|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
57-638 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 586.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 57 FGRVFALAKPDAGKLVIGTIALLIGSTTNLLVPKFGGMIIDIVSRdvKTPEQQTESLIAVrnavviILLIVVIGSICTAL 136
Cdd:COG1132 9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLA--GGDLSALLLLLLL------LLGLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 137 RAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSS 216
Cdd:COG1132 81 QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 217 WKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQ 296
Cdd:COG1132 161 WRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 297 AVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRVFQILDR 376
Cdd:COG1132 241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 377 VSSMSSSGDKCPVGNPDGDVELNDVWFAYPsrPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKIL 456
Cdd:COG1132 321 PPEIPDPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 457 LNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRL 536
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYG-RPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 537 SGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGT 616
Cdd:COG1132 478 SGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGT 557
|
570 580
....*....|....*....|..
gi 22327455 617 HDELLSLNGIYTNLVKRQLQSS 638
Cdd:COG1132 558 HEELLARGGLYARLYRLQFGEE 579
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
45-631 |
1.54e-173 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 511.19 E-value: 1.54e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 45 LEHGVVEAANVGFgRVFALAKPDAGKLVIGTIALLIGSTTNLLVPKFGGMIIDIVSRDvKTPEqqtesliAVRNAVVIIL 124
Cdd:TIGR00958 138 AEQGQSETADLLF-RLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGD-KGPP-------ALASAIFFMC 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 125 LIVVIGSICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTT 204
Cdd:TIGR00958 209 LLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVM 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 205 ALIGVGFMFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSK 284
Cdd:TIGR00958 289 LLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 285 KVDETLKLGLKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAA 364
Cdd:TIGR00958 369 ALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAV 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 365 GASRRVFQILDRVSSMSSSGDKCPVgNPDGDVELNDVWFAYPSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLI 444
Cdd:TIGR00958 449 GASEKVFEYLDRKPNIPLTGTLAPL-NLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 445 ERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGFDgEASFTDIENAAKMANAHEFIEAFPDK 524
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLT-DTPDEEIMAAAKAANAHDFIMEFPNG 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 525 YNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSlmAGRTVLVIAHRLSTVKTADCVA 604
Cdd:TIGR00958 607 YDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQIL 684
|
570 580
....*....|....*....|....*..
gi 22327455 605 VISDGEVAEKGTHDELLSLNGIYTNLV 631
Cdd:TIGR00958 685 VLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
51-635 |
8.65e-153 |
|
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: 457.76 E-value: 8.65e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 51 EAANVGFGRVFALAKPDAGKLVIGTIALLIGSTTNLLVPKFGGMIIDIVsrdvkTPEQQTESLIAVrnAVVIILLIVVIG 130
Cdd:COG2274 138 GEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRV-----LPNQDLSTLWVL--AIGLLLALLFEG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 131 SIcTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSeDTQIIKNAATTNLSEALRNVTTALIGVG 210
Cdd:COG2274 211 LL-RLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 211 FMFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETL 290
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 291 KLGLKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:COG2274 369 NARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 371 FQILDRVSSMSSSGDKCPVGNPDGDVELNDVWFAYPSRpSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDP 450
Cdd:COG2274 449 DDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 451 LKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVG 530
Cdd:COG2274 528 TSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLG-DPDATDEEIIEAARLAGLHDFIEALPMGYDTVVG 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 531 ERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGE 610
Cdd:COG2274 607 EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGR 686
|
570 580
....*....|....*....|....*
gi 22327455 611 VAEKGTHDELLSLNGIYTNLVKRQL 635
Cdd:COG2274 687 IVEDGTHEELLARKGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
65-635 |
2.58e-149 |
|
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: 444.14 E-value: 2.58e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 65 KPDAGKLVIGTIALLIGSTTNLLVPKFGGMIIDivsrdvktPEQQTESLIAVRNAVVIILLIVVIGSICTALRAWLFNSA 144
Cdd:TIGR02204 14 RPYRGRVLAALVALLITAAATLSLPYAVRLMID--------HGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 145 SERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLAL 224
Cdd:TIGR02204 86 GERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 225 VVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQ-------- 296
Cdd:TIGR02204 166 LAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRirtrallt 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 297 AVLVGLFFGGlnaaftlsVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRVFQILDR 376
Cdd:TIGR02204 246 AIVIVLVFGA--------IVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 377 VSSMS--SSGDKCPVGNPdGