGGQKQRIALARAMI 552
Cdd:PRK11650 78 -IAMVFQNYALYPHmSVRENMAYGLKIRgMPKAEIEERVAEAAR--ILELEPLLD----RKPRELSGGQRQRVAMGRAIV 150
|
170
....*....|....*...
gi 1770234124 553 KDPKILLLDEPTSALDPK 570
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAK 168
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1050-1251 |
1.48e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.26 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYD-----PIGGKVMMGGRDL--RDLDLKWLRLQTALVGQEPALFG 1122
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1123 G-TIGENIRFG-------NPNASWSE-VEEAAKEAYIHNFICGLPRGYETevgesgiQLSGGQKQRIAIARAIVKKSKVL 1193
Cdd:PRK14267 99 HlTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWDEVKDRLNDYPS-------NLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 1194 LLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYG 1251
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
398-614 |
2.14e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.82 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSV-PILNSLNLVIPSQRISALVGASGAGKS-TIFALLERFYDPN----KGLILLDGQDIRTLQVKW 471
Cdd:PRK15134 6 LAIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 472 LR----SQMGMVGQEPVLFADTI--LENIL---------MGKEnATKKEAIDACIAV---NAHNFICDLPQgydtqvgek 533
Cdd:PRK15134 86 LRgvrgNKIAMIFQEPMVSLNPLhtLEKQLyevlslhrgMRRE-AARGEILNCLDRVgirQAAKRLTDYPH--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 534 gtQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLEQG 610
Cdd:PRK15134 156 --QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
....
gi 1770234124 611 SVIE 614
Cdd:PRK15134 234 RCVE 237
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1033-1259 |
2.65e-14 |
|
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: 74.25 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPsrpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRdldlkwlRLQT- 1111
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT-------GLPPh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 -------ALVGQEPALFGG-TIGENIRFG-NPNASWSEVEEAAKEAYiHNFicglPRgyeteVGE----SGIQLSGGQKQ 1178
Cdd:COG0410 74 riarlgiGYVPEGRRIFPSlTVEENLLLGaYARRDRAEVRADLERVY-ELF----PR-----LKErrrqRAGTLSGGEQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1179 RIAIARAIVKKSKVLLLDEATSALdleSEKHVQ---DAIRKIIKRTTTIVVV-HRLstiKKANAIA----VVQNGKVSEY 1250
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPSLGL---APLIVEeifEIIRRLNREGVTILLVeQNA---RFALEIAdrayVLERGRIVLE 217
|
....*....
gi 1770234124 1251 GTHDTLLTN 1259
Cdd:COG0410 218 GTAAELLAD 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1063-1269 |
3.16e-14 |
|
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: 78.52 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1063 MVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLrDLDLKWLRLQTALVGQEPALFGG-TIGENIRFGN--PNASWS 1139
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFYAqlKGRSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1140 EVEeAAKEAYIHNficglpRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIK 1219
Cdd:TIGR01257 1037 EAQ-LEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS 1109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1220 RTTTIVVVHRLSTIK-KANAIAVVQNGKVSEYGTHDTLLTNHSNGVYATLV 1269
Cdd:TIGR01257 1110 GRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLV 1160
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1038-1244 |
4.46e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1038 VNFAYPSRpdvIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQE 1117
Cdd:PRK10575 17 VSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1118 -PALFGGTIGENI------------RFGNpnASWSEVEEAAKeayihnfICGLpRGYETEVGESgiqLSGGQKQRIAIAR 1184
Cdd:PRK10575 94 lPAAEGMTVRELVaigrypwhgalgRFGA--ADREKVEEAIS-------LVGL-KPLAHRLVDS---LSGGERQRAWIAM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1185 AIVKKSKVLLLDEATSALDLESEKHVqdairkiikrtttIVVVHRLSTIKKANAIAVVQN 1244
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDV-------------LALVHRLSQERGLTVIAVLHD 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
415-593 |
4.89e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.01 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 415 ILNSLNLVIPSQRISALVGASGAGKSTIFALLErFYDPN----KGLILLDGqdiRTLQVKWLRSQMGMVGQEPVLFAD-T 489
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIPTlT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 490 ILENIL------MGKENAT--KKEAIDACI-AVNahnficdLPQGYDTQVGEKGTQ--LSGGQKQRIALARAMIKDPKIL 558
Cdd:TIGR00955 116 VREHLMfqahlrMPRRVTKkeKRERVDEVLqALG-------LRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 1770234124 559 LLDEPTSALDPKSESLVQQAIDKIS-KGRTTIVIAH 593
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAqKGKTIICTIH 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1040-1251 |
5.02e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.27 E-value: 5.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1040 FAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGR--DLRDLDLKWLRLQTALVGQE 1117
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1118 P--ALFGGTIGENIRFGNPNASWSEVEEAAK--EAyihnficgLPRGYETEVGESGIQ-LSGGQKQRIAIARAIVKKSKV 1192
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNLGVPEAEITRRvdEA--------LTLVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1193 LLLDEATSALDLESEKHVQDAIRKIIKRTTTIVV-VHRLSTIKK-ANAIAVVQNGKVSEYG 1251
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHG 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1252 |
5.02e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.50 E-value: 5.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPDVivLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGR--DLRDLDLKWLRLQ 1110
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1111 TALVGQEP--ALFGGTIGENIRFGNPNASW--SEVEEAAKEAYIHNFICGLpRGYETEVgesgiqLSGGQKQRIAIARAI 1186
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHL-KDKPTHC------LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 1187 VKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT--TTIVVVHRLSTIK-KANAIAVVQNGKVSEYGT 1252
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGN 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1045-1215 |
5.67e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.60 E-value: 5.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1045 RPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLkwlRLQTALVGQ----EPAL 1120
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLGHrnamKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1121 fggTIGENIRF-----GNPNASwseVEEAAkEAYIHNFICGLPRGYetevgesgiqLSGGQKQRIAIARAIVKKSKVLLL 1195
Cdd:PRK13539 89 ---TVAENLEFwaaflGGEELD---IAAAL-EAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWIL 151
|
170 180
....*....|....*....|
gi 1770234124 1196 DEATSALDLESEKHVQDAIR 1215
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIR 171
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1044-1215 |
6.07e-14 |
|
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: 72.14 E-value: 6.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1044 SRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRlQTALVGQEPALFGG 1123
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR-GLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 -TIGENIRFGNPNASWSEVEEAAKEAyihnficGLpRGYETEVGEsgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSAL 1202
Cdd:cd03231 88 lSVLENLRFWHADHSDEQVEEALARV-------GL-NGFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170
....*....|...
gi 1770234124 1203 DLESEKHVQDAIR 1215
Cdd:cd03231 157 DKAGVARFAEAMA 169
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1050-1237 |
1.02e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.54 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDL------DLKWLRLQ------------T 1111
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaakaELRNQKLGfiyqfhhllpdfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVG-QEPALFGGTigenirfgNPnaswSEVEEAAKEAYIhnficglPRGYETEVGESGIQLSGGQKQRIAIARAIVKKS 1190
Cdd:PRK11629 104 ALENvAMPLLIGKK--------KP----AEINSRALEMLA-------AVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1770234124 1191 KVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKKAN 1237
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLqgTAFLVVTHDLQLAKRMS 213
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
722-964 |
1.08e-13 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 73.29 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 722 LAGAILSLFPLVLGQALTV-----YFNPDKSKLQKDVGYLCLALVGLGFGCILTMMgqqgFCGWAGTKLTKRVRDLLFRS 796
Cdd:cd18575 3 IALLIAAAATLALGQGLRLlidqgFAAGNTALLNRAFLLLLAVALVLALASALRFY----LVSWLGERVVADLRKAVFAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 797 ILNQEPGWFDSdqNSPGSLVSKLSVNCTSFRSILGD------RYSVLFMGlssaavGLSVSFYLEWRLALLATIVTPFTL 870
Cdd:cd18575 79 LLRLSPSFFET--TRTGEVLSRLTTDTTLIQTVVGSslsialRNLLLLIG------GLVMLFITSPKLTLLVLLVIPLVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 871 GAsyfslIINIG------SKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGI 944
Cdd:cd18575 151 LP-----IILFGrrvrrlSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTAL 225
|
250 260
....*....|....*....|
gi 1770234124 945 SQGAMYSAYTLVLFFGAYLV 964
Cdd:cd18575 226 VIFLVFGAIVFVLWLGAHDV 245
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
400-613 |
1.11e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.54 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 400 LKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVK-WLRSQMGM 478
Cdd:PRK10982 1 MSNISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 479 VGQEPVLFAD-TILENILMGKEnATKKEAIDACIAVNAHNFICDlPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKI 557
Cdd:PRK10982 78 VHQELNLVLQrSVMDNMWLGRY-PTKGMFVDQDKMYRDTKAIFD-ELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 558 LLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRLATV-KNAETIIVLEQGSVI 613
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLkERGCGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
72-335 |
1.45e-13 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 73.21 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 72 LFLIIIGCLGALInggsqPWysyLFGNFVNKIaldNDKDQMIKDVRELCVLMSALSGIVVIGAYLqiacWRL----VGER 147
Cdd:cd18541 6 LFLILVDLLQLLI-----PR---IIGRAIDAL---TAGTLTASQLLRYALLILLLALLIGIFRFL----WRYlifgASRR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 148 LGHRIRSKYLRAVLRQDVSFFDTDiSTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAV 227
Cdd:cd18541 71 IEYDLRNDLFAHLLTLSPSFYQKN-RTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 228 TPLtmfcgVAYKAVYVGlaaKEVNS-YKKA----GSIAEQA---IGSIRTVFSFVAEDSLAARYDAVLDESVpiGKKLGF 299
Cdd:cd18541 150 LPL-----LALLVYRLG---KKIHKrFRKVqeafSDLSDRVqesFSGIRVIKAFVQEEAEIERFDKLNEEYV--EKNLRL 219
|
250 260 270
....*....|....*....|....*....|....*...
gi 1770234124 300 AKGIGL--GVIYLVTYSTWALAFWYGSILVSRNELSGG 335
Cdd:cd18541 220 ARVDALffPLIGLLIGLSFLIVLWYGGRLVIRGTITLG 257
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1048-1259 |
1.53e-13 |
|
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: 75.11 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1048 VIVLREFCLKVKGGTMVAVVGGSGSGKS----TVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLR----LQTALVGQEP- 1118
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1119 -AL-----FGGTIGENIR--FG-NPNASWSEVEEAAKE-----------AYIHnficglprgyetevgesgiQLSGGQKQ 1178
Cdd:COG4172 103 tSLnplhtIGKQIAEVLRlhRGlSGAAARARALELLERvgipdperrldAYPH-------------------QLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1179 RIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIV--------VVHRLstikkANAIAVVQNGKVSEY 1250
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALllithdlgVVRRF-----ADRVAVMRQGEIVEQ 238
|
....*....
gi 1770234124 1251 GTHDTLLTN 1259
Cdd:COG4172 239 GPTAELFAA 247
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1050-1256 |
1.58e-13 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 71.79 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWL-RLQTALV--GQE--PALfggT 1124
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVpqGREifPRL---T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1125 IGENIRFGNPNAswseveeAAKEAYIHNFICGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDL 1204
Cdd:TIGR03410 92 VEENLLTGLAAL-------PRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1205 ESEKHVQDAIRKIIKRTT-TIVVV-HRLS-TIKKANAIAVVQNGKVSEYGTHDTL 1256
Cdd:TIGR03410 165 SIIKDIGRVIRRLRAEGGmAILLVeQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1050-1259 |
1.81e-13 |
|
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: 71.42 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDL-KWLRLQTALVGQEPALFGG-TIGE 1127
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1128 NIR-----FGNPNASWSEveeaAKEAYIHNFicglprGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSAL 1202
Cdd:cd03218 95 NILavleiRGLSKKEREE----KLEELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1203 DlesEKHVQDaIRKIIKRTTT--IVVV---HR----LSTIKKAnaiAVVQNGKVSEYGTHDTLLTN 1259
Cdd:cd03218 165 D---PIAVQD-IQKIIKILKDrgIGVLitdHNvretLSITDRA---YIIYEGKVLAEGTPEEIAAN 223
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
380-625 |
2.11e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.01 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 380 AIDPYSTTGRKPETVHG--RLELKNVSFAYPSR-MSVpilNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGL 456
Cdd:PRK10522 303 ALAPYKAEFPRPQAFPDwqTLELRNVTFAYQDNgFSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 457 ILLDGQDIRTLQVKWLRSQMGMVgqepvlFADTILENILMGKENATKKEAIdaciavnAHNFICDLPQGYDTQVgEKG-- 534
Cdd:PRK10522 380 ILLDGKPVTAEQPEDYRKLFSAV------FTDFHLFDQLLGPEGKPANPAL-------VEKWLERLKMAHKLEL-EDGri 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 535 --TQLSGGQKQRIALARAMIKDPKILLLDEPTSALDP--------KSESLVQQaidkisKGRTTIVIAHRLATVKNAETI 604
Cdd:PRK10522 446 snLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPhfrrefyqVLLPLLQE------MGKTIFAISHDDHYFIHADRL 519
|
250 260
....*....|....*....|..
gi 1770234124 605 IVLEQGSVIEI-GDHNKLMAQE 625
Cdd:PRK10522 520 LEMRNGQLSELtGEERDAASRD 541
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1051-1259 |
2.40e-13 |
|
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: 73.21 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1051 LREFCLKVK----GGTMVAVVGGSGSGKSTVIWLM---QRfydPIGGKVMMGGRDLRDlDLKWLRLQT-----ALVGQEP 1118
Cdd:COG4148 11 RGGFTLDVDftlpGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEVLQD-SARGIFLPPhrrriGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1119 ALFGG-TIGENIRFG----NPNASWSEVEEAAKeayihnfICGL-------PRgyetevgesgiQLSGGQKQRIAIARAI 1186
Cdd:COG4148 87 RLFPHlSVRGNLLYGrkraPRAERRISFDEVVE-------LLGIghlldrrPA-----------TLSGGERQRVAIGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1187 VKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTT-IVVV-H------RLstikkANAIAVVQNGKVSEYGTHDTLLT 1258
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVsHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLS 223
|
.
gi 1770234124 1259 N 1259
Cdd:COG4148 224 R 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1047-1251 |
2.54e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.53 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwlRLQTALVGQEPALFGG-TI 1125
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMVFQSYALYPHlSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1126 GENIRFGN--PNASWSE----VEEAAKEAYIHNFICGLPRGyetevgesgiqLSGGQKQRIAIARAIVKKSKVLLLDEAT 1199
Cdd:PRK11000 93 AENMSFGLklAGAKKEEinqrVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1200 SALDLESEKHVQDAIRKIIKR--TTTIVVVH-RLSTIKKANAIAVVQNGKVSEYG 1251
Cdd:PRK11000 162 SNLDAALRVQMRIEISRLHKRlgRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1061-1203 |
2.84e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 70.67 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1061 GTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRD---LRDLDLKWLRLQTALVGQE---------------PALFG 1122
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDhhllmdrtvydnvaiPLIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1123 GTIGENIRfgnpnaswSEVEEAAKEAYIHNFICGLPrgyetevgesgIQLSGGQKQRIAIARAIVKKSKVLLLDEATSAL 1202
Cdd:PRK10908 108 GASGDDIR--------RRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
.
gi 1770234124 1203 D 1203
Cdd:PRK10908 169 D 169
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
398-594 |
3.04e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 69.10 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmSVPILNSLNLVI-PSQRIsALVGASGAGKSTIFALLERFYdpnkglilldgqdirtlqvKWLRSQM 476
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIkPGDRL-LITGPSGTGKSSLFRALAGLW-------------------PWGSGRI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQEPVLFadtilenilmgkenatkkeaidaciavnahnficdLPQ-GYDTQvgekGT-----------QLSGGQKQR 544
Cdd:cd03223 59 GMPEGEDLLF-----------------------------------LPQrPYLPL----GTlreqliypwddVLSGGEQQR 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1770234124 545 IALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKisKGRTTIVIAHR 594
Cdd:cd03223 100 LAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
414-615 |
3.73e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.37 E-value: 3.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 414 PILNSLNLVIPSQRISALVGASGAGKSTIF-ALLERFYD-PNKGLILLDGQDIrtlqvkwlrsqmgmvGQEPvlfadTIL 491
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLrLLAGALKGtPVAGCVDVPDNQF---------------GREA-----SLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 492 ENILMGKENATKKEAIDACIAVNAHNFIcdlpqgydtqvgEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKS 571
Cdd:COG2401 104 DAIGRKGDFKDAVELLNAVGLSDAVLWL------------RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1770234124 572 ESLVQQAIDKISK--GRTTIVIAHRlATVKNA---ETIIVLEQGSVIEI 615
Cdd:COG2401 172 AKRVARNLQKLARraGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPEE 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
419-617 |
4.19e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.60 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 419 LNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGqdiRTL----QVKWL---RSQMGMVGQEPVLFAD-TI 490
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG---RVLfdaeKGICLppeKRRIGYVFQDARLFPHyKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 491 LENILMGkenatkkeaidaCIAVNAHNFicdlpqgyDTQVGEKGTQ---------LSGGQKQRIALARAMIKDPKILLLD 561
Cdd:PRK11144 94 RGNLRYG------------MAKSMVAQF--------DKIVALLGIEplldrypgsLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 562 EPTSALD-P-KSESLvqQAIDKISKG-RTTIV-IAHRLATV-KNAETIIVLEQGSVIEIGD 617
Cdd:PRK11144 154 EPLASLDlPrKRELL--PYLERLAREiNIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGP 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1033-1261 |
4.60e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSrpdVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDL-KWLRLQT 1111
Cdd:PRK11614 6 LSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVGQEPALFGG-TIGENIRFGNPNASWSEVEEAAKEAYihnficGL-PRGYETEVGESGiQLSGGQKQRIAIARAIVKK 1189
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWVY------ELfPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 1190 SKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLS--TIKKANAIAVVQNGKVSEYGTHDTLLTNHS 1261
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
713-964 |
5.22e-13 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 71.31 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 713 LCVGVIFGmLAGAILSLF-PLVLGQALtvyfnpDKSKLQKDVGYLCLALVGLGFGCILTMMGQQGFCGWAGTKLTKRVRD 791
Cdd:cd18551 1 LILALLLS-LLGTAASLAqPLLVKNLI------DALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 792 LLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPFTLG 871
Cdd:cd18551 74 RLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 872 asyfsLIINIGSKLDNDSFD------KASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGIS 945
Cdd:cd18551 152 -----IILPLGRRIRKASKRaqdalgELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLM 226
|
250
....*....|....*....
gi 1770234124 946 QGAMYSAYTLVLFFGAYLV 964
Cdd:cd18551 227 GLAVQLALLVVLGVGGARV 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1050-1258 |
7.17e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.11 E-value: 7.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPAL--------- 1120
Cdd:COG4604 16 VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHInsrltvrel 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1121 --FGgtigeniRF----GNPNAS-WSEVEEAA--------KEAYIHnficglprgyetevgesgiQLSGGQKQRIAIARA 1185
Cdd:COG4604 96 vaFG-------RFpyskGRLTAEdREIIDEAIayldledlADRYLD-------------------ELSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1186 IVKKSKVLLLDEATSALDLeseKH-VQdaIRKIIKRT------TTIVVVHrlsTIKKANA----IAVVQNGKVSEYGTHD 1254
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDM---KHsVQ--MMKLLRRLadelgkTVVIVLH---DINFASCyadhIVAMKDGRVVAQGTPE 221
|
....
gi 1770234124 1255 TLLT 1258
Cdd:COG4604 222 EIIT 225
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
717-964 |
7.55e-13 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 71.04 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 717 VIFGMLAGAILSL-FPLVLGQALTV---YFNPDKSK----LQKDVGYLCLALV---GLGFGCI--LTMMGQQgfcgwagt 783
Cdd:cd18574 1 AVLSALAAALVNIqIPLLLGDLVNVisrSLKETNGDfiedLKKPALKLLGLYLlqsLLTFAYIslLSVVGER-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 784 kLTKRVRDLLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGdrySVLFMGLSSAA--VGLSVSFYL-EWRLAL 860
Cdd:cd18574 73 -VAARLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFK---QCVSQGLRSVTqtVGCVVSLYLiSPKLTL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 861 LATIVTP--FTLGASYFSLIINIgSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKrsqiT 938
Cdd:cd18574 147 LLLVIVPvvVLVGTLYGSFLRKL-SRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEK----L 221
|
250 260 270
....*....|....*....|....*....|
gi 1770234124 939 GIALGISQG----AMYSAYTLVLFFGAYLV 964
Cdd:cd18574 222 GLGIGIFQGlsnlALNGIVLGVLYYGGSLV 251
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
398-595 |
8.19e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 8.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKwlRSQ-- 475
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK--SSQea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 -MGMVGQEPVLFAD-TILENILMGKENATKKEAID-ACIAVNAHNFICDL--PQGYDTQVGEkgtqLSGGQKQRIALARA 550
Cdd:PRK10762 80 gIGIIHQELNLIPQlTIAENIFLGREFVNRFGRIDwKKMYAEADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1770234124 551 MIKDPKILLLDEPTSAL-DPKSESLVQQAIDKISKGRTTIVIAHRL 595
Cdd:PRK10762 156 LSFESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
715-964 |
1.17e-12 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 70.54 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 715 VGVIFGMLAGAILSLF-PLVLGQAL-TVYFNPDKSKLqkdvGYLCLALVGLGFGCILTMMGQQGFCGWAGTKLTKRVRDL 792
Cdd:cd18542 2 LLAILALLLATALNLLiPLLIRRIIdSVIGGGLRELL----WLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 793 LFRSILNQEPGWFdsDQNSPGSLVSKlsvnCTS----FRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPF 868
Cdd:cd18542 78 LYDHLQRLSFSFH--DKARTGDLMSR----CTSdvdtIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 869 TLGASY-FSLIIN-IGSKLDnDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQ 946
Cdd:cd18542 152 IALFSYvFFKKVRpAFEEIR-EQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMD 230
|
250
....*....|....*...
gi 1770234124 947 GAMYSAYTLVLFFGAYLV 964
Cdd:cd18542 231 FLSGLQIVLVLWVGGYLV 248
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1050-1247 |
1.30e-12 |
|
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: 68.40 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALvgQEPALFGGTIG-EN 1128
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI--EAPGFYPNLTArEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1129 IR-----FGNPNASWSEVEEaakeayihnficglprgyetEVGESGI------QLSGGQKQRIAIARAIVKKSKVLLLDE 1197
Cdd:cd03268 93 LRllarlLGIRKKRIDEVLD--------------------VVGLKDSakkkvkGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1198 ATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKV 1247
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKL 204
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
400-582 |
1.35e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 69.37 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 400 LKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQdirtlqvkwLRsqMGMV 479
Cdd:PRK09544 7 LENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 480 GQEpvLFADTIL----ENILMGKENATKKEAIDACIAVNAHNFIcDLPQgydtqvgekgTQLSGGQKQRIALARAMIKDP 555
Cdd:PRK09544 73 PQK--LYLDTTLpltvNRFLRLRPGTKKEDILPALKRVQAGHLI-DAPM----------QKLSGGETQRVLLARALLNRP 139
|
170 180
....*....|....*....|....*..
gi 1770234124 556 KILLLDEPTSALDPKSESLVQQAIDKI 582
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQL 166
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1061-1257 |
1.35e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1061 GTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDL---------KWLRLQTALVGQEPA-------LFGGT 1124
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerrRLLRTEWGFVHQHPRdglrmqvSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1125 IGE-----------NIRfgNPNASW-SEVEEAAKEayihnfICGLPRGYetevgesgiqlSGGQKQRIAIARAIVKKSKV 1192
Cdd:PRK11701 112 IGErlmavgarhygDIR--ATAGDWlERVEIDAAR------IDDLPTTF-----------SGGMQQRLQIARNLVTHPRL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1193 LLLDEATSALDLESEKHVQDAIRKIIKRT--TTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLL 1257
Cdd:PRK11701 173 VFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVL 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1026-1258 |
1.36e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.05 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1026 EQSKPFdLEFKMVNFAYPSRPDV--------IVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYdPIGGKVMMGGR 1097
Cdd:PRK15134 270 EPASPL-LDVEQLQVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1098 DLRDLDLKWL---RLQTALVGQEP--AL-----FGGTIGENIRFGNPNASWSEVEEAAKEAYihnficglprgyeTEVG- 1166
Cdd:PRK15134 348 PLHNLNRRQLlpvRHRIQVVFQDPnsSLnprlnVLQIIEEGLRVHQPTLSAAQREQQVIAVM-------------EEVGl 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1167 --ES----GIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDleseKHVQDAIRKIIK------RTTTIVVVHRLSTIK 1234
Cdd:PRK15134 415 dpETrhryPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAQILALLKslqqkhQLAYLFISHDLHVVR 490
|
250 260
....*....|....*....|....*
gi 1770234124 1235 K-ANAIAVVQNGKVSEYGTHDTLLT 1258
Cdd:PRK15134 491 AlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
398-617 |
1.62e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 68.95 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYP-------------------SRMSVPILNSLNLVIPS-QRIsALVGASGAGKSTIFALLERFYDPNKGLI 457
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERgESV-GIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 458 LLDGqdirtlQVKWLRS-QMGMVGQepvLfadTILENI-----LMGKENATKKEAIDACIAvnahnFiCDLPQGYDTQVG 531
Cdd:COG1134 84 EVNG------RVSALLElGAGFHPE---L---TGRENIylngrLLGLSRKEIDEKFDEIVE-----F-AELGDFIDQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 532 ekgtQLSGGQKQRIALARAMIKDPKILLLDEPTSALDP----KSESLVQqaiDKISKGRTTIVIAHRLATVKN-AETIIV 606
Cdd:COG1134 146 ----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRAIW 218
|
250
....*....|.
gi 1770234124 607 LEQGSVIEIGD 617
Cdd:COG1134 219 LEKGRLVMDGD 229
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
95-339 |
1.63e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 69.85 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 95 LFGNFVNKIALDNDKDQMIKDVRE--LCVLMSALSGIVVIGAYLQIACWRL---VGERLGHRIRSKYLRAVLRQDVSFFD 169
Cdd:cd18563 16 LVPPYLTKILIDDVLIQLGPGGNTslLLLLVLGLAGAYVLSALLGILRGRLlarLGERITADLRRDLYEHLQRLSLSFFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 170 tDISTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPL----TMFCGVAYKAVY--V 243
Cdd:cd18563 96 -KRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLvvwgSYFFWKKIRRLFhrQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 244 GLAAKEVNSYkkagsIAEqAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLG-----FAKGIGLgVIYLVTYSTWal 318
Cdd:cd18563 175 WRRWSRLNSV-----LND-TLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEklwatFFPLLTF-LTSLGTLIVW-- 245
|
250 260
....*....|....*....|.
gi 1770234124 319 afWYGSILVSRNELSGGAAIA 339
Cdd:cd18563 246 --YFGGRQVLSGTMTLGTLVA 264
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1033-1246 |
1.78e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 66.32 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVmmggrdlrdldlkwlrlqta 1112
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 lvgqepalfggTIGENIRFGnpnaswseveeaakeaYIHnficglprgyetevgesgiQLSGGQKQRIAIARAIVKKSKV 1192
Cdd:cd03221 58 -----------TWGSTVKIG----------------YFE-------------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1193 LLLDEATSALDLESEKHVQDAIRKiiKRTTTIVVVH-R--LSTIkkANAIAVVQNGK 1246
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1044-1206 |
2.00e-12 |
|
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: 67.77 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1044 SRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRlQTALVGQEPALFGG 1123
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE-NILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 -TIGENIRFgnpnasWSEVEEAAKEAyIHNFIcglprgyeTEVGESGI------QLSGGQKQRIAIARAIVKKSKVLLLD 1196
Cdd:TIGR01189 88 lSALENLHF------WAAIHGGAQRT-IEDAL--------AAVGLTGFedlpaaQLSAGQQRRLALARLWLSRRPLWILD 152
|
170
....*....|
gi 1770234124 1197 EATSALDLES 1206
Cdd:TIGR01189 153 EPTTALDKAG 162
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1047-1258 |
2.47e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.89 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGG-TI 1125
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1126 GENIRFG-NPNAS-W--------SEVEEAAKEAYIHNFIcglprgyETEVGEsgiqLSGGQKQRIAIARAIVKKSKVLLL 1195
Cdd:PRK11231 94 RELVAYGrSPWLSlWgrlsaednARVNQAMEQTRINHLA-------DRRLTD----LSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1196 DEATSALDLESEKHVQDAIRKI-IKRTTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLT 1258
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
72-339 |
2.50e-12 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 69.42 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 72 LFLIIIGCLGALINggsqPwysYLFGNFVNKIALDNDKDQMIkdvrELCVLMSALSGIVVIGAYLQIACWRLVGERLGHR 151
Cdd:cd18545 6 LLLMLLSTAASLAG----P---YLIKIAIDEYIPNGDLSGLL----IIALLFLALNLVNWVASRLRIYLMAKVGQRILYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 152 IRSKYLRAVLRQDVSFFDTDiSTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLt 231
Cdd:cd18545 75 LRQDLFSHLQKLSFSFFDSR-PVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 232 MFCGV---------AYKAVYVGLAAkeVNSYkkagsIAEqAIGSIRTVFSFVAEDSLAARYDAVLDESV----------- 291
Cdd:cd18545 153 LVLVVfllrrrarkAWQRVRKKISN--LNAY-----LHE-SISGIRVIQSFAREDENEEIFDELNRENRkanmravrlna 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 292 ---PIgkkLGFAKGIGLGVIYlvtystwalafWYGSILVSRNELSGGAAIA 339
Cdd:cd18545 225 lfwPL---VELISALGTALVY-----------WYGGKLVLGGAITVGVLVA 261
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
415-616 |
3.74e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 415 ILNSLNLVIPSQRISALVGASGAGKSTIF-ALLERFYDPN-------KGLILLDGQDIRTL---QVKWLRSQMGMVGQEP 483
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGaprgarvTGDVTLNGEPLAAIdapRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 484 vlFADTILENILMGK-ENATKKEAI---DACIAVNAHNFicdlpQGYDTQVGEKGTQLSGGQKQRIALARAM-------- 551
Cdd:PRK13547 96 --FAFSAREIVLLGRyPHARRAGALthrDGEIAWQALAL-----AGATALVGRDVTTLSGGELARVQFARVLaqlwpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 552 -IKDPKILLLDEPTSALDPKSESLVQQAIDKISK----GRTTIVIAHRLATvKNAETIIVLEQGSVIEIG 616
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwnlGVLAIVHDPNLAA-RHADRIAMLADGAIVAHG 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1033-1251 |
3.78e-12 |
|
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: 67.22 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRpdvIVLREFCLKVKGGtMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDlDLKWLRlqtA 1112
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLR---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGG----TIGENIRFG------NPNASWSEVEEAAKEAYIHNFicglprgYETEVGesgiQLSGGQKQRIAI 1182
Cdd:cd03264 73 RIGYLPQEFGVypnfTVREFLDYIawlkgiPSKEVKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1183 ARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYG 1251
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
397-612 |
4.82e-12 |
|
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: 66.30 E-value: 4.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAYPsrmsvpiLNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQV-KWLRSQ 475
Cdd:cd03215 4 VLEVRGLSVKGA-------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MGMVGQEPV---LFAD-TILENILMGkenatkkeaidaciavnahnficdlpqgydtqvgekgTQLSGGQKQRIALARAM 551
Cdd:cd03215 77 IAYVPEDRKregLVLDlSVAENIALS-------------------------------------SLLSGGNQQKVVLARWL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 552 IKDPKILLLDEPTSALDPKSESLVQQAIDKIS-KGRTTIVIAHRLATV-KNAETIIVLEQGSV 612
Cdd:cd03215 120 ARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1050-1258 |
5.41e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKS-TVIWLMQRFYDP----IGGKVMMGGRDLRDLDLKWLRL----QTALVGQEPAL 1120
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1121 fggtigenirfgnpnaSWSEVEEAAKEAYIhnfICGLPRGYETEVGES---------GI------------QLSGGQKQR 1179
Cdd:PRK15134 104 ----------------SLNPLHTLEKQLYE---VLSLHRGMRREAARGeilncldrvGIrqaakrltdyphQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1180 IAIARAIVKKSKVLLLDEATSALDLEsekhVQDAIRKIIKR------TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGT 1252
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVS----VQAQILQLLRElqqelnMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNR 240
|
....*.
gi 1770234124 1253 HDTLLT 1258
Cdd:PRK15134 241 AATLFS 246
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
713-964 |
5.47e-12 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 68.21 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 713 LCVGVIFgMLAGAILSLF-PLVLGQALTVYFNPDKSklQKDVGYLCLALVGLGFGCILTMMGQQGFCGWAGTKLTKRVRD 791
Cdd:cd18541 1 YLLGILF-LILVDLLQLLiPRIIGRAIDALTAGTLT--ASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 792 LLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPF-TL 870
Cdd:cd18541 78 DLFAHLLTLSPSFYQ--KNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLlAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 871 GASYFSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMY 950
Cdd:cd18541 156 LVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIG 235
|
250
....*....|....
gi 1770234124 951 SAYTLVLFFGAYLV 964
Cdd:cd18541 236 LSFLIVLWYGGRLV 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
398-617 |
5.66e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.65 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAY-PSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDI--RTLQVKWLRS 474
Cdd:PRK10261 13 LAVENLNIAFmQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 Q------------MGMVGQEPV-----LFA--DTILENILM----GKENATK--KEAIDACIAVNAHNFICDLPQgydtq 529
Cdd:PRK10261 93 QsaaqmrhvrgadMAMIFQEPMtslnpVFTvgEQIAESIRLhqgaSREEAMVeaKRMLDQVRIPEAQTILSRYPH----- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 530 vgekgtQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRT--TIVIAHRLATVKN-AETIIV 606
Cdd:PRK10261 168 ------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLV 241
|
250
....*....|.
gi 1770234124 607 LEQGSVIEIGD 617
Cdd:PRK10261 242 MYQGEAVETGS 252
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1042-1221 |
5.76e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.80 E-value: 5.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1042 YPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLkwlrlQTALVGQEPALF 1121
Cdd:PRK11248 11 YGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA-----ERGVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1122 G-GTIGENIRFGNPNASwseVEEAAKEAYIHNFIcglprgyeTEVGESGI------QLSGGQKQRIAIARAIVKKSKVLL 1194
Cdd:PRK11248 83 PwRNVQDNVAFGLQLAG---VEKMQRLEIAHQML--------KKVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLL 151
|
170 180
....*....|....*....|....*..
gi 1770234124 1195 LDEATSALDLESEKHVQDAIRKIIKRT 1221
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQET 178
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
75-339 |
5.90e-12 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 68.18 E-value: 5.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 75 IIIGCLGALINGGSQPWYSYLFGNFVNKIALDNDKDqmIKDVRELCVLMSALSGIVVIGAYLQIACWRLVGERLGHRIRS 154
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGD--LQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 155 KYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFC 234
Cdd:cd18544 79 DLFSHIQRLPLSFFDR-TPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 235 --------GVAYKAVYVGLAakEVNSYkkagsIAEQaIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLG 306
Cdd:cd18544 158 tylfrkksRKAYREVREKLS--RLNAF-----LQES-ISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRP 229
|
250 260 270
....*....|....*....|....*....|...
gi 1770234124 307 VIYLVTYSTWALAFWYGSILVSRNELSGGAAIA 339
Cdd:cd18544 230 LVELLSSLALALVLWYGGGQVLSGAVTLGVLYA 262
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1046-1246 |
6.11e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 6.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1046 PDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYdPIG---GKVMMGGRDL-----RDLDlkwlRLQTALVGQE 1117
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELqasniRDTE----RAGIAIIHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1118 PALFGG-TIGENIRFGNP---------NASWSEVEEAAKEAyihnficGLPRGYETEVGEsgiqLSGGQKQRIAIARAIV 1187
Cdd:PRK13549 91 LALVKElSVLENIFLGNEitpggimdyDAMYLRAQKLLAQL-------KLDINPATPVGN----LGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1188 KKSKVLLLDEATSALDlESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGK 1246
Cdd:PRK13549 160 KQARLLILDEPTASLT-ESETAVLLDIIRDLKAhgIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1043-1247 |
7.80e-12 |
|
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: 66.62 E-value: 7.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1043 PSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDlrdldlkwlrlqtalVGQEPA--- 1119
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD---------------VVKEPAear 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1120 -----LFGG-------TIGENIR-FG-----NPNASWSEVEEAAKEAYIHNFIcglprgyETEVGEsgiqLSGGQKQRIA 1181
Cdd:cd03266 78 rrlgfVSDStglydrlTARENLEyFAglyglKGDELTARLEELADRLGMEELL-------DRRVGG----FSTGMRQKVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1182 IARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVV-VHRLSTIKK-ANAIAVVQNGKV 1247
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFsTHIMQEVERlCDRVVVLHRGRV 214
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
114-339 |
9.94e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 67.51 E-value: 9.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 114 KDVRELCVLMSALSGIVVIGA---YLQIACWRLVGERLGHRIRSKYLRAVLRQDVSFFdTDISTSDIMHGISSDVAQIQE 190
Cdd:cd18550 33 GDLGLLVLLALGMVAVAVASAllgVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFF-TRTRTGEIQSRLNNDVGGAQS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 191 VMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFcgvayKAVYVGLAAKEVnSYKKAGSIAEQA------- 263
Cdd:cd18550 112 VVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVL-----PTRRVGRRRRKL-TREQQEKLAELNsimqetl 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 264 -IGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYSTWALAFWYGSILVSRNELSGGAAIA 339
Cdd:cd18550 186 sVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVA 262
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
398-623 |
1.08e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.12 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVS--FAYPS----RMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKW 471
Cdd:PRK15112 5 LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 472 lRSQ-MGMVGQEP------------VLFADTILENILMGKEnatKKEAIDACIavnahnficdlpqgydTQVGEKGTQ-- 536
Cdd:PRK15112 85 -RSQrIRMIFQDPstslnprqrisqILDFPLRLNTDLEPEQ---REKQIIETL----------------RQVGLLPDHas 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 537 -----LSGGQKQRIALARAMIKDPKILLLDEPTSALDpksESLVQQAIDKI-----SKGRTTIVIAHRLATVKN-AETII 605
Cdd:PRK15112 145 yyphmLAPGQKQRLGLARALILRPKVIIADEALASLD---MSMRSQLINLMlelqeKQGISYIYVTQHLGMMKHiSDQVL 221
|
250
....*....|....*...
gi 1770234124 606 VLEQGSVIEIGDHNKLMA 623
Cdd:PRK15112 222 VMHQGEVVERGSTADVLA 239
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
430-616 |
1.09e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 430 ALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL---QVKWLRSQMGMVGQEPVLFAD-------TILE-----NI 494
Cdd:PRK10261 354 SLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDPYASLDprqtvgdSIMEplrvhGL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 495 LMGKENATKKEAIDACIAVnahnficdLPQgydtQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPkseSL 574
Cdd:PRK10261 434 LPGKAAAARVAWLLERVGL--------LPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV---SI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1770234124 575 VQQAIDKI-----SKGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIG 616
Cdd:PRK10261 499 RGQIINLLldlqrDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
398-595 |
1.49e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSrmsVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVK-WLRSQM 476
Cdd:PRK11288 5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 GMVGQEPVLFAD-TILENILMG---------KENATKKEAIDACIAVnahnficdlpqGYDTQVGEKGTQLSGGQKQRIA 546
Cdd:PRK11288 82 AIIYQELHLVPEmTVAENLYLGqlphkggivNRRLLNYEAREQLEHL-----------GVDIDPDTPLKYLSIGQRQMVE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 547 LARAMIKDPKILLLDEPTSALD-PKSESLVqQAIDKI-SKGRTTIVIAHRL 595
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSLSaREIEQLF-RVIRELrAEGRVILYVSHRM 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1022-1250 |
1.49e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.94 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1022 GKKIeqskpfdLEFKMVNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTViwlmqrfydpiggkvmmggrdlrd 1101
Cdd:COG0488 312 GKKV-------LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTL------------------------ 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1102 ldlkwLRLqtaLVGQEPALfGGTI--GENIRFG---------NPNAS-WSEVEEAAKEAYIHNficglPRGY-------- 1161
Cdd:COG0488 358 -----LKL---LAGELEPD-SGTVklGETVKIGyfdqhqeelDPDKTvLDELRDGAPGGTEQE-----VRGYlgrflfsg 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1162 ---ETEVGEsgiqLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIikrTTTIVVV-H-R--LSTIk 1234
Cdd:COG0488 424 ddaFKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF---PGTVLLVsHdRyfLDRV- 495
|
250
....*....|....*.
gi 1770234124 1235 kANAIAVVQNGKVSEY 1250
Cdd:COG0488 496 -ATRILEFEDGGVREY 510
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1054-1204 |
1.68e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.30 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1054 FCLKvKGGTMvAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLD---LKWLRLQTALVGQEPalFGG-----TI 1125
Cdd:PRK11308 36 FTLE-RGKTL-AVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP--YGSlnprkKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1126 GENIrfGNP---NASWSEVEEAAKEA---------------YIHNFicglprgyetevgesgiqlSGGQKQRIAIARAIV 1187
Cdd:PRK11308 112 GQIL--EEPlliNTSLSAAERREKALammakvglrpehydrYPHMF-------------------SGGQRQRIAIARALM 170
|
170
....*....|....*..
gi 1770234124 1188 KKSKVLLLDEATSALDL 1204
Cdd:PRK11308 171 LDPDVVVADEPVSALDV 187
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
416-611 |
1.76e-11 |
|
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: 64.27 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 416 LNSLNLVIPSQRISALVGASGAGKSTIfaLLERFYDPNKGLIlldgqdirtlqvkwlrsqmgmvgqepvlfadtilenil 495
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARL-------------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 496 mgkENATKKEAIDACIAVNAHNFICDLPQGYDTqVGEKGTQLSGGQKQRIALARAMIKDPK--ILLLDEPTSALDP-KSE 572
Cdd:cd03238 51 ---ISFLPKFSRNKLIFIDQLQFLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQqDIN 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 1770234124 573 SLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVLEQGS 611
Cdd:cd03238 127 QLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1046-1254 |
1.79e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 68.66 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1046 PDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYdPIG---GKVMMGG-----RDLRDLDlkwlRLQTALVGQE 1117
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGevcrfKDIRDSE----ALGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1118 PALFGG-TIGENIRFGNPNAS-----WSEVEEAAKE--AYIhnficGLPRGYETEVGESGIqlsgGQKQRIAIARAIVKK 1189
Cdd:NF040905 87 LALIPYlSIAENIFLGNERAKrgvidWNETNRRAREllAKV-----GLDESPDTLVTDIGV----GKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1190 SKVLLLDEATSALDLESEKHVQDAIRKIIKR-TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEygTHD 1254
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRvADSITVLRDGRTIE--TLD 222
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
72-339 |
2.14e-11 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 66.65 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 72 LFLIIIGCLGALInggsQPwysYLFGNFVNKIALDNDKDQMIKdvreLCVLMSALSGIVVIGAYLQIACWRLVGERLGHR 151
Cdd:cd18548 5 PLFKLLEVLLELL----LP---TLMADIIDEGIANGDLSYILR----TGLLMLLLALLGLIAGILAGYFAAKASQGFGRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 152 IRSKYLRAVLRQDVSFFDtDISTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLT 231
Cdd:cd18548 74 LRKDLFEKIQSFSFAEID-KFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 232 MFC--GVAYKAV--YVGLAAK--EVNSykkagSIAEQAIGsIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGL 305
Cdd:cd18548 153 ALVvfLIMKKAIplFKKVQKKldRLNR-----VVRENLTG-IRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLN 226
|
250 260 270
....*....|....*....|....*....|....
gi 1770234124 306 GVIYLVTYSTWALAFWYGSILVSRNELSGGAAIA 339
Cdd:cd18548 227 PLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVA 260
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
113-290 |
2.26e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 66.82 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 113 IKDVRELCVLMSALSGIVVIG----AYLQIACWRLVGERLGHRIRSKYLRAVLRQDVSFFDtDISTSDIMHGISSDVAQI 188
Cdd:cd18565 46 PADPRGQLWLLGGLTVAAFLLeslfQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFE-DRQTGDLMSVLNNDVNQL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 189 QEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFCGVAYKAVyvgLAAKEVNSYKKAGSIA---EQAIG 265
Cdd:cd18565 125 ERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRR---IEPRYRAVREAVGDLNarlENNLS 201
|
170 180
....*....|....*....|....*
gi 1770234124 266 SIRTVFSFVAEDSLAARydaVLDES 290
Cdd:cd18565 202 GIAVIKAFTAEDFERER---VADAS 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1050-1228 |
2.27e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 65.15 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMM----GGRDL-----RD-LDLK---------WLRL- 1109
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLaqaspREiLALRrrtigyvsqFLRVi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1110 --QTAL-VGQEPALFGGTigenirfgnpnaswsEVEEAAKEA--YIHNFicGLPrgyetevgESGIQL-----SGGQKQR 1179
Cdd:COG4778 106 prVSALdVVAEPLLERGV---------------DREEARARAreLLARL--NLP--------ERLWDLppatfSGGEQQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1180 IAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIV-VVH 1228
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1053-1252 |
2.62e-11 |
|
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: 65.51 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1053 EFCLKVKGGT-----MVAVVGGSGSGKSTVIWLMQRFYDPIGGKVmmgGRDLRDLDLKWLRLQTALVGQEPALFGGTIGe 1127
Cdd:cd03237 12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKPQYIKADYEGTVRDLLSSITK- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1128 niRFGNPNASWSEVEEAAKeayihnficgLPRGYETEVGEsgiqLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESE 1207
Cdd:cd03237 88 --DFYTHPYFKTEIAKPLQ----------IEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1770234124 1208 KHVQDAIRKII--KRTTTIVVVHRLSTIKKANAIAVVQNGKVSEYGT 1252
Cdd:cd03237 152 LMASKVIRRFAenNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGV 198
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1047-1256 |
2.74e-11 |
|
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: 67.91 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRF--YDPIGGKVMMggRDLRDLDLKWLRLQTaLVGQEPALFGGT 1124
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIY--HVALCEKCGYVERPS-KVGEPCPVCGGT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1125 IG-ENIRFGNPnaswSEVEEAA-----------------KEAYIHNFICGLPR-GYEtevGESGIQ-------------- 1171
Cdd:TIGR03269 89 LEpEEVDFWNL----SDKLRRRirkriaimlqrtfalygDDTVLDNVLEALEEiGYE---GKEAVGravdliemvqlshr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1172 -------LSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRT--TTIVVVHRLSTIKKANAIAV- 1241
Cdd:TIGR03269 162 ithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDLSDKAIw 241
|
250
....*....|....*
gi 1770234124 1242 VQNGKVSEYGTHDTL 1256
Cdd:TIGR03269 242 LENGEIKEEGTPDEV 256
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1056-1228 |
2.80e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.18 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwLRlQTALVGQEPALFGG-TIGENIRFGNP 1134
Cdd:PRK11650 25 LDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DR-DIAMVFQNYALYPHmSVRENMAYGLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1135 NASWSE------VEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSALD----- 1203
Cdd:PRK11650 103 IRGMPKaeieerVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrv 171
|
170 180 190
....*....|....*....|....*....|
gi 1770234124 1204 ---LEsekhvqdaIRKIIKR--TTTIVVVH 1228
Cdd:PRK11650 172 qmrLE--------IQRLHRRlkTTSLYVTH 193
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1045-1228 |
2.83e-11 |
|
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: 64.98 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1045 RPDVIVLREFCLKVKGGTMVAVVGGSGSGKST---VIWLMQRFYDPIGGKVMMGGRDL-RDLDLKwlrlQTALVGQEPAL 1120
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGQPRkPDQFQK----CVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1121 FGG-TIGENIRFGNPNASWSEVEEAAKEAYIHNFicGLPRGYETEVGESGIQ-LSGGQKQRIAIARAIVKKSKVLLLDEA 1198
Cdd:cd03234 93 LPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDV--LLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190
....*....|....*....|....*....|.
gi 1770234124 1199 TSALDLESEKHVQDAIRKIIKRTTTIVV-VH 1228
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILtIH 201
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
398-617 |
3.01e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 66.67 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKN--VSFAYPSRmSVPILNSLNLVIPSQRISALVGASGAGKS-TIFALLERFYDPNK--GLILLDGQDIRTL---QV 469
Cdd:PRK09473 13 LDVKDlrVTFSTPDG-DVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREILNLpekEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 470 KWLRS-QMGMVGQEPVL-------FADTILEnILMGKENATKKEAIDACI----AVN---AHNFICDLPQgydtqvgekg 534
Cdd:PRK09473 92 NKLRAeQISMIFQDPMTslnpymrVGEQLME-VLMLHKGMSKAEAFEESVrmldAVKmpeARKRMKMYPH---------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 535 tQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTT--IVIAHRLATVKN-AETIIVLEQGS 611
Cdd:PRK09473 161 -EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGiCDKVLVMYAGR 239
|
....*.
gi 1770234124 612 VIEIGD 617
Cdd:PRK09473 240 TMEYGN 245
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
415-643 |
3.51e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 415 ILNSLNLVIPSQRISALVGASGAGKSTIF-ALLERFYDPN-KGLILLDGQDIrtlqVKWLRSQMGMVGQEPVLFAD-TIL 491
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLnALAGRIQGNNfTGTILANNRKP----TKQILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 492 E-----NILMGKENATKKEAIDACIAVNAHnfiCDLPQGYDTQVGEKGTQ-LSGGQKQRIALARAMIKDPKILLLDEPTS 565
Cdd:PLN03211 159 EtlvfcSLLRLPKSLTKQEKILVAESVISE---LGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 566 ALDPKSE-SLVQQAIDKISKGRTTIVIAHRLAT--VKNAETIIVLEQGSVIEIGDHNKLMaqegAYFSLIKLaTEAISSN 642
Cdd:PLN03211 236 GLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAM----AYFESVGF-SPSFPMN 310
|
.
gi 1770234124 643 P 643
Cdd:PLN03211 311 P 311
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1050-1251 |
3.60e-11 |
|
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: 64.09 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRF--YDPIGGKVMMGGRDLRDLDLKwlrlQTALVG-----QEPALFG 1122
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE----ERARLGiflafQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1123 G-TIGENIRFGNpnaswseveeaakeayihnficglprgyeteVGesgiqLSGGQKQRIAIARAIVKKSKVLLLDEATSA 1201
Cdd:cd03217 91 GvKNADFLRYVN-------------------------------EG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1202 LDLESEKHVQDAIRKIIKRTTTIVVV---HRLSTIKKANAIAVVQNGKVSEYG 1251
Cdd:cd03217 135 LDIDALRLVAEVINKLREEGKSVLIIthyQRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1048-1259 |
3.84e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.38 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1048 VIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLD-LKWLRLQTALVGQEPALFGG-TI 1125
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1126 GENIRFGNPNaswSEVEEAAKEAYIHNFICGLprgyetEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALD-L 1204
Cdd:PRK15439 104 KENILFGLPK---RQASMQKMKQLLAALGCQL------DLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1205 ESEKHVQDaIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:PRK15439 175 ETERLFSR-IRELLAQGVGIVFIsHKLPEIRQlADRISVMRDGTIALSGKTADLSTD 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1038-1250 |
4.17e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1038 VNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRdlrdldlkwlrLQTALVGQE 1117
Cdd:COG0488 4 LSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1118 PALF-GGTIGENI-------------------RFGNPNASWSEVEE-----AAKEAY---------IHNFicGLPRG-YE 1162
Cdd:COG0488 70 PPLDdDLTVLDTVldgdaelraleaeleeleaKLAEPDEDLERLAElqeefEALGGWeaearaeeiLSGL--GFPEEdLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1163 TEVGEsgiqLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLES----EKHVQDairkiikRTTTIVVV-H-R--LSTIk 1234
Cdd:COG0488 148 RPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKN-------YPGTVLVVsHdRyfLDRV- 215
|
250
....*....|....*.
gi 1770234124 1235 kANAIAVVQNGKVSEY 1250
Cdd:COG0488 216 -ATRILELDRGKLTLY 230
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1045-1231 |
5.55e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.38 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1045 RPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTviwLMQ--RFYDP----IGGKVMMGGRDLrdlDLKWLRLQTALVGQEP 1118
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTT---LMNalAFRSPkgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1119 ALFGG-TIGENI----RFGNPNASWSEVEEAAKEAYIHNFicGLPRGYETEVGESGIQ--LSGGQKQRIAIARAIVKKSK 1191
Cdd:TIGR00955 109 LFIPTlTVREHLmfqaHLRMPRRVTKKEKRERVDEVLQAL--GLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1770234124 1192 VLLLDEATSALDLESEKHVQDAIRKII-KRTTTIVVVHRLS 1231
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAqKGKTIICTIHQPS 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1042-1220 |
7.33e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.89 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1042 YPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTViwlmqrFY------DPIGGKVMMGGRDLRDLDLkWLRlqtALVG 1115
Cdd:COG1137 13 YGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKR---ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1116 -----QEPALFGG-TIGENIR----FGNPNASwsEVEEAAkEAYIHNFicGLprgyeTEVGES-GIQLSGGQKQRIAIAR 1184
Cdd:COG1137 80 igylpQEASIFRKlTVEDNILavleLRKLSKK--EREERL-EELLEEF--GI-----THLRKSkAYSLSGGERRRVEIAR 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 1770234124 1185 AIVKKSKVLLLDEATSALDLESekhVQDaIRKIIKR 1220
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIA---VAD-IQKIIRH 181
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1056-1228 |
7.78e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.64 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKW---LRLQTalVG----------------- 1115
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKH--VGfvfqsfmliptlnalen 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1116 -QEPALFGGTigenirfgNPNASWSEVEEAAKEAYIHNFICGLPRgyetevgesgiQLSGGQKQRIAIARAIVKKSKVLL 1194
Cdd:PRK10584 109 vELPALLRGE--------SSRQSRNGAKALLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 1770234124 1195 LDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVH 1228
Cdd:PRK10584 170 ADEPTGNLDRQTGDKIADLLFSLNREhgTTLILVTH 205
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1044-1271 |
8.08e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 64.47 E-value: 8.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1044 SRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPalfgg 1123
Cdd:COG4167 22 RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDP----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 tigeNIRFgNP--------------NASWSEVEEAAK---------------EAYIHnficglprgyetevgesgiQLSG 1174
Cdd:COG4167 97 ----NTSL-NPrlnigqileeplrlNTDLTAEEREERifatlrlvgllpehaNFYPH-------------------MLSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1175 GQKQRIAIARAIVKKSKVLLLDEATSALDLesekhvqdAIR-KII---------KRTTTIVVVHRLSTIKK-ANAIAVVQ 1243
Cdd:COG4167 153 GQKQRVALARALILQPKIIIADEALAALDM--------SVRsQIInlmlelqekLGISYIYVSQHLGIVKHiSDKVLVMH 224
|
250 260
....*....|....*....|....*...
gi 1770234124 1244 NGKVSEYGTHDTLLTNHSNGVYATLVHS 1271
Cdd:COG4167 225 QGEVVEYGKTAEVFANPQHEVTKRLIES 252
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
715-974 |
8.76e-11 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 64.73 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 715 VGVIFGMLAGAILSLF-PLVLGQALTVYFNPDKSKLQKD---VGYLCLALVGLGFGCILTMMGQQGFCGWAGTKLTKRVR 790
Cdd:cd18547 2 ILVIILAIISTLLSVLgPYLLGKAIDLIIEGLGGGGGVDfsgLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 791 DLLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPFTL 870
Cdd:cd18547 82 KDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 871 GASYFslIINIGSKLdndsFDK-------ASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKrSQITGIALG 943
Cdd:cd18547 160 LVTKF--IAKRSQKY----FRKqqkalgeLNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFK-AQFYSGLLM 232
|
250 260 270
....*....|....*....|....*....|..
gi 1770234124 944 -ISQGAMYSAYTLVLFFGAYLVKKDYTKFGDV 974
Cdd:cd18547 233 pIMNFINNLGYVLVAVVGGLLVINGALTVGVI 264
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
398-626 |
1.05e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.80 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVsfAYPSRmsvpiLNSLNLVIPSQRISALVGASGAGKSTIFA----LLerfydPNKGLILLDGQDIRTLQVK--- 470
Cdd:PRK03695 1 MQLNDV--AVSTR-----LGPLSAEVRAGEILHLVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAela 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 471 ----WLrSQmgmvgQEPVLFADTILENILMGKENATKKEAIDACIavnahNFICDLPQGYDtQVGEKGTQLSGGQKQRIA 546
Cdd:PRK03695 69 rhraYL-SQ-----QQTPPFAMPVFQYLTLHQPDKTRTEAVASAL-----NEVAEALGLDD-KLGRSVNQLSGGEWQRVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 547 LARAMIK-------DPKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRLA-TVKNAETIIVLEQGSVIEIGD 617
Cdd:PRK03695 137 LAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGR 216
|
....*....
gi 1770234124 618 HNKLMAQEG 626
Cdd:PRK03695 217 RDEVLTPEN 225
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1047-1251 |
1.08e-10 |
|
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: 63.07 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDlkwlRLQTALVGQEPALFGG-TI 1125
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYPKmKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1126 GENIRF-----GNPNaswsevEEAAKEA--YIHNFicGLpRGYETEVGEsgiQLSGGQKQRIAIARAIVKKSKVLLLDEA 1198
Cdd:cd03269 88 IDQLVYlaqlkGLKK------EEARRRIdeWLERL--EL-SEYANKRVE---ELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1199 TSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYG 1251
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILStHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
75-233 |
1.10e-10 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 64.35 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 75 IIIGCLGALINGGSQPWYSYLFGNFVNKIALDNDKDQMI--KDVRELCVLMSALSGIVVIGAYLQIACWRLVGERLGHRI 152
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVdfSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 153 RSKYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTM 232
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDT-HSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSL 159
|
.
gi 1770234124 233 F 233
Cdd:cd18547 160 L 160
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1045-1252 |
1.93e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.65 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1045 RPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQT------------- 1111
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEqsaaqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 -ALVGQEPAL-------FGGTIGENIRFgNPNASwseVEEAAKEAYIHNFICGLPRGyETEVGESGIQLSGGQKQRIAIA 1183
Cdd:PRK10261 106 mAMIFQEPMTslnpvftVGEQIAESIRL-HQGAS---REEAMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1184 RAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTT--TIVVVHRLSTIKK-ANAIAVVQNGKVSEYGT 1252
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
400-593 |
2.26e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.96 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 400 LKNVSFAYPSRMsvPILNSLNL-VIPSQRIsALVGASGAGKST---IFALLERFYDpnkglilldGQDIRTLQVKwlrsq 475
Cdd:TIGR03719 7 MNRVSKVVPPKK--EILKDISLsFFPGAKI-GVLGLNGAGKSTllrIMAGVDKDFN---------GEARPQPGIK----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MGMVGQEPVLFAD-TILENILMG-----------------------------KENATKKEAIDAC----------IAVNA 515
Cdd:TIGR03719 70 VGYLPQEPQLDPTkTVRENVEEGvaeikdaldrfneisakyaepdadfdklaAEQAELQEIIDAAdawdldsqleIAMDA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 516 HNficdLPQGyDTQVgekgTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKIsKGrTTIVIAH 593
Cdd:TIGR03719 150 LR----CPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
431-579 |
2.35e-10 |
|
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: 61.74 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 431 LVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMGMVGQEPVLFADTILENILMGKENATKKEAIDAC 510
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQVEEAL 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 511 IAVNAHNFIcDLPQGydtqvgekgtQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAI 579
Cdd:cd03231 111 ARVGLNGFE-DRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
409-593 |
2.96e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.79 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 409 SRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQvkwlRSQ-MGMVGQEPVLFA 487
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 488 D-TILENI--LMGKENATKKEAIDACIAvnahnfICDLPQGYDTQVgekgTQLSGGQKQRIALARAMIKDPKILLLDEPT 564
Cdd:PRK13543 96 DlSTLENLhfLCGLHGRRAKQMPGSALA------IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPY 165
|
170 180 190
....*....|....*....|....*....|
gi 1770234124 565 SALDPKSESLVQQAID-KISKGRTTIVIAH 593
Cdd:PRK13543 166 ANLDLEGITLVNRMISaHLRGGGAALVTTH 195
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
431-616 |
4.34e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.22 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 431 LVGASGAGKS----TIFALLERfydPNKGL---ILLDGQDIRTLQVKWLR----SQMGMVGQEPVLFAD-------TILE 492
Cdd:PRK11022 38 IVGESGSGKSvsslAIMGLIDY---PGRVMaekLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMTSLNpcytvgfQIME 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 493 NILM---GKENATKKEAIDACIAVNahnfICDLPQGYDTQvgekGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDP 569
Cdd:PRK11022 115 AIKVhqgGNKKTRRQRAIDLLNQVG----IPDPASRLDVY----PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 570 KSESlvqQAIDKI-----SKGRTTIVIAHRLATV-KNAETIIVLEQGSVIEIG 616
Cdd:PRK11022 187 TIQA---QIIELLlelqqKENMALVLITHDLALVaEAAHKIIVMYAGQVVETG 236
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1049-1260 |
4.41e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.15 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1049 IVLREFCLKVKGGTMVAVVGGSGSGKSTVI-WLMQRFYDP-------IGGKVMMGGRDLRDLDLKWLRLQTALVGQ--EP 1118
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1119 AlFGGTIGENIRFGN-PNAswseveEAAKEAYIHN---FICGLPR-GYETEVGESGIQLSGGQKQRIAIARAIVK----- 1188
Cdd:PRK13547 95 A-FAFSAREIVLLGRyPHA------RRAGALTHRDgeiAWQALALaGATALVGRDVTTLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1189 ----KSKVLLLDEATSALDLESEKHVQDAIRKIIK--RTTTIVVVHRLS-TIKKANAIAVVQNGKVSEYGT-HDTLLTNH 1260
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGApADVLTPAH 247
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1046-1255 |
4.55e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.89 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1046 PDVIVLREFCLKVKGGTMVAVVGGSGSGKSTviwLMQ---RFYDPIGGKVMMGGRDL-----RDLdlkwLRLQTALVGQE 1117
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKST---LMKilyGLYQPDSGEILIDGKPVrirspRDA----IALGIGMVHQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1118 PALFGG-TIGENIRFGNPNA-----SWSEVEEAAKE------------AYIHnficglprgyetevgesgiQLSGGQKQR 1179
Cdd:COG3845 89 FMLVPNlTVAENIVLGLEPTkggrlDRKAARARIRElserygldvdpdAKVE-------------------DLSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 1180 IAIARAIVKKSKVLLLDEATSAL-DLESEkHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKVSeyGTHDT 1255
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLtPQEAD-ELFEILRRLAAEGKSIIFItHKLREVMAiADRVTVLRRGKVV--GTVDT 225
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
128-378 |
4.96e-10 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 62.50 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 128 GIVVIGA--YLQIACWRLVGERLG----HRIRSKYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGdKMSQFIY 201
Cdd:cd18543 44 LLLALGVaeAVLSFLRRYLAGRLSlgveHDLRTDLFAHLQRLDGAFHDR-WQSGQLLSRATSDLSLVQRFLA-FGPFLLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 202 HIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFCGVAYKAVYVGLAAKevnSYKKAG---SIAEQAIGSIRTVFSFVAEDS 278
Cdd:cd18543 122 NLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRR---AQDQAGdlaTVVEESVTGIRVVKAFGRERR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 279 ---------------------LAARYDAVLdESVPigkklgfakGIGLGVIylvtystwalaFWYGSILVSRNELSGGAA 337
Cdd:cd18543 199 eldrfeaaarrlratrlraarLRARFWPLL-EALP---------ELGLAAV-----------LALGGWLVANGSLTLGTL 257
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1770234124 338 IAcFFGVTIGGRGLALSLSYFAQFAQGTVAASkvfaiiDRI 378
Cdd:cd18543 258 VA-FSAYLTMLVWPVRMLGWLLAMAQRARAAA------ERV 291
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1050-1247 |
5.84e-10 |
|
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: 60.14 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLD-LKWLRLQTALVGQEP---ALFGG-T 1124
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDRkreGLVLDlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1125 IGENIRFGnpnaswseveeaakeayihnficglprgyetevgesgIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDL 1204
Cdd:cd03215 95 VAENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1770234124 1205 ESEKHVQDAIRKIIKRTTTIVVVhrlST-----IKKANAIAVVQNGKV 1247
Cdd:cd03215 138 GAKAEIYRLIRELADAGKAVLLI---SSeldelLGLCDRILVMYEGRI 182
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1049-1258 |
7.81e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.54 E-value: 7.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1049 IVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPALFGG-TIGE 1127
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1128 NIRFGN-PN----ASW-SEVEEAAKEAYIHNFICGLprgyeteVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSA 1201
Cdd:PRK10253 101 LVARGRyPHqplfTRWrKEDEEAVTKAMQATGITHL-------ADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1202 LDLESEKHVQDAIRKI--IKRTTTIVVVHRLS-TIKKANAIAVVQNGKVSEYGTHDTLLT 1258
Cdd:PRK10253 174 LDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1047-1246 |
8.65e-10 |
|
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: 63.31 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYdPIG---GKVMMGGRDL-----RDLDLKWLrlqtALVGQEP 1118
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLkasniRDTERAGI----VIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1119 ALFGG-TIGENIRFGNP----------NASWSEVEEAAKEAYIHNFICGLPRGyetevgesgiQLSGGQKQRIAIARAIV 1187
Cdd:TIGR02633 88 TLVPElSVAENIFLGNEitlpggrmayNAMYLRAKNLLRELQLDADNVTRPVG----------DYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1188 KKSKVLLLDEATSALDLESEKHVQDAIRKIIKR-TTTIVVVHRLSTIKK-ANAIAVVQNGK 1246
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHgVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1051-1291 |
9.27e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1051 LREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDldlkwlRLQTALVGQEPAlfggtigenir 1130
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ------ALQKNLVAYVPQ----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1131 fgNPNASWS---EVEEAAKEA-YIHNFICGLPRGYETEVGESGI--------------QLSGGQKQRIAIARAIVKKSKV 1192
Cdd:PRK15056 86 --SEEVDWSfpvLVEDVVMMGrYGHMGWLRRAKKRDRQIVTAALarvdmvefrhrqigELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1193 LLLDEATSALDLESEKHVQDAIRKIIKRTTTIVV-VHRLSTIKKANAIAVVQNGKVSEYGTHDTLLT--NHSNGVYATLV 1269
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVsTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTaeNLELAFSGVLR 243
|
250 260
....*....|....*....|..
gi 1770234124 1270 HSEMEANADHFslvqqpVTDPE 1291
Cdd:PRK15056 244 HVALNGSEESI------ITDDE 259
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
398-597 |
1.27e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.65 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLdGQDIrtlqvkwlrsQMG 477
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD--TILENILMGKENAT--KKEaIDACIAVNAHNFicdlpQGYDTQ--VGekgtQLSGGQKQRIALARAM 551
Cdd:TIGR03719 389 YVDQSRDALDPnkTVWEEISGGLDIIKlgKRE-IPSRAYVGRFNF-----KGSDQQkkVG----QLSGGERNRVHLAKTL 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 552 IKDPKILLLDEPTSALDPKSESLVQQAIDKIskGRTTIVIAH------RLAT 597
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
395-610 |
1.27e-09 |
|
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: 59.56 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 395 HGRLELKNVSFAYPS-RMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPN--KGLILLDGQDIRtlqvKW 471
Cdd:cd03232 1 GSVLTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD----KN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 472 LRSQMGMVGQEPVLFadtilenilmgkENATKKEAIDaciavnahnFICDLpqgydtqvgeKGtqLSGGQKQRIALARAM 551
Cdd:cd03232 77 FQRSTGYVEQQDVHS------------PNLTVREALR---------FSALL----------RG--LSVEQRKRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 552 IKDPKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHR--LATVKNAETIIVLEQG 610
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
433-602 |
1.45e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 433 GASGAGKSTIFALLERFYDPNKGLILLDGQDIRTL------QVKWLRSQMGMvgqEPVLfadTILEN--ILMGKENATKK 504
Cdd:PRK13538 34 GPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGI---KTEL---TALENlrFYQRLHGPGDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 505 EAI-DACIAVNAHNFIcDLPQGydtqvgekgtQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDK-I 582
Cdd:PRK13538 108 EALwEALAQVGLAGFE-DVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQhA 176
|
170 180
....*....|....*....|
gi 1770234124 583 SKGRTTIVIAHRLATVKNAE 602
Cdd:PRK13538 177 EQGGMVILTTHQDLPVASDK 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
430-608 |
1.47e-09 |
|
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: 58.15 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 430 ALVGASGAGKSTIFALLERFYDP-NKGLILLDGQDIRTLQVKWLRsqmgmvgqepvlfadtilenilmgkenatkkeaid 508
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPpGGGVIYIDGEDILEEVLDQLL----------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 509 aciavnahnficdlpqgyDTQVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAID-------K 581
Cdd:smart00382 51 ------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllllK 112
|
170 180
....*....|....*....|....*..
gi 1770234124 582 ISKGRTTIVIAHRLATVKNAETIIVLE 608
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGPALLRRRFD 139
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1044-1245 |
1.52e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.49 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1044 SRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKW-LRLQTALVGQEPALFG 1122
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQELSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1123 G-TIGENIR---------FGNPNASWSEVEEAAKEAYIhnfICGLPRGYETEVGEsgiqLSGGQKQRIAIARAIVKKSKV 1192
Cdd:PRK09700 94 ElTVLENLYigrhltkkvCGVNIIDWREMRVRAAMMLL---RVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1193 LLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNG 1245
Cdd:PRK09700 167 IIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYIsHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1053-1233 |
1.64e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1053 EFCLKVKGGTM-----VAVVGGSGSGKSTVIWLMQRFYDPIGGKVmmggrdlrDLDLKwlrlqtalVGQEP----ALFGG 1123
Cdd:PRK13409 352 DFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELK--------ISYKPqyikPDYDG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 TIGENIRFGNPNAS----WSEVeeaakeayIHNFicGLPRGYETEVGEsgiqLSGGQKQRIAIARAIVKKSKVLLLDEAT 1199
Cdd:PRK13409 416 TVEDLLRSITDDLGssyyKSEI--------IKPL--QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190
....*....|....*....|....*....|....*.
gi 1770234124 1200 SALDLESEKHVQDAIRKII--KRTTTIVVVHRLSTI 1233
Cdd:PRK13409 482 AHLDVEQRLAVAKAIRRIAeeREATALVVDHDIYMI 517
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1050-1229 |
1.72e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.59 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFY--DPIGGKVmmggrDLRDLDLkwlrlqtalvGQEPALFggtigE 1127
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV-----DVPDNQF----------GREASLI-----D 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1128 NI-RFGNPNAswseveeaAKEAyIHNfiCGL--PRGYETEVGEsgiqLSGGQKQRIAIARAIVKKSKVLLLDEATSALDL 1204
Cdd:COG2401 105 AIgRKGDFKD--------AVEL-LNA--VGLsdAVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*..
gi 1770234124 1205 ESEKHVQDAIRKIIKR--TTTIVVVHR 1229
Cdd:COG2401 170 QTAKRVARNLQKLARRagITLVVATHH 196
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
397-623 |
1.93e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.10 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAYPsrmsVPILNSLNLVIPSQRISALVGASGAGKS-TIFALLERFydP-----NKGLILLDGQDIRTLQvk 470
Cdd:PRK10418 4 QIELRNIALQAA----QPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PagvrqTAGRVLLDGKPVAPCA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 471 wLRSQM-GMVGQEP-------VLFADTILENIL-MGKE--NATKKEAIDACIAVNAHNficdLPQGYdtqvgekGTQLSG 539
Cdd:PRK10418 76 -LRGRKiATIMQNPrsafnplHTMHTHARETCLaLGKPadDATLTAALEAVGLENAAR----VLKLY-------PFEMSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 540 GQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAHRLATV-KNAETIIVLEQGSVIEIG 616
Cdd:PRK10418 144 GMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
....*..
gi 1770234124 617 DHNKLMA 623
Cdd:PRK10418 224 DVETLFN 230
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1038-1217 |
2.28e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1038 VNFAYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLrDLDLKWLRLQTALVGQE 1117
Cdd:PRK13540 7 LDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1118 ----PALfggTIGEN----IRFGNPNASWSEVEEAAKEAYIHNFICGLprgyetevgesgiqLSGGQKQRIAIARAIVKK 1189
Cdd:PRK13540 83 sginPYL---TLRENclydIHFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSK 145
|
170 180
....*....|....*....|....*...
gi 1770234124 1190 SKVLLLDEATSALDlesEKHVQDAIRKI 1217
Cdd:PRK13540 146 AKLWLLDEPLVALD---ELSLLTIITKI 170
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1047-1252 |
3.96e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.93 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKST---VIwlMQR-FYDPIGGKVMMGGRDLRDLDLKwlrlQTALVG-----QE 1117
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVL--MGHpKYEVTSGSILLDGEDILELSPD----ERARAGiflafQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1118 PALFGG--------TIGENIRFGNPNA--SWSEVEEAAKEAyihnficGLPRGY-ETEVGESgiqLSGGQKQRIAIARAI 1186
Cdd:COG0396 86 PVEIPGvsvsnflrTALNARRGEELSAreFLKLLKEKMKEL-------GLDEDFlDRYVNEG---FSGGEKKRNEILQML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 1187 VKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-H--RLSTIKKANAIAVVQNGKVSEYGT 1252
Cdd:COG0396 156 LLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIItHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
783-973 |
4.15e-09 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 59.79 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 783 TKLTKRVRDLLFRSILNQEPGWFDSDQnsPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLA 862
Cdd:cd18589 65 SRIHSRLQGLVFAAVLRQEIAFFDSNQ--TGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 863 TIVTPFTLGASYFS--LIINIGSKLdNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKS----------S 930
Cdd:cd18589 143 ALGLPLLLLVPKFVgkFQQSLAVQV-QKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRlnkkeaaayaV 221
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1770234124 931 SIKRSQITGIALGISqgamysaytlVLFFGAYLVKKDYTKFGD 973
Cdd:cd18589 222 SMWTSSFSGLALKVG----------ILYYGGQLVTAGTVSSGD 254
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1058-1225 |
4.69e-09 |
|
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: 57.64 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1058 VKGGTMVAVVGGSGSGKSTVI-WLMQRFYD-PIGGKVMMGGRDLRdldlKWLRLQTALVGQEPALFGG-TIGENIRFgnp 1134
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLdVLAGRKTAgVITGEILINGRPLD----KNFQRSTGYVEQQDVHSPNlTVREALRF--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1135 naswseveeaakEAYIhnficglpRGyetevgesgiqLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAI 1214
Cdd:cd03232 103 ------------SALL--------RG-----------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
170
....*....|.
gi 1770234124 1215 RKIIKRTTTIV 1225
Cdd:cd03232 152 KKLADSGQAIL 162
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
430-655 |
4.71e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 59.72 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 430 ALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRsQMGMV-GQEPVLFAD-TILENILMGKE-----NAT 502
Cdd:COG4586 52 GFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfGQRSQLWWDlPAIDSFRLLKAiyripDAE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 503 KKEAIDACIAV-NAHNFIcdlpqgyDTQVgekgTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDK 581
Cdd:COG4586 131 YKKRLDELVELlDLGELL-------DTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 582 ISKGR-TTIVIA-HRLATVKN-AETIIVLEQGSVIEIGDHNKLMAQEGAYfSLIKLATEAISSNPVSKKGKTVINQE 655
Cdd:COG4586 200 YNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY-KTIVLELAEPVPPLELPRGGEVIERE 275
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
398-617 |
4.84e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.88 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVsfaYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLERF--YDPNKGLILLDGQDIRTLQVKwLRSQ 475
Cdd:CHL00131 8 LEIKNL---HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 476 MG--MVGQEPVLFADTILENILMGKENATKK-------EAIDACIAVNAHNFICDLPQGYDTQVGEKGtqLSGGQKQRIA 546
Cdd:CHL00131 84 LGifLAFQYPIEIPGVSNADFLRLAYNSKRKfqglpelDPLEFLEIINEKLKLVGMDPSFLSRNVNEG--FSGGEKKRNE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 547 LARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKIS-KGRTTIVIAH--RLATVKNAETIIVLEQGSVIEIGD 617
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
382-568 |
5.20e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.95 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 382 DPYSTTGRKPETV-HGRLELKNVSFAYPSRMsvpILNS--LNLViPSQRIsALVGASGAGKSTIFALLERFYDPNKGLIL 458
Cdd:PRK10636 296 NPFHFSFRAPESLpNPLLKMEKVSAGYGDRI---ILDSikLNLV-PGSRI-GLLGRNGAGKSTLIKLLAGELAPVSGEIG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 459 LdGQDIRtlqvkwlrsqMGMVGQEPVLF--AD-TILENILMGKENATKKEAIDaciAVNAHNFICDlpqgydtQVGEKGT 535
Cdd:PRK10636 371 L-AKGIK----------LGYFAQHQLEFlrADeSPLQHLARLAPQELEQKLRD---YLGGFGFQGD-------KVTEETR 429
|
170 180 190
....*....|....*....|....*....|...
gi 1770234124 536 QLSGGQKQRIALARAMIKDPKILLLDEPTSALD 568
Cdd:PRK10636 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1053-1233 |
5.26e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.95 E-value: 5.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1053 EFCLKVKGGTM-----VAVVGGSGSGKSTVIWLMQRFYDPIGGKVmmggrdlrDLDLKwlrlqtalVGQEP----ALFGG 1123
Cdd:COG1245 353 GFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLK--------ISYKPqyisPDYDG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 TIGENIRFGNPNA---SWSEVEeaakeaYIHNFicGLPRGYETEVGEsgiqLSGGQKQRIAIARAIVKKSKVLLLDEATS 1200
Cdd:COG1245 417 TVEEFLRSANTDDfgsSYYKTE------IIKPL--GLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190
....*....|....*....|....*....|....*
gi 1770234124 1201 ALDLESEKHVQDAIRKII--KRTTTIVVVHRLSTI 1233
Cdd:COG1245 485 HLDVEQRLAVAKAIRRFAenRGKTAMVVDHDIYLI 519
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
400-571 |
5.80e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 400 LKNVSFAYPSRMsvPILNSLNL-VIPSQRIsALVGASGAGKST---IFALLERFYD----PNKGLilldgqdirtlqvkw 471
Cdd:PRK11819 9 MNRVSKVVPPKK--QILKDISLsFFPGAKI-GVLGLNGAGKSTllrIMAGVDKEFEgearPAPGI--------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 472 lrsQMGMVGQEPVLFAD-TILENILMG-----------------------------KENATKKEAIDACiavNAHNFicD 521
Cdd:PRK11819 71 ---KVGYLPQEPQLDPEkTVRENVEEGvaevkaaldrfneiyaayaepdadfdalaAEQGELQEIIDAA---DAWDL--D 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 522 -----------LPQGyDTQVgekgTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKS 571
Cdd:PRK11819 143 sqleiamdalrCPPW-DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
430-616 |
5.89e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.78 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 430 ALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQV---------KWLRSQMGMVGQEPvlfAD------TILENI 494
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerrRLLRTEWGFVHQHP---RDglrmqvSAGGNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 495 ---LMG---------KENATK---KEAIDAciavnahNFICDLPqgydtqvgekgTQLSGGQKQRIALARAMIKDPKILL 559
Cdd:PRK11701 113 gerLMAvgarhygdiRATAGDwleRVEIDA-------ARIDDLP-----------TTFSGGMQQRLQIARNLVTHPRLVF 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 560 LDEPTSALDPKSE--------SLVQQAidkiskGRTTIVIAHRLATVKN-AETIIVLEQGSVIEIG 616
Cdd:PRK11701 175 MDEPTGGLDVSVQarlldllrGLVREL------GLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
715-964 |
6.00e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 59.03 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 715 VGVIFGMLAGAILSLFPLVLGQALTvyfnpDKSKLQKDVG---YLCLALVGLGFGCILTMMGQQGFCGWAGTKLTKRVRD 791
Cdd:cd18550 2 ALVLLLILLSALLGLLPPLLLREII-----DDALPQGDLGllvLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 792 LLFRSILNQEPGWFDSdqNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTP-FTL 870
Cdd:cd18550 77 QLYAHLQRMSLAFFTR--TRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPlFVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 871 GASYFSLIINigsKLDNDSFDKASGIASAA-----VSNIRTVTTLATQEKIVQSFEQslskpKSSSIKRSQITGIALGIS 945
Cdd:cd18550 155 PTRRVGRRRR---KLTREQQEKLAELNSIMqetlsVSGALLVKLFGREDDEAARFAR-----RSRELRDLGVRQALAGRW 226
|
250 260
....*....|....*....|....
gi 1770234124 946 QGAMYSAYT-----LVLFFGAYLV 964
Cdd:cd18550 227 FFAALGLFTaigpaLVYWVGGLLV 250
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
525-602 |
6.53e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 525 GYDTQVGEKGTQ-LSGGQkQRIAL-ARAMIKDPKILLLDEPTSALDPKSESLVQQAIDK-ISKGRTTIV----------- 590
Cdd:PRK10938 389 GIDKRTADAPFHsLSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapa 467
|
90
....*....|...
gi 1770234124 591 -IAHRLATVKNAE 602
Cdd:PRK10938 468 cITHRLEFVPDGD 480
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
414-618 |
6.77e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.26 E-value: 6.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 414 PILNSLNLVIPSQRISALVGASGAGKSTIFALL--ERFYDPNKGLILLDGQDIRTLQVKwLRSQMG--MVGQEPVLFADT 489
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGifMAFQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 490 ILENILMGKENATKK----EAIDaciAVNAHNFI------CDLPQGYDTQVGEKGtqLSGGQKQRIALARAMIKDPKILL 559
Cdd:PRK09580 94 SNQFFLQTALNAVRSyrgqEPLD---RFDFQDLMeekialLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 560 LDEPTSALDPKSESLVQQAIDKISKG-RTTIVIAH--RLATVKNAETIIVLEQGSVIEIGDH 618
Cdd:PRK09580 169 LDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1061-1240 |
7.35e-09 |
|
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: 56.23 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1061 GTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMggrdlrdLDLKWLRLQTALvgqepalfggtigenirfgnpnaswse 1140
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLD--------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1141 veeaakeayihnficglpRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIR----- 1215
Cdd:smart00382 48 ------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlll 109
|
170 180
....*....|....*....|....*..
gi 1770234124 1216 --KIIKRTTTIVVVHRLSTIKKANAIA 1240
Cdd:smart00382 110 llKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1170-1252 |
7.60e-09 |
|
ATP-binding cassette domain 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 more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 56.81 E-value: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1170 IQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIK--RTTTIVVVHRLSTIKKANAIAVVQNGKV 1247
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEGEP 149
|
....*
gi 1770234124 1248 SEYGT 1252
Cdd:cd03222 150 GVYGI 154
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1057-1252 |
9.94e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.98 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1057 KVKGGTMVAVVGGSGSGKS-TVIWLMQRFYDPigGKVM-----MGGRDLRDLDLKWLRlqtALVGQEPALFggtigenir 1130
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaekleFNGQDLQRISEKERR---NLVGAEVAMI--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1131 FGNPNASWS-------EVEEAAKEAYIHNFICGLPRGYE--TEVG----ESGI-----QLSGGQKQRIAIARAIVKKSKV 1192
Cdd:PRK11022 95 FQDPMTSLNpcytvgfQIMEAIKVHQGGNKKTRRQRAIDllNQVGipdpASRLdvyphQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1193 LLLDEATSALDLESEKHVQDAIRKIIKRTTT--IVVVHRLSTIKK-ANAIAVVQNGKVSEYGT 1252
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEaAHKIIVMYAGQVVETGK 237
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
518-607 |
1.11e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 60.03 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 518 FICDLPQGYdTQVGEKGTQLSGGQKQRIALARAMIKD---PKILLLDEPTSAL---DPKSESLVQQAIdkISKGRTTIVI 591
Cdd:TIGR00630 812 TLCDVGLGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLQRL--VDKGNTVVVI 888
|
90
....*....|....*.
gi 1770234124 592 AHRLATVKNAETIIVL 607
Cdd:TIGR00630 889 EHNLDVIKTADYIIDL 904
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
389-579 |
1.17e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.66 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 389 RKPETVHG--RLELKNVSfaYPSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALL--ERfyDPNKGLILLDGQDI 464
Cdd:COG3845 247 EKAPAEPGevVLEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 465 RTLQVKWL-----------RSQMGMVGQEpvlfadTILENILMG---KENATKKEAID-ACIAVNAHNFICDL---PQGY 526
Cdd:COG3845 323 TGLSPRERrrlgvayipedRLGRGLVPDM------SVAENLILGryrRPPFSRGGFLDrKAIRAFAEELIEEFdvrTPGP 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 527 DTQVGekgtQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAI 579
Cdd:COG3845 397 DTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL 445
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
536-597 |
1.34e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 1.34e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 536 QLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLAT 597
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAV 273
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1044-1233 |
1.35e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1044 SRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKwlRLQTALVG---QEPAL 1120
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK--SSQEAGIGiihQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1121 FGG-TIGENI--------RFGNPNasWSEVEEAAKEAYIHnfiCGLPRGYETEVGEsgiqLSGGQKQRIAIARAIVKKSK 1191
Cdd:PRK10762 91 IPQlTIAENIflgrefvnRFGRID--WKKMYAEADKLLAR---LNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESK 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1770234124 1192 VLLLDEATSAL-DLESEKhVQDAIRKIIKRTTTIVVV-HRLSTI 1233
Cdd:PRK10762 162 VIIMDEPTDALtDTETES-LFRVIRELKSQGRGIVYIsHRLKEI 204
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
715-875 |
1.54e-08 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 57.78 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 715 VGVIFGMLAGAILSLF-PLVLGQALTVYFNPDKSKLQK----DVGYLCLALVGLGFGCILTMMGQqgfcgWAGTKLTKRV 789
Cdd:cd18544 2 ILALLLLLLATALELLgPLLIKRAIDDYIVPGQGDLQGllllALLYLGLLLLSFLLQYLQTYLLQ-----KLGQRIIYDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 790 RDLLFRSILNQEPGWFDsdQNSPGSLVSKL-----SVNcTSFRSILgdrySVLFMGLSSAAVGLSVSFYLEWRLALLATI 864
Cdd:cd18544 77 RRDLFSHIQRLPLSFFD--RTPVGRLVTRVtndteALN-ELFTSGL----VTLIGDLLLLIGILIAMFLLNWRLALISLL 149
|
170
....*....|.
gi 1770234124 865 VTPFTLGASYF 875
Cdd:cd18544 150 VLPLLLLATYL 160
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1049-1234 |
1.61e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 59.38 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1049 IVLREFCLKVKGGTMVAVVGGSGSGKSTV------IWlmqrfydPIggkvmMGGRDLRDLDLKWLrlqtaLVGQEPALFG 1122
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLfrilgeLW-------PV-----YGGRLTKPAKGKLF-----YVPQRPYMTL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1123 GTIGENI-------RFGNPNASWSEVEEAAKEAYIHNFIcglprgyETEVGESGIQ-----LSGGQKQRIAIARAIVKKS 1190
Cdd:TIGR00954 529 GTLRDQIiypdsseDMKRRGLSDKDLEQILDNVQLTHIL-------EREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKP 601
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1770234124 1191 KVLLLDEATSALDLESEKHVQDAIRKiiKRTTTIVVVHRLSTIK 1234
Cdd:TIGR00954 602 QFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWK 643
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1047-1252 |
1.62e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 57.81 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLkwlrlqtALVG---QEPALFGG 1123
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR-------RRIGylpEERGLYPK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 -TIGENIRF-----GnpnASWSEVEEAAKEaYIHNFicGLPRGYETEVGEsgiqLSGGQKQRIAIARAIVKKSKVLLLDE 1197
Cdd:COG4152 86 mKVGEQLVYlarlkG---LSKAEAKRRADE-WLERL--GLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1198 ATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYGT 1252
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
520-607 |
2.02e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 57.24 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 520 CDLPQGYdTQVGEKGTQLSGGQKQRIALARAMIK---DPKILLLDEPTSALDPKSeslVQQAIDK----ISKGRTTIVIA 592
Cdd:cd03271 154 CDVGLGY-IKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHD---VKKLLEVlqrlVDKGNTVVVIE 229
|
90
....*....|....*
gi 1770234124 593 HRLATVKNAETIIVL 607
Cdd:cd03271 230 HNLDVIKCADWIIDL 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1064-1256 |
2.77e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1064 VAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTALVGQEPAlfgGTIGENIRFGN----PNASWS 1139
Cdd:PRK15112 42 LAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPS---TSLNPRQRISQildfPLRLNT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1140 EVEEAAKEAYIHNFI--CGLPRGYETEVGEsgiQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKI 1217
Cdd:PRK15112 119 DLEPEQREKQIIETLrqVGLLPDHASYYPH---MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1770234124 1218 IKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYG-THDTL 1256
Cdd:PRK15112 196 QEKqgISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGsTADVL 238
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1027-1235 |
3.00e-08 |
|
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: 56.19 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1027 QSKPFDLEFKMVNFAYPSRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKW 1106
Cdd:cd03267 13 YSKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1107 LRLQTALVGQE-------PALFGGTIGENI------RFGNPNASWSEVEEAAKEAYIhnficglprgyetevgeSGIQLS 1173
Cdd:cd03267 93 LRRIGVVFGQKtqlwwdlPVIDSFYLLAAIydlppaRFKKRLDELSELLDLEELLDT-----------------PVRQLS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1174 GGQKQRIAIARAIVKKSKVLLLDEATSALDLesekHVQDAIRKIIKR------TTTIVVVHRLSTIKK 1235
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDV----VAQENIRNFLKEynrergTTVLLTSHYMKDIEA 219
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
398-593 |
3.27e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvPILNSLNLVI-PSQRIsALVGASGAGKSTIFALLERFYDPNKGlilldgqdirtlQVKWlrsqm 476
Cdd:PRK15064 320 LEVENLTKGFDNG---PLFKNLNLLLeAGERL-AIIGENGVGKTTLLRTLVGELEPDSG------------TVKW----- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 gmvgqepvlfadtilenilmgKENAtkkeAIDACIAVNAHNFICDL----------PQGYDTQ---------------VG 531
Cdd:PRK15064 379 ---------------------SENA----NIGYYAQDHAYDFENDLtlfdwmsqwrQEGDDEQavrgtlgrllfsqddIK 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 532 EKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKS-ESLvQQAIDKIsKGrTTIVIAH 593
Cdd:PRK15064 434 KSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESiESL-NMALEKY-EG-TLIFVSH 493
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1061-1204 |
3.33e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1061 GTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGR---DLRDLDLKWLRLQTALVGQEP-------ALFGGTIGENIR 1130
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPyasldprQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1131 FGNpnasWSEVEEAAKE-AYIHNFICGLPRG---YETEvgesgiqLSGGQKQRIAIARAIVKKSKVLLLDEATSALDL 1204
Cdd:PRK10261 430 VHG----LLPGKAAAARvAWLLERVGLLPEHawrYPHE-------FSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
377-594 |
3.43e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.22 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 377 RIPAIDPYSTTGRKPETVHGR---------LELKNVSFAYPSrmSVPILNSLNLVIPSQRISALVGASGAGKSTIFALLE 447
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGRgiveyqdngIKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILG 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 448 --------RFYDPNKGLILLDGQdirtlqvkwlRSQMGmVG--QEPVLFADTILEnilMGKENATKKEAIDACIAVNAHN 517
Cdd:TIGR00954 500 elwpvyggRLTKPAKGKLFYVPQ----------RPYMT-LGtlRDQIIYPDSSED---MKRRGLSDKDLEQILDNVQLTH 565
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 518 fICDLPQGYDTqVGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKisKGRTTIVIAHR 594
Cdd:TIGR00954 566 -ILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| R-SNARE |
cd15843 |
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment ... |
1471-1527 |
4.87e-08 |
|
SNARE motif, subgroup R-SNARE; SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins consist of coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). In contrast to Qa-, Qb- and Qc-SNAREs that are localized to target organelle membranes, R-SNAREs are localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles. Examples for members of the Qa SNAREs are syntaxin 18, syntaxin 5, syntaxin 16, and syntaxin 1.
Pssm-ID: 277196 [Multi-domain] Cd Length: 60 Bit Score: 50.96 E-value: 4.87e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1471 NISKLNDELYEVHQIMTRNVQEVLGVGEKLDQVSQMSSRLTSESRIYADKARDLNRQ 1527
Cdd:cd15843 2 KLSKVQEQVDEVKDVMQENIDKVLERGEKLEDLVDKTENLNESANAFKKQARKLKRK 58
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1170-1251 |
5.61e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.81 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1170 IQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTT--IVVVHRLSTIKK-ANAIAVVQNGK 1246
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIpiLYVSHSLDEILRlADRVVVLEQGK 206
|
....*
gi 1770234124 1247 VSEYG 1251
Cdd:PRK11144 207 VKAFG 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
428-593 |
5.70e-08 |
|
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: 55.49 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 428 ISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDI----RTLQVKWlrsqmgmvgqepvlfaDTILENILMGKENatk 503
Cdd:cd03237 27 VIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpQYIKADY----------------EGTVRDLLSSITK--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 504 keaiDACIAVNAHNFICD---LPQGYDTQVgekgTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAID 580
Cdd:cd03237 88 ----DFYTHPYFKTEIAKplqIEQILDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170
....*....|....*
gi 1770234124 581 KI--SKGRTTIVIAH 593
Cdd:cd03237 160 RFaeNNEKTAFVVEH 174
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1006-1252 |
6.77e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.27 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1006 PAVFEIMNRNPLIDGKgkkieqskpfDLEfkmVNFAYPSrPDVIVLREFCLKVKGGTMVAVVGGSGSGKS-TVIWLMQRF 1084
Cdd:PRK09473 1 TVPLAQQQADALLDVK----------DLR---VTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1085 YDP--IGGKVMMGGRDLRDLDLKWL-RL---QTALVGQEPAlfggT-------IGENI--------RFGNPNASWSEVE- 1142
Cdd:PRK09473 67 AANgrIGGSATFNGREILNLPEKELnKLraeQISMIFQDPM----TslnpymrVGEQLmevlmlhkGMSKAEAFEESVRm 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1143 -EAAK--EA------YIHNFicglprgyetevgesgiqlSGGQKQRIAIARAIVKKSKVLLLDEATSALDLEsekhVQDA 1213
Cdd:PRK09473 143 lDAVKmpEArkrmkmYPHEF-------------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVT----VQAQ 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1770234124 1214 IRKI---IKR---TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGT 1252
Cdd:PRK09473 200 IMTLlneLKRefnTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
400-611 |
8.27e-08 |
|
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: 54.19 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 400 LKNVSFAYPSRMS-VPILNSLNLVIPSQRISALVGASGAGKSTIFALL----ERFYDPNkGLILLDGQDIRTLQVKWlRS 474
Cdd:cd03233 6 WRNISFTTGKGRSkIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrtEGNVSVE-GDIHYNGIPYKEFAEKY-PG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQEPVLFAdtilenilmgkeNATKKEAIDACIAVNAHNFIcdlpqgydtqvgeKGtqLSGGQKQRIALARAMIKD 554
Cdd:cd03233 84 EIIYVSEEDVHFP------------TLTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 555 PKILLLDEPTSALDPKSeslvqqAIDKISKGRTtiviahrLATVKNAETIIVLEQGS 611
Cdd:cd03233 137 ASVLCWDNSTRGLDSST------ALEILKCIRT-------MADVLKTTTFVSLYQAS 180
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
398-612 |
1.01e-07 |
|
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: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSVPILNSLNLVIPSQRISALVGASGAGKS-TIFALLERFYDPNKGLILLDGQ--DIRTLQvKWLRS 474
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKpvDIRNPA-QAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 475 QMGMVGQE-------PVLfadTILENI----------LMGKENATKKEAIDACIA-VNAHNFICDLPQGydtqvgekgtQ 536
Cdd:TIGR02633 337 GIAMVPEDrkrhgivPIL---GVGKNItlsvlksfcfKMRIDAAAELQIIGSAIQrLKVKTASPFLPIG----------R 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 537 LSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKIS-KGRTTIVIAHRLATVKN-AETIIVLEQGSV 612
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
398-604 |
1.10e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 53.72 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRmsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLrsqmG 477
Cdd:PRK13541 2 LSLHQLQFNIEQK----NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----T 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQEPVLFAD-TILENILMGKENATKKEAIDACIavnaHNF-ICDLpqgydtqVGEKGTQLSGGQKQRIALARAMIKDP 555
Cdd:PRK13541 74 YIGHNLGLKLEmTVFENLKFWSEIYNSAETLYAAI----HYFkLHDL-------LDEKCYSLSSGMQKIVAIARLIACQS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1770234124 556 KILLLDEPTSALDPKSESLVQQAID-KISKGRTTIVIAHRLATVKNAETI 604
Cdd:PRK13541 143 DLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
531-638 |
1.42e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.51 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 531 GEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLATVKN-AETIIVLE 608
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQlAHELTVID 218
|
90 100 110
....*....|....*....|....*....|
gi 1770234124 609 QGSVIEIGDHNKLMAQEGAYFSLIKLATEA 638
Cdd:NF000106 219 RGRVIADGKVDELKTKVGGRTLQIRPAHAA 248
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1058-1239 |
1.75e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1058 VKGGTMVAVVGGSGSGKSTVI-WLMQRFYDPI--GGKVMMGGrdlRDLDLKWLRLQTALVGQEPALFGGTIGENIRFGNP 1134
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLnVLAERVTTGVitGGDRLVNG---RPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1135 NASWSEVEEAAKEAYIHNFI--CGLPRGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLL-LDEATSALDLESEKHVQ 1211
Cdd:TIGR00956 863 LRQPKSVSKSEKMEYVEEVIklLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSIC 942
|
170 180
....*....|....*....|....*...
gi 1770234124 1212 DAIRKIIKRTTTIvvvhrLSTIKKANAI 1239
Cdd:TIGR00956 943 KLMRKLADHGQAI-----LCTIHQPSAI 965
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
416-628 |
1.98e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.67 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 416 LNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTLQVKWLRSQMgmvgqepvlfadTILENI- 494
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQL------------TGIENIe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 495 ----LMGKENATKKEAIDACIA-VNAHNFICDLPQGYdtqvgekgtqlSGGQKQRIALARAMIKDPKILLLDEPTSALDp 569
Cdd:PRK13545 108 lkglMMGLTKEKIKEIIPEIIEfADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGD- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 570 ksESLVQQAIDKIS----KGRTTIVIAHRLATVKNAET-IIVLEQGSVIEIGDHNKLMAQEGAY 628
Cdd:PRK13545 176 --QTFTKKCLDKMNefkeQGKTIFFISHSLSQVKSFCTkALWLHYGQVKEYGDIKEVVDHYDEF 237
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1033-1197 |
1.99e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRPdvIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRLQTA 1112
Cdd:PRK10522 323 LELRNVTFAYQDNG--FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQEPALFGGTIG-ENirfgnpnaswSEVEEAAKEAYIHnfICGLPRGYETEVGE-SGIQLSGGQKQRIAIARAIVKKS 1190
Cdd:PRK10522 401 AVFTDFHLFDQLLGpEG----------KPANPALVEKWLE--RLKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEER 468
|
....*..
gi 1770234124 1191 KVLLLDE 1197
Cdd:PRK10522 469 DILLLDE 475
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1051-1225 |
2.05e-07 |
|
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: 53.04 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1051 LREFCLKVKGGTMVAVVGGSGSGKST---VIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLRlQTALVGQE----PALfgg 1123
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKYPG-EIIYVSEEdvhfPTL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 TIGENIRFgnpnaswseveeaAKEAYIHNFIcglpRGyetevgesgiqLSGGQKQRIAIARAIVKKSKVLLLDEATSALD 1203
Cdd:cd03233 99 TVRETLDF-------------ALRCKGNEFV----RG-----------ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180
....*....|....*....|....
gi 1770234124 1204 LESEKHVQDAIRKIIK--RTTTIV 1225
Cdd:cd03233 151 SSTALEILKCIRTMADvlKTTTFV 174
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1061-1232 |
2.14e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.66 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1061 GTMVAVVGGSGSGKSTVI-WLMQRFY-DPIGGKVMMGGRDLRDLDLKwlrlQTALVGQEPALFGG-TIGENIRFGN---- 1133
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLnALAGRIQgNNFTGTILANNRKPTKQILK----RTGFVTQDDILYPHlTVRETLVFCSllrl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1134 PNASWSEVEEAAKEAYIHNFicGLPRGYETEVGESGIQ-LSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQD 1212
Cdd:PLN03211 170 PKSLTKQEKILVAESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180
....*....|....*....|.
gi 1770234124 1213 AIRKIIKRTTTIVV-VHRLST 1232
Cdd:PLN03211 248 TLGSLAQKGKTIVTsMHQPSS 268
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
535-613 |
2.29e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 535 TQLSGGQKQRIALARAMIKDPKILLLDEPTSALDpkseslvqqaIDKIS---------KGrTTIVIAHRLATVKNAETII 605
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----------IETIEwlegflktfQG-SIIFISHDRSFIRNMATRI 223
|
....*....
gi 1770234124 606 V-LEQGSVI 613
Cdd:PRK11147 224 VdLDRGKLV 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1033-1240 |
2.53e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.43 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPsrpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDlDLKWLRLQTA 1112
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1113 LVGQ----EPALfggTIGENIR-----FGNPNASWSE----VEEAAKeayihnficgLPRGYETEVGEsgiqLSGGQKQR 1179
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLvfgryFGLSAAAARAlvppLLEFAK----------LENKADAKVGE----LSGGMKRR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1180 IAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-----------HRLSTIKKANAIA 1240
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTthfmeeaerlcDRLCVIEEGRKIA 218
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
717-972 |
2.74e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 54.02 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 717 VIFGMLAGAILSLFPLVLGQALTVYFNP-DKSKLQKDVGYLCLALVGLGFGCILTMMgqqgFCGWAGTKLTKRVRDLLFR 795
Cdd:cd18540 8 IILMLLVALLDAVFPLLTKYAIDHFITPgTLDGLTGFILLYLGLILIQALSVFLFIR----LAGKIEMGVSYDLRKKAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 796 SILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPFTLGASYF 875
Cdd:cd18540 84 HLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 876 --SLIIN-------IGSKLdndsfdkaSGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQ 946
Cdd:cd18540 162 fqKKILKayrkvrkINSRI--------TGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVL 233
|
250 260
....*....|....*....|....*.
gi 1770234124 947 GAMYSAYTLVLFFGAYLVKKDYTKFG 972
Cdd:cd18540 234 FLGSIATALVLWYGGILVLAGAITIG 259
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1171-1251 |
2.97e-07 |
|
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: 53.52 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1171 QLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKKANAIAVVQNGKVSE 1249
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVeHDLAVLDYLSDYIHCLYGEPGA 218
|
..
gi 1770234124 1250 YG 1251
Cdd:cd03236 219 YG 220
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
726-964 |
3.19e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 53.74 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 726 ILSL-FPLVLgqaLTVYfnpDKSKLQKDVGYLCLALVGLGFGCILTM---MGQQGFCGWAGTKLTKRVRDLLFRSILNQE 801
Cdd:cd18566 16 ILALaTPLFI---LQVY---DRVIPNESIPTLQVLVIGVVIAILLESllrLLRSYILAWIGARFDHRLSNAAFEHLLSLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 802 PGWFDSdqNSPGSLVSKLsvncTSFRSI---LGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLativtPFTLGASYFSLI 878
Cdd:cd18566 90 LSFFER--EPSGAHLERL----NSLEQIrefLTGQALLALLDLPFVLIFLGLIWYLGGKLVLV-----PLVLLGLFVLVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 879 INIGSKLDNDSfdKASGIASA--------AVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMY 950
Cdd:cd18566 159 ILLGPILRRAL--KERSRADErrqnflieTLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQ 236
|
250
....*....|....
gi 1770234124 951 SAYTLVLFFGAYLV 964
Cdd:cd18566 237 VSMVAVVAFGALLV 250
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1046-1271 |
3.37e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.16 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1046 PDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDP----IGGKVMMGGRDLRDLDLKwlRLQTALVGQEP-AL 1120
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--GRKIATIMQNPrSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1121 FGG--TIGENIR-----FGNP--NASWSEVEEAAkeayihnficGLPRGyETEVGESGIQLSGGQKQRIAIARAIVKKSK 1191
Cdd:PRK10418 92 FNPlhTMHTHARetclaLGKPadDATLTAALEAV----------GLENA-ARVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1192 VLLLDEATSALDLESEKHVQDAIRKIIKR--------TTTIVVVHRLstikkANAIAVVQNGKVSEYGTHDTLLTNHSNG 1263
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKralgmllvTHDMGVVARL-----ADDVAVMSHGRIVEQGDVETLFNAPKHA 235
|
....*...
gi 1770234124 1264 VYATLVHS 1271
Cdd:PRK10418 236 VTRSLVSA 243
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
431-615 |
3.38e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.64 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 431 LVGASGAGKS----TIFALLErfydPNKGLILLDGQDIRTLQVK-WLRSQMGMV-------GqepvLFAD-TILENILM- 496
Cdd:COG1129 283 IAGLVGAGRTelarALFGADP----ADSGEIRLDGKPVRIRSPRdAIRAGIAYVpedrkgeG----LVLDlSIRENITLa 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 497 -------------GKENATKKEAIDaciavnahnficDL---PQGYDTQVGekgtQLSGGQKQRIALARAMIKDPKILLL 560
Cdd:COG1129 355 sldrlsrgglldrRRERALAEEYIK------------RLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 561 DEPTSALDP--KSEslVQQAIDKI-SKGRTTIVI----------AHRlatvknaetIIVLEQGSVIEI 615
Cdd:COG1129 419 DEPTRGIDVgaKAE--IYRLIRELaAEGKAVIVIsselpellglSDR---------ILVMREGRIVGE 475
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
398-595 |
3.72e-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: 55.40 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMSvPILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRTlQVKWLRSQMG 477
Cdd:TIGR01257 1938 LRLNELTKVYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQepvlfADTIlENILMGKEN--------ATKKEAIDACIAVNAHNFicdlpqGYDTQVGEKGTQLSGGQKQRIALAR 549
Cdd:TIGR01257 2016 YCPQ-----FDAI-DDLLTGREHlylyarlrGVPAEEIEKVANWSIQSL------GLSLYADRLAGTYSGGNKRKLSTAI 2083
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1770234124 550 AMIKDPKILLLDEPTSALDPKSESLVQQAI-DKISKGRTTIVIAHRL 595
Cdd:TIGR01257 2084 ALIGCPPLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSM 2130
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
713-964 |
3.73e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 53.67 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 713 LCVGVIFgMLAGAILSLF-PLVLGQAL-TVYFNPDKSKLQKDVGYLCLALVGLGFGCILTMMGQQGFCGWAGTKLTKRVR 790
Cdd:cd18563 1 LILGFLL-MLLGTALGLVpPYLTKILIdDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 791 DLLFRSILNQEPGWFDSdqNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPFTL 870
Cdd:cd18563 80 RDLYEHLQRLSLSFFDK--RQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 871 GASYFsliinIGSKLDN------DSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITG----- 939
Cdd:cd18563 158 WGSYF-----FWKKIRRlfhrqwRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWAtffpl 232
|
250 260
....*....|....*....|....*
gi 1770234124 940 IALGISQGAMysaytLVLFFGAYLV 964
Cdd:cd18563 233 LTFLTSLGTL-----IVWYFGGRQV 252
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
125-371 |
4.69e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 53.26 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 125 ALSGIVVIGAYLQIACWRL---VGERLGHRIRSKYLRAVLRQDVSFFDTDIStSDIMHGISSDVAQIQEVMGDKMSQFIY 201
Cdd:cd18546 44 AYLAVVLAGWVAQRAQTRLtgrTGERLLYDLRLRVFAHLQRLSLDFHERETS-GRIMTRMTSDIDALSELLQTGLVQLVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 202 HIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFCGV--------AYKAVYVGLAAkeVNSYkkagsIAEqAIGSIRTVFSF 273
Cdd:cd18546 123 SLLTLVGIAVVLLVLDPRLALVALAALPPLALATRwfrrrssrAYRRARERIAA--VNAD-----LQE-TLAGIRVVQAF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 274 VAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYSTWALAFWYGSILVSRNELSGGAAIACFfgvtiggrgLAL 353
Cdd:cd18546 195 RRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFL---------LYL 265
|
250 260
....*....|....*....|....*..
gi 1770234124 354 SLSY---------FAQFAQGTVAASKV 371
Cdd:cd18546 266 RRFFapiqqlsqvFDSYQQARAALEKI 292
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1061-1239 |
5.08e-07 |
|
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: 53.00 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1061 GTMVAVVGGSGSGKSTVIW------LMQRFYdpiGGKVMMGGRD----LRDLDlKWLRLQTALVGQEP------------ 1118
Cdd:cd03271 21 GVLTCVTGVSGSGKSSLINdtlypaLARRLH---LKKEQPGNHDriegLEHID-KVIVIDQSPIGRTPrsnpatytgvfd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1119 ---ALF----GGTigeniRFgNP--------NASWSEV-EEAAKEAY--------IHNFI---CGLPRGYETeVGESGIQ 1171
Cdd:cd03271 97 eirELFcevcKGK-----RY-NRetlevrykGKSIADVlDMTVEEALeffenipkIARKLqtlCDVGLGYIK-LGQPATT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1172 LSGGQKQRIAIARAIVKKSK---VLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKKANAI 1239
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLDVIKCADWI 241
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
714-964 |
6.80e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 52.90 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 714 CVGVIFGMLAGAILSL-----FPLVLGQALTVYFNPDKSKLQKDVG--------YLCLALVGL-GFGCILTMMGQQGFcG 779
Cdd:cd18564 1 LALALLALLLETALRLlepwpLKVVIDDVLGDKPLPGLLGLAPLLGpdplalllLAAAALVGIaLLRGLASYAGTYLT-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 780 WAGTKLTKRVRDLLFRSILNQEPGWFDsdQNSPGSLVSKLSVNCTSFRSILGdrySVLFMGLSSAA--VG-LSVSFYLEW 856
Cdd:cd18564 80 LVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLLV---SGVLPLLTNLLtlVGmLGVMFWLDW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 857 RLALLATIVTP-FTLGASYFSLIINIGSKldnDSFDKASGIASAA---VSNIRTVTTLATQEKIVQSFEQSLSKPKSSSI 932
Cdd:cd18564 155 QLALIALAVAPlLLLAARRFSRRIKEASR---EQRRREGALASVAqesLSAIRVVQAFGREEHEERRFARENRKSLRAGL 231
|
250 260 270
....*....|....*....|....*....|..
gi 1770234124 933 KRSQITGIALGISQGAMYSAYTLVLFFGAYLV 964
Cdd:cd18564 232 RAARLQALLSPVVDVLVAVGTALVLWFGAWLV 263
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1033-1256 |
6.86e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSrpdVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLK-WLRLQT 1111
Cdd:PRK11288 5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1112 ALVGQE----PALfggTIGENIRFGN-PN-ASWSEVEEAAKEAYIHNFICGLPRGYETEVGEsgiqLSGGQKQRIAIARA 1185
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQlPHkGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1186 IVKKSKVLLLDEATSALDL-ESEKhvqdaIRKIIKR-----TTTIVVVHRLSTI-KKANAIAVVQNGKVSEygTHDTL 1256
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSArEIEQ-----LFRVIRElraegRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
415-590 |
7.10e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 415 ILNSLN-LVIPSQrISALVGASGAGKSTIF-ALLERFydpNKGLI-----LLDGqdiRTLQVKWLRSqMGMVGQEPV-LF 486
Cdd:TIGR00956 778 ILNNVDgWVKPGT-LTALMGASGAGKTTLLnVLAERV---TTGVItggdrLVNG---RPLDSSFQRS-IGYVQQQDLhLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 487 ADTILENI-----LMGKENATKKEA---IDACIAvnahnfICDLPQGYDTQVGEKGTQLSGGQKQRIALARAMIKDPKIL 558
Cdd:TIGR00956 850 TSTVRESLrfsayLRQPKSVSKSEKmeyVEEVIK------LLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLL 923
|
170 180 190
....*....|....*....|....*....|...
gi 1770234124 559 L-LDEPTSALDPKSESLVQQAIDKISKGRTTIV 590
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKLADHGQAIL 956
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
505-628 |
9.75e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 505 EAIDACIA-VNAHNFICDLPQGYDTQVGEKGTqLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKIS 583
Cdd:PLN03073 313 ELIDAYTAeARAASILAGLSFTPEMQVKATKT-FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP 391
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1770234124 584 KgrTTIVIAHRLATVKNAETIIVLEQGsvieigdhNKLMAQEGAY 628
Cdd:PLN03073 392 K--TFIVVSHAREFLNTVVTDILHLHG--------QKLVTYKGDY 426
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1141-1239 |
9.98e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.86 E-value: 9.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1141 VEEAAK--EAY--IH---NFICGLPRGYeTEVGESGIQLSGGQKQRIAIARAIVKKSK---VLLLDEATSALDLESEKHV 1210
Cdd:TIGR00630 793 VEEAYEffEAVpsISrklQTLCDVGLGY-IRLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDIKKL 871
|
90 100 110
....*....|....*....|....*....|
gi 1770234124 1211 QDAIRKIIKRTTTIVVV-HRLSTIKKANAI 1239
Cdd:TIGR00630 872 LEVLQRLVDKGNTVVVIeHNLDVIKTADYI 901
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
536-596 |
9.99e-07 |
|
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: 51.98 E-value: 9.99e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 536 QLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLA 596
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLA 200
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1054-1258 |
1.01e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.86 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1054 FCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYdPIGGKVMMGGRDLRDLDLKWLRLQTA-LVGQEPALFGGTIGENIRFG 1132
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1133 NPnaswSEVEEAAKEAYIhNFICGLpRGYETEVGESGIQLSGGQKQRIAIA-------RAIVKKSKVLLLDEATSALDLE 1205
Cdd:PRK03695 94 QP----DKTRTEAVASAL-NEVAEA-LGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1206 SEKHVQDAIRKIIKRTTTIVVV-HRLS-TIKKANAIAVVQNGKVSEYGTHDTLLT 1258
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSsHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
144-341 |
1.02e-06 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 52.45 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 144 VGERLGHRIRSKYLRAVLRQDVSFFDTdISTSDImhgIS--SDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVS 221
Cdd:cd18570 69 LSQKLDIRLILGYFKHLLKLPLSFFET-RKTGEI---ISrfNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 222 LAVLAVTPLTMFCGVAYKAVYVGLAAKEVNSYKKAGSIAEQAIGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAK 301
Cdd:cd18570 145 LITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLS 224
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1770234124 302 GIGLGVIYLVTYSTWALAFWYGSILVSRNELSGGAAIACF 341
Cdd:cd18570 225 NLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFN 264
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
536-597 |
1.12e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.25 E-value: 1.12e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 536 QLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLAT 597
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEeGKYVLVVEHDLAI 274
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
402-576 |
1.23e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 402 NVSFAYPSRmsvPIL-NSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILldgqdiRTLQVKwlrsqMGMVG 480
Cdd:PLN03073 513 DASFGYPGG---PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF------RSAKVR-----MAVFS 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 481 QEPVLFADTILENILMgkenatkkeaidaciavNAHNFICDLPQGYDTQVGEKGTQ----------LSGGQKQRIALARA 550
Cdd:PLN03073 579 QHHVDGLDLSSNPLLY-----------------MMRCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSRVAFAKI 641
|
170 180
....*....|....*....|....*..
gi 1770234124 551 MIKDPKILLLDEPTSALDPKS-ESLVQ 576
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1058-1203 |
1.29e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1058 VKGGTMVAVVGGSGSGKSTVIWLM----QRFYDPIGGKVMMGGRDLRDLdLKWLRLQTALVGQEPALFGG-TIGENIRF- 1131
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFPHlTVGETLDFa 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770234124 1132 ------GNPNASWSEVEEAAKEAYIHNFICGLPRGYETEVGESGIQ-LSGGQKQRIAIARAIVKKSKVLLLDEATSALD 1203
Cdd:TIGR00956 163 arcktpQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1056-1259 |
1.33e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.53 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDL-DLKWLRLQTALVGQEPALFGG-TIGENIR--- 1130
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVRTFQHVRLFREmTVIENLLvaq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1131 ------------FGNPNASWSEVEEAAKEAYIHNFIcGLprgyeTEVG--ESGiQLSGGQKQRIAIARAIVKKSKVLLLD 1196
Cdd:PRK11300 106 hqqlktglfsglLKTPAFRRAESEALDRAATWLERV-GL-----LEHAnrQAG-NLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1197 EATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNEhnVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNN 244
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
526-593 |
1.51e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.51e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 526 YDTQVGEkgtqLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAH 593
Cdd:PRK13409 447 LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIaeEREATALVVDH 512
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1171-1230 |
1.63e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.63e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1171 QLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRL 1230
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1041-1259 |
1.73e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 51.05 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1041 AYPSRPdviVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDL-KWLRLQTALVGQEPA 1119
Cdd:PRK10895 12 AYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1120 LFGG-TIGEN------IRfgnPNASWSEVEEAAKEAYIHNFICGLprgyETEVGESgiqLSGGQKQRIAIARAIVKKSKV 1192
Cdd:PRK10895 89 IFRRlSVYDNlmavlqIR---DDLSAEQREDRANELMEEFHIEHL----RDSMGQS---LSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1193 LLLDEATSALDLESekhVQDaIRKIIKRTT-----TIVVVHRL-STIKKANAIAVVQNGKVSEYGTHDTLLTN 1259
Cdd:PRK10895 159 ILLDEPFAGVDPIS---VID-IKRIIEHLRdsglgVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
526-608 |
2.13e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.48 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 526 YDTQVGEkgtqLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKI--SKGRTTIVIAHRLATVKN-AE 602
Cdd:COG1245 449 LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaeNRGKTAMVVDHDIYLIDYiSD 524
|
....*.
gi 1770234124 603 TIIVLE 608
Cdd:COG1245 525 RLMVFE 530
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
536-605 |
2.75e-06 |
|
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: 48.90 E-value: 2.75e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 536 QLSGGQKQRIALARAM----IKDPKILLLDEPTSALDPKSESLVQQAIDKIS-KGRTTIVIAHRLATVKNAETII 605
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
714-974 |
3.05e-06 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 50.86 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 714 CVGVIFGMLAGAILSLF-PLVLGQALtvyfnpDKSKLQKDVGY---LCLALVGLGFGCILTMMGQQGFCGWAGTKLTKRV 789
Cdd:cd18548 1 AILAPLFKLLEVLLELLlPTLMADII------DEGIANGDLSYilrTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 790 RDLLFRSILNQEPGwfDSDQNSPGSLVSKLSVNCTSFRSILGdrySVLFMGLSS---AAVGLSVSFYLEWRLALLATIVT 866
Cdd:cd18548 75 RKDLFEKIQSFSFA--EIDKFGTSSLITRLTNDVTQVQNFVM---MLLRMLVRApimLIGAIIMAFRINPKLALILLVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 867 PFTLGASYFslIINIGSKLdndsF-------DKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITG 939
Cdd:cd18548 150 PILALVVFL--IMKKAIPL----FkkvqkklDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMA 223
|
250 260 270
....*....|....*....|....*....|....*
gi 1770234124 940 IALGISQGAMYSAYTLVLFFGAYLVKKDYTKFGDV 974
Cdd:cd18548 224 LLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDL 258
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
398-568 |
3.55e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAYPSRMsvpILNSLNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLdGQDIrtlqvkwlrsQMG 477
Cdd:PRK11819 325 IEAENLSKSFGDRL---LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 478 MVGQepvlFADTI-------------LENILMGKenatkKEaIDACIAVNAHNFicdlpQGYDTQ--VGekgtQLSGGQK 542
Cdd:PRK11819 391 YVDQ----SRDALdpnktvweeisggLDIIKVGN-----RE-IPSRAYVGRFNF-----KGGDQQkkVG----VLSGGER 451
|
170 180
....*....|....*....|....*.
gi 1770234124 543 QRIALARAMIKDPKILLLDEPTSALD 568
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
537-608 |
3.75e-06 |
|
ATP-binding cassette domain 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 more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.11 E-value: 3.75e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 537 LSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATVKN-AETIIVLE 608
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
419-610 |
4.28e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 419 LNLVIPSQRISALVGASGAGKsTIFAllERFY---DPNKGLILLDGQDIRTLQVKwLRSQMGMV-----GQEPVLFADTI 490
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGR-TELA--ETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 491 LE-NI------LMGKENATKKEAidaciAVnahnficdlPQGYDTQVGEKGTQ-------LSGGQKQRIALARAMIKDPK 556
Cdd:PRK15439 358 LAwNVcalthnRRGFWIKPAREN-----AV---------LERYRRALNIKFNHaeqaartLSGGNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 557 ILLLDEPTSALDPKSESLVQQAIDKISKGRTTIV-IAHRLATV-KNAETIIVLEQG 610
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIeQMADRVLVMHQG 479
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1166-1252 |
4.49e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1166 GESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-----------HRLSTIK 1234
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTtqymeeaeqlaHELTVID 218
|
90
....*....|....*...
gi 1770234124 1235 KANAIAvvqNGKVSEYGT 1252
Cdd:NF000106 219 RGRVIA---DGKVDELKT 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
540-569 |
4.77e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 4.77e-06
10 20 30
....*....|....*....|....*....|
gi 1770234124 540 GQKQRIALARAMIKDPKILLLDEPTSALDP 569
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
537-623 |
5.46e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 537 LSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLATVKN-AETIIVLEQGSV-- 612
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGmSDRILVMHEGRIsg 475
|
90
....*....|....
gi 1770234124 613 ---IEIGDHNKLMA 623
Cdd:PRK10762 476 eftREQATQEKLMA 489
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1171-1232 |
6.34e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.94 E-value: 6.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1171 QLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLST 1232
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVeHDLAI 274
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1056-1251 |
6.49e-06 |
|
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: 50.57 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGK--VMMG---------GRDLRDLDLKWLrlqtALVGQEPALFG-G 1123
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGdewvdmtkpGPDGRGRAKRYI----GILHQEYDLYPhR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 TIGENIrfgNPNASWSEVEEAAKEAYIHNFICGlprGYETEVGESGI-----QLSGGQKQRIAIARAIVKKSKVLLLDEA 1198
Cdd:TIGR03269 381 TVLDNL---TEAIGLELPDELARMKAVITLKMV---GFDEEKAEEILdkypdELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1199 TSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKVSEYG 1251
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIG 510
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1048-1227 |
8.89e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.03 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1048 VIVLREFCLKVKGGTMVAVVGGSGSGKST---VIWLMQRfydPIGGKVMMGGRDLRDLDLKWL-----------RLQTAL 1113
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSElaeALAGLRP---PASGSIRLDGEDITGLSPRERrrlgvayipedRLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1114 VGqepalfGGTIGENI---RFGNPNAS------WSEVEEAAKEAyIHNF-IcgLPRGYETEVGesgiQLSGGQKQRIAIA 1183
Cdd:COG3845 348 VP------DMSVAENLilgRYRRPPFSrggfldRKAIRAFAEEL-IEEFdV--RTPGPDTPAR----SLSGGNQQKVILA 414
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1770234124 1184 RAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV 1227
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLI 458
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
428-594 |
9.15e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.61 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 428 ISALVGASGAGKSTIFALL--ERFYDPNKGLILLDG-----------------QDIRTLQVK---------WLRSQMGMV 479
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGfpkkqetfarisgyceqNDIHSPQVTvresliysaFLRLPKEVS 987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 480 GQEPVLFADTILEniLMGKENAtkKEAIdaciavnahnficdlpqgydtqVGEKG-TQLSGGQKQRIALARAMIKDPKIL 558
Cdd:PLN03140 988 KEEKMMFVDEVME--LVELDNL--KDAI----------------------VGLPGvTGLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190
....*....|....*....|....*....|....*..
gi 1770234124 559 LLDEPTSALDPKSESLVQQAI-DKISKGRTTIVIAHR 594
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQ 1078
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1035-1212 |
9.75e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 9.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1035 FKM--VNFAYPsrPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLM----QRF-------------Y-------DP- 1087
Cdd:TIGR03719 5 YTMnrVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdKDFngearpqpgikvgYlpqepqlDPt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1088 --IGGKVMMGGRDLRDLdLKWLRLQTALVGQEPALFGGTIGENIRFGNPNASW------SEVEEAAkEAYihnficGLPR 1159
Cdd:TIGR03719 83 ktVRENVEEGVAEIKDA-LDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAAdawdldSQLEIAM-DAL------RCPP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1160 GyETEVGEsgiqLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLES----EKHVQD 1212
Cdd:TIGR03719 155 W-DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
536-586 |
9.80e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.51 E-value: 9.80e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 536 QLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISKGR 586
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAER 186
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
715-964 |
1.46e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 48.62 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 715 VGVIFGMLAGAILSLF-PLVLGQALtvyfnpDKSKLQKDVGYL---CLALVGLGFGCILTMMGQQGFCGWAGTKLTKRVR 790
Cdd:cd18545 3 LLALLLMLLSTAASLAgPYLIKIAI------DEYIPNGDLSGLliiALLFLALNLVNWVASRLRIYLMAKVGQRILYDLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 791 DLLFRSILNQEPGWFDSdqNSPGSLVSKLS--VNC------TSFRSILGDRYSVLFMglssaavgLSVSFYLEWRLALLA 862
Cdd:cd18545 77 QDLFSHLQKLSFSFFDS--RPVGKILSRVIndVNSlsdllsNGLINLIPDLLTLVGI--------VIIMFSLNVRLALVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 863 TIVTPFTLGASYFsliinIGSKLdNDSFDKASgIASAAV--------SNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKR 934
Cdd:cd18545 147 LAVLPLLVLVVFL-----LRRRA-RKAWQRVR-KKISNLnaylhesiSGIRVIQSFAREDENEEIFDELNRENRKANMRA 219
|
250 260 270
....*....|....*....|....*....|...
gi 1770234124 935 SQITGI---ALGISQGAmysAYTLVLFFGAYLV 964
Cdd:cd18545 220 VRLNALfwpLVELISAL---GTALVYWYGGKLV 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
535-610 |
1.54e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.54 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 535 TQLSGGQKQRIALARAMIKDPKILLLDEPTSALD--PKSE------SLVQQAIdkiskgrTTIVIAHRLATVKN-AETII 605
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYEiyklinQLVQQGV-------AIIVISSELPEVLGlSDRVL 476
|
....*
gi 1770234124 606 VLEQG 610
Cdd:PRK13549 477 VMHEG 481
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
713-875 |
1.57e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 48.72 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 713 LCVGVIFGMLAgAILSLFP-LVLGQALTVYFNPDKSKLQ--------KDVGYLCLALVGLGFGCILTMMGQQGFCGWAGT 783
Cdd:cd18565 1 LVLGLLASILN-RLFDLAPpLLIGVAIDAVFNGEASFLPlvpaslgpADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 784 KLTKRVRDLL----FRSILNQEPGWFDSDQNspGSLVSKLS--VN------CTSFRSILgdRYSVLFMGLSSaavglsVS 851
Cdd:cd18565 80 RFAQRVQHDLrtdtYDHVQRLDMAFFEDRQT--GDLMSVLNndVNqlerflDDGANSII--RVVVTVLGIGA------IL 149
|
170 180
....*....|....*....|....
gi 1770234124 852 FYLEWRLALLATIVTPFTLGASYF 875
Cdd:cd18565 150 FYLNWQLALVALLPVPLIIAGTYW 173
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
119-285 |
1.76e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 48.30 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 119 LCVLMSALSGIVVigaylQIACWRLVGErlghrIRSKYLRAVLRQDVSFFDtDISTSDIMHGISSDVAQIQEVMGDKMSQ 198
Cdd:cd18778 52 LRALLNFLRIYLN-----HVAEQKVVAD-----LRSDLYDKLQRLSLRYFD-DRQTGDLMSRVINDVANVERLIADGIPQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 199 FIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFCGVAYkAVYVGLAAKEVNsyKKAG---SIAEQAIGSIRTVFSFVA 275
Cdd:cd18778 121 GITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY-SKKVRPRYRKVR--EALGelnALLQDNLSGIREIQAFGR 197
|
170
....*....|
gi 1770234124 276 EDSLAARYDA 285
Cdd:cd18778 198 EEEEAKRFEA 207
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1031-1205 |
1.91e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1031 FDLEfkMVNFAYPsrpDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGgrdlrdldlkwLRLQ 1110
Cdd:PRK11147 320 FEME--NVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-----------TKLE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1111 TALVGQEPALFG--GTIGENIRFGNpnaswSEVEEAAKE----AYIHNFICGlPRGYETEVGesgiQLSGGQKQRIAIAR 1184
Cdd:PRK11147 384 VAYFDQHRAELDpeKTVMDNLAEGK-----QEVMVNGRPrhvlGYLQDFLFH-PKRAMTPVK----ALSGGERNRLLLAR 453
|
170 180
....*....|....*....|.
gi 1770234124 1185 AIVKKSKVLLLDEATSALDLE 1205
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVE 474
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1047-1252 |
2.65e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTV--IWLMQRFYDPIGGKVMMGGRDLRDLD--------------------- 1103
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLskVIAGHPAYKILEGDILFKGESILDLEpeerahlgiflafqypieipg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1104 ---LKWLRL-------QTALVGQEPALFGGTIGENIRFGNPNASWseveeaakeayihnficgLPRgyetEVGESgiqLS 1173
Cdd:CHL00131 99 vsnADFLRLaynskrkFQGLPELDPLEFLEIINEKLKLVGMDPSF------------------LSR----NVNEG---FS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1174 GGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-H--RLSTIKKANAIAVVQNGKVSEY 1250
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILItHyqRLLDYIKPDYVHVMQNGKIIKT 233
|
..
gi 1770234124 1251 GT 1252
Cdd:CHL00131 234 GD 235
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
72-277 |
3.22e-05 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 47.83 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 72 LFLIIIGClgALINGGSQPWYSYLFGNFVNKIALDNDKDQMIKdvreLCVLMSALSGIVVIGAYLQIACWRLVGERLGHR 151
Cdd:cd18549 3 LFFLDLFC--AVLIAALDLVFPLIVRYIIDDLLPSKNLRLILI----IGAILLALYILRTLLNYFVTYWGHVMGARIETD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 152 IRSKYLRAVLRQDVSFFDtDISTSDIMHGISSDVAQIQEVmgdkmsqfiYH---------IFTFICGYIVGFLKSWKVSL 222
Cdd:cd18549 77 MRRDLFEHLQKLSFSFFD-NNKTGQLMSRITNDLFDISEL---------AHhgpedlfisIITIIGSFIILLTINVPLTL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 223 AVLAVTPLTMFCGV--------AYKAVYVGLAakEVNSYkkagsiAEQAIGSIRTVFSFVAED 277
Cdd:cd18549 147 IVFALLPLMIIFTIyfnkkmkkAFRRVREKIG--EINAQ------LEDSLSGIRVVKAFANEE 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1172-1227 |
3.67e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 3.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 1172 LSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV 1227
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILV 451
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
416-605 |
4.13e-05 |
|
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: 46.48 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 416 LNSLNLVIPSQRISALVGASGAGKS-----TIFALLERFYdpnkglilldgqdIRTLQVkwlrsqmgmvgqepvlFADTI 490
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSslafdTIYAEGQRRY-------------VESLSA----------------YARQF 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 491 LENilMGKENATKKEAIDACIAVN----AHN-----------------------------FICDLPQGYDTQVGEKGTqL 537
Cdd:cd03270 62 LGQ--MDKPDVDSIEGLSPAIAIDqkttSRNprstvgtvteiydylrllfarvgirerlgFLVDVGLGYLTLSRSAPT-L 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 538 SGGQKQRIALAR--AMIKDPKILLLDEPTSALDPKSESLVQQAIDKI-SKGRTTIVIAHRLATVKNAETII 605
Cdd:cd03270 139 SGGEAQRIRLATqiGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVEHDEDTIRAADHVI 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1047-1226 |
4.24e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 47.52 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1047 DVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLdlkwLRLQTALVGQEPAL------ 1120
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR----ARLARARIGVVPQFdnldle 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1121 FggTIGEN-IRFGNpnasWSEVEEAAKEAYIHNFI--CGLPRGYETEVGEsgiqLSGGQKQRIAIARAIVKKSKVLLLDE 1197
Cdd:PRK13536 129 F--TVRENlLVFGR----YFGMSTREIEAVIPSLLefARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDE 198
|
170 180
....*....|....*....|....*....
gi 1770234124 1198 ATSALDLESEKHVQDAIRKIIKRTTTIVV 1226
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLARGKTILL 227
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1172-1212 |
4.98e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 4.98e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1770234124 1172 LSGGQKQRIAIARAIVKKSKVLLLDEATSALDLES----EKHVQD 1212
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlEQFLHD 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
397-612 |
5.19e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 397 RLELKNVSFAypsRMSVPIlnslNLVIPSQRISALVGASGAGKSTIFALLERFYDPNKGLILLDGQDIRtlqvkwLRSqm 476
Cdd:PRK11288 257 RLRLDGLKGP---GLREPI----SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRS-- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 477 gmvgqePvlfADTILENILMGKENaTKKEAIDACIAV--------------------------NAHNFICDL----PQGy 526
Cdd:PRK11288 322 ------P---RDAIRAGIMLCPED-RKAEGIIPVHSVadninisarrhhlragclinnrweaeNADRFIRSLniktPSR- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 527 DTQVGekgtQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK-GRTTIVIAHRLATVKN-AETI 604
Cdd:PRK11288 391 EQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAqGVAVLFVSSDLPEVLGvADRI 466
|
....*...
gi 1770234124 605 IVLEQGSV 612
Cdd:PRK11288 467 VVMREGRI 474
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
535-625 |
6.62e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 535 TQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKIS-KGRTTIVIAHRLATVKNA-ETIIVLEQGSV 612
Cdd:PRK09700 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRL 487
|
90
....*....|...
gi 1770234124 613 IEIGDHNKLMAQE 625
Cdd:PRK09700 488 TQILTNRDDMSEE 500
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1171-1292 |
7.50e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1171 QLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKrtTTIVVVHR---LSTIkkANAIAVVQNGKV 1247
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVVSHArefLNTV--VTDILHLHGQKL 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 1248 SEY-GTHDTL-------LTNHS----------------------NGVYATLVHSEMEAnADHFSLVQQPVTDPEF 1292
Cdd:PLN03073 420 VTYkGDYDTFertreeqLKNQQkafesnersrshmqafidkfryNAKRASLVQSRIKA-LDRLGHVDAVVNDPDY 493
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
988-1250 |
1.02e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 988 VGQFAGLAPDTSMASTAIPAVFEIMNRNPLIDGKGKKIEQSKPFD------LEFKMVNFAYPSRPdvIVLREFCLKVKGG 1061
Cdd:PLN03073 458 IDKFRYNAKRASLVQSRIKALDRLGHVDAVVNDPDYKFEFPTPDDrpgppiISFSDASFGYPGGP--LLFKNLNFGIDLD 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1062 TMVAVVGGSGSGKSTVIWLMQRFYDPIGG------KVMMG--------GRDLRDLDLKWLRlqtalvgqepALFGGTIGE 1127
Cdd:PLN03073 536 SRIAMVGPNGIGKSTILKLISGELQPSSGtvfrsaKVRMAvfsqhhvdGLDLSSNPLLYMM----------RCFPGVPEQ 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1128 NIRfgnpnaswseveeaakeAYIHNFicGLprgyeteVGESGIQ----LSGGQKQRIAIARAIVKKSKVLLLDEATSALD 1203
Cdd:PLN03073 606 KLR-----------------AHLGSF--GV-------TGNLALQpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1204 LesekhvqDAIRKIIK-----RTTTIVVVHRLSTIK-KANAIAVVQNGKVSEY 1250
Cdd:PLN03073 660 L-------DAVEALIQglvlfQGGVLMVSHDEHLISgSVDELWVVSEGKVTPF 705
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1033-1214 |
1.18e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 46.47 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1033 LEFKMVNFAYPSRpdvIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMG----------GRDlrDL 1102
Cdd:TIGR03719 323 IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGetvklayvdqSRD--AL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1103 DlkwlrlQTALVGQEPAlfGGTigENIRFGNpnaswsevEEAAKEAYI--HNFicglpRGYETE--VGesgiQLSGGQKQ 1178
Cdd:TIGR03719 398 D------PNKTVWEEIS--GGL--DIIKLGK--------REIPSRAYVgrFNF-----KGSDQQkkVG----QLSGGERN 450
|
170 180 190
....*....|....*....|....*....|....*.
gi 1770234124 1179 RIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAI 1214
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL 486
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
525-605 |
1.22e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 525 GYdTQVGEKGTQLSGGQKQRIALARAMIKDP--KIL-LLDEPTSAL---DPKSESLVQQAIdkISKGRTTIVIAHRLATV 598
Cdd:PRK00349 820 GY-IKLGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLhfeDIRKLLEVLHRL--VDKGNTVVVIEHNLDVI 896
|
....*..
gi 1770234124 599 KNAETII 605
Cdd:PRK00349 897 KTADWII 903
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
421-624 |
1.45e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 421 LVIPSQRIS-----ALVGASGAGKSTIFALLErfydpnKGLILLDGQ---DIRT--------LQ----VKWLRSQMGMVG 480
Cdd:PRK10938 19 LQLPSLTLNagdswAFVGANGSGKSALARALA------GELPLLSGErqsQFSHitrlsfeqLQklvsDEWQRNNTDMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 481 QEPVLFADTILENILMGkenaTKKEAidACIAVNAHNFICDLpqgydtqVGEKGTQLSGGQKQRIALARAMIKDPKILLL 560
Cdd:PRK10938 93 PGEDDTGRTTAEIIQDE----VKDPA--RCEQLAQQFGITAL-------LDRRFKYLSTGETRKTLLCQALMSEPDLLIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 561 DEPTSALDPKSESLVQQAIDKISKGRTTIV-IAHRLATVKN-AETIIVLEQGSVIEIGDHNKLMAQ 624
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
530-611 |
1.56e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 530 VGEKGTQLSGGQKQRIALARAMI---KDPKILLLDEPTSALDPKSESLVQQAIDK-ISKGRTTIVIAHRLATVKNAETII 605
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
....*.
gi 1770234124 606 VLEQGS 611
Cdd:PRK00635 1773 EMGPGS 1778
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
715-964 |
1.61e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 45.55 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 715 VGVIFGMLAGAILSLFPLVLGQAL-TVYFNPDKSKLqkdVGYLcLALVGLGFGCILTMMGQQGFCGWAGTKLTKRVRDLL 793
Cdd:cd18543 3 LALLAALLATLAGLAIPLLTRRAIdGPIAHGDRSAL---WPLV-LLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 794 FRSILNQEPGWFDSDQnsPGSLVSKLSVNCTSFRSILGdRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPFTLGAS 873
Cdd:cd18543 79 FAHLQRLDGAFHDRWQ--SGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 874 Y-FSLIINIGSKLDNDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITG------IAL-GIS 945
Cdd:cd18543 156 RrFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRArfwpllEALpELG 235
|
250
....*....|....*....
gi 1770234124 946 QGAmysaytlVLFFGAYLV 964
Cdd:cd18543 236 LAA-------VLALGGWLV 247
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
537-607 |
1.73e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 537 LSGGQKQRIALARAMI---KDPKILLLDEPTSALDPKS-ESLVQQAIDKISKGRTTIVIAHRLATVKNAETIIVL 607
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1172-1239 |
1.93e-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: 1.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1770234124 1172 LSGGQKQRIAIARAIVKKSK--VLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKKANAI 1239
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIeHNLDVLSSADWI 158
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1172-1258 |
2.11e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1172 LSGGQKQRIAIARAIVKKSKVLLLDEATSALDLES----EKHVQDAirkiikRTTTIVVVHRLSTIKK-ANAIAVVQNGK 1246
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiewlEGFLKTF------QGSIIFISHDRSFIRNmATRIVDLDRGK 230
|
90
....*....|...
gi 1770234124 1247 VSEY-GTHDTLLT 1258
Cdd:PRK11147 231 LVSYpGNYDQYLL 243
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
398-623 |
2.47e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.18 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 398 LELKNVSFAY-PSRMSVPILNSLNLVIPSQRISALVGASGAGKSTIFALL------------ERFYDPNKGLILLDGQDI 464
Cdd:PRK15093 4 LDIRNLTIEFkTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtaDRMRFDDIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 465 RtlqvKWLRSQMGMVGQEPVLFAD-------TILENI--------LMGKENATKKEAIDAC--IAVNAHNficDLPQGYD 527
Cdd:PRK15093 84 R----KLVGHNVSMIFQEPQSCLDpservgrQLMQNIpgwtykgrWWQRFGWRKRRAIELLhrVGIKDHK---DAMRSFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 528 TQvgekgtqLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKISK--GRTTIVIAHRLATV-KNAETI 604
Cdd:PRK15093 157 YE-------LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKI 229
|
250
....*....|....*....
gi 1770234124 605 IVLEQGSVIEIGDHNKLMA 623
Cdd:PRK15093 230 NVLYCGQTVETAPSKELVT 248
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
808-964 |
2.52e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 44.81 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 808 DQNSPGSLVSKLSVNcTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATIVTPFTLGASYFSL-IINIGSKLD 886
Cdd:cd18555 94 ENRSSGDLLFRANSN-VYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRkKIKKLNQEE 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 887 NDSFDKASGIASAAVSNIRTVTTLATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMYSAYTLVLFFGAYLV 964
Cdd:cd18555 173 IVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLV 250
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
827-964 |
2.68e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 44.86 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 827 RSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLA-TIVTPFTLGASYFSLIINigsKLDNDSFDKASGIASA---AVS 902
Cdd:cd18568 112 RRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVlAFIPLYVLLTLLSSPKLK---RNSREIFQANAEQQSFlveALT 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770234124 903 NIRTVTTLATQEKIVQSFEQSLSKpkssSIK---RSQITGIALG-ISQGAMYSAYTLVLFFGAYLV 964
Cdd:cd18568 189 GIATIKALAAERPIRWRWENKFAK----ALNtrfRGQKLSIVLQlISSLINHLGTIAVLWYGAYLV 250
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1170-1253 |
3.25e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1170 IQLSGGQKQRIAIARAI----VKKSKVLLLDEATSALDLESEKHVQDAIRKI-IKRTTTIVVVHRLSTIKKANAIAVVqn 1244
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlVKGAQVIVITHLPELAELADKLIHI-- 153
|
....*....
gi 1770234124 1245 GKVSEYGTH 1253
Cdd:cd03227 154 KKVITGVYK 162
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
535-605 |
3.85e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 3.85e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 535 TQLSGGQKQRIALAraMI-----KDPK-ILLLDEPTSALDPKSESLVQQAIDKISKGRTTIVIAHRLATVKNAETII 605
Cdd:pfam02463 1076 DLLSGGEKTLVALA--LIfaiqkYKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
428-593 |
4.26e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 43.36 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 428 ISALVGASGAGKSTIF-ALLERFY---DPNKGLILLDGQDIRTLQVKwlrsqmgmvGQepvlfADTILENILMGKENATK 503
Cdd:cd03240 24 LTLIVGQNGAGKTTIIeALKYALTgelPPNSKGGAHDPKLIREGEVR---------AQ-----VKLAFENANGKKYTITR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 504 K-EAIDACIavnahnFIcdlPQG-YDTQVGEKGTQLSGGQKQ------RIALARAMIKDPKILLLDEPTSALDP--KSES 573
Cdd:cd03240 90 SlAILENVI------FC---HQGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEenIEES 160
|
170 180
....*....|....*....|..
gi 1770234124 574 LVqQAIDKIS--KGRTTIVIAH 593
Cdd:cd03240 161 LA-EIIEERKsqKNFQLIVITH 181
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
525-625 |
5.40e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 525 GYDTQVGekgtQLSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKIS-KGRTTIVIAHRLATVKN-AE 602
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGiTD 459
|
90 100
....*....|....*....|...
gi 1770234124 603 TIIVLEQGSVIEIGDHNKLMAQE 625
Cdd:PRK10982 460 RILVMSNGLVAGIVDTKTTTQNE 482
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
540-593 |
5.71e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 5.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 540 GQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKisKGRTTIVIAH 593
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISH 210
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
535-605 |
6.82e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.25 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 535 TQLSGGQKQRIALARAMIK---DPKILLLDEPTSAL---DpkseslVQQ---AIDK-ISKGRTTIVIAHRLATVKNAETI 604
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLhfhD------IRKlleVLHRlVDKGNTVVVIEHNLDVIKTADWI 898
|
.
gi 1770234124 605 I 605
Cdd:COG0178 899 I 899
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1044-1246 |
6.86e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1044 SRPDVIVLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLK-WLRLQTALVGQEPALF- 1121
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMVHQELNLVl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1122 GGTIGENIRFGN-PNASW----SEVEEAAKEAYIHNFICGLPRgyetevgESGIQLSGGQKQRIAIARAIVKKSKVLLLD 1196
Cdd:PRK10982 87 QRSVMDNMWLGRyPTKGMfvdqDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1197 EATSALDLESEKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGK 1246
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYIsHKMEEIFQlCDEITILRDGQ 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1171-1262 |
6.88e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.54 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1171 QLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKR--TTTIVVVHRLSTIKK-ANAIAVVQNGKV 1247
Cdd:COG4586 154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErgTTILLTSHDMDDIEAlCDRVIVIDHGRI 233
|
90
....*....|....*
gi 1770234124 1248 SEYGTHDTLLTNHSN 1262
Cdd:COG4586 234 IYDGSLEELKERFGP 248
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
937-1108 |
6.97e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 44.02 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 937 ITGIALGISQGAMYSAYTLVLFFGAYLVKKDY---TKFgdvykIFLILVLSTfSVGQFAGLAPDTSMASTA---IPAVFE 1010
Cdd:COG4615 231 IFALANNWGNLLFFALIGLILFLLPALGWADPavlSGF-----VLVLLFLRG-PLSQLVGALPTLSRANVAlrkIEELEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1011 IMNRNPLIDGKGKKIEQSKPFD-LEFKMVNFAYPSRPDvivLREFC-----LKVKGGTMVAVVGGSGSGKSTVIWLMQRF 1084
Cdd:COG4615 305 ALAAAEPAAADAAAPPAPADFQtLELRGVTYRYPGEDG---DEGFTlgpidLTIRRGELVFIVGGNGSGKSTLAKLLTGL 381
|
170 180
....*....|....*....|....
gi 1770234124 1085 YDPIGGKVMMGGRDLRDLDLKWLR 1108
Cdd:COG4615 382 YRPESGEILLDGQPVTADNREAYR 405
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
537-647 |
8.04e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 537 LSGGQKQRIALARAMIKDPKILLLDEPTSALDPKSESLVQQAIDKIsKGrTTIVIAHRLATVKNAET-IIVLEQGSVIE- 614
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY-QG-TVLLVSHDRQFVDNTVTeCWIFEGNGKIGr 518
|
90 100 110
....*....|....*....|....*....|....
gi 1770234124 615 -IGDHNKLMAQEGAYFSLIKLATEAISSNPVSKK 647
Cdd:PRK11147 519 yVGGYHDARQQQAQYLALKQPAVKKKEEAAAPKA 552
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1056-1277 |
8.43e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.85 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1056 LKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGK--------VMMGGRDLRDL-DLKWLRLQTALVGQEPALFGGTIG 1126
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLvSDEWQRNNTDMLSPGEDDTGRTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1127 ENIRFGNPNASwsEVEEAAKEAYIHNFicgLPRGYetevgesgIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLES 1206
Cdd:PRK10938 104 EIIQDEVKDPA--RCEQLAQQFGITAL---LDRRF--------KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1207 EKHVQDAIRKIIKRTTTIV-VVHRLSTIKK-ANAIAVVQNGKVSEYGTHDTLLtnhSNGVYATLVHSEMEANA 1277
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL---QQALVAQLAHSEQLEGV 240
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
836-964 |
8.75e-04 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 43.26 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 836 VLFMGlssaaVGLSVSFYLEWRLALLATIVTPFTLGasyFSLIIN-IGSKLDNDSFDKASgIASA----AVSNIRTVTTL 910
Cdd:cd18588 126 LVFSV-----VFLAVMFYYSPTLTLIVLASLPLYAL---LSLLVTpILRRRLEEKFQRGA-ENQSflveTVTGIETVKSL 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1770234124 911 ATQEKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMYSAYTLVLFFGAYLV 964
Cdd:cd18588 197 AVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLV 250
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1068-1236 |
9.67e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.17 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1068 GGSGSGKSTVIWLMQRFYDPIGGKVMMGGRDLRDLDLKWLrlqtALVGQEPAL-FGGTIGENIRFgnpnasWSEVEEAAK 1146
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----TYIGHNLGLkLEMTVFENLKF------WSEIYNSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1147 EAY--IHNFicglprGYETEVGESGIQLSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIrkIIKRTTTI 1224
Cdd:PRK13541 103 TLYaaIHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI--VMKANSGG 174
|
170
....*....|....*
gi 1770234124 1225 VVV---HRLSTIKKA 1236
Cdd:PRK13541 175 IVLlssHLESSIKSA 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1124-1248 |
1.32e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.08 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1124 TIGENI---------RFG--NPNAswsevEEAAKEAYIHNFicGL-PRGYETEVGesgiQLSGGQKQRIAIARAIVKKSK 1191
Cdd:COG1129 346 SIRENItlasldrlsRGGllDRRR-----ERALAEEYIKRL--RIkTPSPEQPVG----NLSGGNQQKVVLAKWLATDPK 414
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1192 VLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVV-----------HRlstikkanaIAVVQNGKVS 1248
Cdd:COG1129 415 VLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVIsselpellglsDR---------ILVMREGRIV 473
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1050-1217 |
1.82e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 42.02 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1050 VLREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMMGGRdlrdldlkwlrLQTALVGQEPAL---FGGTIG 1126
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-----------LRIGYVPQKLYLdttLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1127 ENIRFgNPNASWSEVEEAAKEAYIHNFIcglprgyetevgESGIQ-LSGGQKQRIAIARAIVKKSKVLLLDEATSALDLE 1205
Cdd:PRK09544 88 RFLRL-RPGTKKEDILPALKRVQAGHLI------------DAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170
....*....|..
gi 1770234124 1206 SEKHVQDAIRKI 1217
Cdd:PRK09544 155 GQVALYDLIDQL 166
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
72-238 |
1.88e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 42.11 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 72 LFLIIIGCLGALINGGSQPWYSYLFGNFVNKIALDNDKdqmikdvrELCVLMSALSGIVVIGAYLQIACWRLVGERLGHR 151
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGY--------YLGVYAALLVLASVLLVLLRWLLFVLAGLRASRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 152 IRSKYLRAVLRQDVSFFDTdISTSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVgflkswkVSLAVLAVTPLT 231
Cdd:cd18580 74 LHDKLLRSVLRAPMSFFDT-TPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIV-------IAIVSPYFLIVL 145
|
....*..
gi 1770234124 232 MFCGVAY 238
Cdd:cd18580 146 PPLLVVY 152
|
|
| R-SNARE_VAMP4 |
cd15869 |
SNARE motif of VAMP4; The VAMP-4 (vesicle-associated membrane protein 4) protein belongs to ... |
1470-1527 |
1.98e-03 |
|
SNARE motif of VAMP4; The VAMP-4 (vesicle-associated membrane protein 4) protein belongs to the R-SNARE subgroup of SNAREs and interacts with syntaxin 16 (Qa), Vti1a (Qb) and syntaxin 6 (Qc). This complex plays a role in maintenance of Golgi ribbon structure and normal retrograde trafficking from the early endosome to the trans-Golgi network (TGN). SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins contain coiled-coil helices (called SNARE motifs) which mediate the interactions between SNARE proteins, and a transmembrane domain. The SNARE complex mediates membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, depending on whether the residue in the hydrophilic center layer of the four-helical bundle is a glutamine (Q) or arginine (R). Qa-, as well as Qb- and Qc-SNAREs, are localized to target organelle membranes, while R-SNARE is localized to vesicle membranes. They form unique complexes consisting of one member of each subgroup, that mediate fusion between a specific type of vesicles and their target organelle. Their SNARE motifs form twisted and parallel heterotetrameric helix bundles.
Pssm-ID: 277222 [Multi-domain] Cd Length: 67 Bit Score: 38.14 E-value: 1.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1770234124 1470 RNISKLNDELYEVHQIMTRNVQEVLGVGEKLDQVSQMSSRLTSESRIYADKARDLNRQ 1527
Cdd:cd15869 2 DKIRRVQNQVDEVVDVMQDNITKVIDRGEKLEDLQDKSESLSDNASAFRSRSKQLRRK 59
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1172-1239 |
2.57e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 40.91 E-value: 2.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770234124 1172 LSGGQKQRIAIAR--AI--VKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLSTIKKANAI 1239
Cdd:cd03278 114 LSGGEKALTALALlfAIfrVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRL 185
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
530-568 |
2.90e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 2.90e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1770234124 530 VGEKGTQLSGGQKQRIALARAMIKDPKILLLDEPTSALD 568
Cdd:NF040905 398 VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
121-339 |
3.57e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 41.42 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 121 VLMSALSGIVVIGAYLQIACWRLVGERLGHRIRSKYLRAVLRQDVSFFDTDiSTSDIMHGISsDVAQIQEVMGDKM-SQF 199
Cdd:cd18782 46 VVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKR-PVGELSTRIS-ELDTIRGFLTGTAlTTL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 200 IYHIFTFIcgYI-VGFLKSWKVSLAVLAVTPL----TMFCGVAYKAVYVGLAAkevnSYKKAGSIAEQAIGSIRTVFSFV 274
Cdd:cd18782 124 LDVLFSVI--YIaVLFSYSPLLTLVVLATVPLqlllTFLFGPILRRQIRRRAE----ASAKTQSYLVESLTGIQTVKAQN 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770234124 275 AEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYSTWALAFWYGSILVSRNELSGGAAIA 339
Cdd:cd18782 198 AELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIA 262
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
99-361 |
3.68e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 41.31 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 99 FVNKIALDN-----DKDQMIKDVrelcVLMSALSGIVVIGAYLQIACWRLVGERLGHRIRSKYLRAVLRQDVSFFDTDiS 173
Cdd:cd18540 23 LLTKYAIDHfitpgTLDGLTGFI----LLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKT-P 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 174 TSDIMHGISSDVAQIQEVMGDKMSQFIYHIFTFICGYIVGFLKSWKVSLAVLAVTPLTMFCGV--------AYKAVyvgl 245
Cdd:cd18540 98 VGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIyfqkkilkAYRKV---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 246 aaKEVNSyKKAGSIAEqAIGSIRTVFSFVAEDSLAARYDAVLDE----SVpigkKLGFAKGIGLGVIYLVTYSTWALAFW 321
Cdd:cd18540 174 --RKINS-RITGAFNE-GITGAKTTKTLVREEKNLREFKELTEEmrraSV----RAARLSALFLPIVLFLGSIATALVLW 245
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1770234124 322 YGSILVSRNelsggaaiacffGVTIGgrGLALSLSYFAQF 361
Cdd:cd18540 246 YGGILVLAG------------AITIG--TLVAFISYATQF 271
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1171-1258 |
3.95e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.33 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1171 QLSGGQKQRIAIARAIVKKSKVLLLDEATSALdlesEKHVQDAIRKIIKR------TTTIVVVHRLSTIKK-ANAIAVVQ 1243
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAM----EPTTQAQIFRLLTRlnqnnnTTILLISHDLQMLSQwADKINVLY 233
|
90
....*....|....*
gi 1770234124 1244 NGKVSEYGTHDTLLT 1258
Cdd:PRK15093 234 CGQTVETAPSKELVT 248
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
713-964 |
4.83e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 40.94 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 713 LCVGVIFGMLAGAILSLFPLVLGQALtvyfnpDKSKLQKDVGYLcLALVGLGFGCILTmmgqQGFCGWAGTKLTKRV--- 789
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGI------DSGVRAGDLGVL-LLAAAAYLAVVLA----GWVAQRAQTRLTGRTger 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 790 -----RDLLFRSILNQEPGWFDSdqNSPGSLVSKLSVNCTSFRSILGDRYSVLFMGLSSAAVGLSVSFYLEWRLALLATI 864
Cdd:cd18546 70 llydlRLRVFAHLQRLSLDFHER--ETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 865 VTPFTLGASYFsliinigskldndsFDKASGIA-------SAAV--------SNIRTVTTLATQEKIVQSFEQSlskpkS 929
Cdd:cd18546 148 ALPPLALATRW--------------FRRRSSRAyrrarerIAAVnadlqetlAGIRVVQAFRRERRNAERFAEL-----S 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1770234124 930 SSIKRSQITGI-ALGISQGAMY----SAYTLVLFFGAYLV 964
Cdd:cd18546 209 DDYRDARLRAQrLVAIYFPGVEllgnLATAAVLLVGAWRV 248
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
119-340 |
5.12e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 40.64 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 119 LCVLMSALSGIVVIGAYLQIACWRLV---GERLGHRIRSKYLRAVLRQDVSFFDTDistsdimhGISSDVAQIQEVmgDK 195
Cdd:cd18566 41 LQVLVIGVVIAILLESLLRLLRSYILawiGARFDHRLSNAAFEHLLSLPLSFFERE--------PSGAHLERLNSL--EQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 196 MSQF---------IYHIFTFICGYIVGFLKSWkvslavLAVTPLTMFcgvaykAVYVGLAAKEVNSYKKAGSIAEQA--- 263
Cdd:cd18566 111 IREFltgqallalLDLPFVLIFLGLIWYLGGK------LVLVPLVLL------GLFVLVAILLGPILRRALKERSRAder 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 264 --------IGSIRTVFSFVAEDSLAARYDAVLDESVPIGKKLGFAKGIGLGVIYLVTYSTWALAFWYGSILVSRNELSGG 335
Cdd:cd18566 179 rqnflietLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVG 258
|
....*
gi 1770234124 336 AAIAC 340
Cdd:cd18566 259 ALIAC 263
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1154-1258 |
5.55e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.37 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1154 ICGLPRGYETEVGESGIQ-LSGGQKQRIAIARAIVKKSKVLLLDEATSALDLESEKHVQDAIRKIIKRTTTIVVVHRLS- 1231
Cdd:PLN03140 318 ILGLDICKDTIVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQp 397
|
90 100 110
....*....|....*....|....*....|
gi 1770234124 1232 ---TIKKANAIAVVQNGKVSEYGTHDTLLT 1258
Cdd:PLN03140 398 apeTFDLFDDIILLSEGQIVYQGPRDHILE 427
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1171-1239 |
5.98e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 5.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770234124 1171 QLSGGQKQRIAIA--RAI--VKKSKVLLLDEATSALDlesEKHVQdAIRKIIKRTTT----IVVVHRLSTIKKANAI 1239
Cdd:pfam02463 1077 LLSGGEKTLVALAliFAIqkYKPAPFYLLDEIDAALD---DQNVS-RVANLLKELSKnaqfIVISLREEMLEKADKL 1149
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1125-1227 |
6.29e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.07 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1125 IGENI------RFgnpnASWSEVEEAAKEAYIHNFICGLPrgYETEVGESGI-QLSGGQKQRIAIARAIVKKSKVLLLDE 1197
Cdd:PRK13549 358 VGKNItlaaldRF----TGGSRIDDAAELKTILESIQRLK--VKTASPELAIaRLSGGNQQKAVLAKCLLLNPKILILDE 431
|
90 100 110
....*....|....*....|....*....|
gi 1770234124 1198 ATSALDLESEKHVQDAIRKIIKRTTTIVVV 1227
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1051-1257 |
7.06e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.18 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1051 LREFCLKVKGGTMVAVVGGSGSGKSTVIWLMQRFYDPIGGKVMmggrdlRDLDLKWLRLQTALVGQEPALfggtigENIR 1130
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD------RNGEVSVIAISAGLSGQLTGI------ENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 1131 FGNPNASWSEVEEAAKEAYIHNFicglprgyeTEVGESGIQ----LSGGQKQRIAIARAIVKKSKVLLLDEATSALDLES 1206
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEF---------SELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1770234124 1207 EKHVQDAIRKIIKRTTTIVVV-HRLSTIKK-ANAIAVVQNGKVSEYGTHDTLL 1257
Cdd:PRK13546 179 AQKCLDKIYEFKEQNKTIFFVsHNLGQVRQfCTKIAWIEGGKLKDYGELDDVL 231
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
837-1005 |
9.54e-03 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 39.74 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 837 LFMGLSSAAVGLSVSFYLEWRLALLATIVTPFTLGASYFSLIINIgsKLDNDSFDKASGIASAAV---SNIRTVTTLATQ 913
Cdd:cd18570 122 LFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFK--KKNREVMESNAELNSYLIeslKGIETIKSLNAE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770234124 914 EKIVQSFEQSLSKPKSSSIKRSQITGIALGISQGAMYSAYTLVLFFGAYLVKKDYTKFGDVYKIFLILVLSTFSVGQFAG 993
Cdd:cd18570 200 EQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLIN 279
|
170
....*....|..
gi 1770234124 994 LAPDTSMASTAI 1005
Cdd:cd18570 280 LQPKIQEAKVAA 291
|
|
| |
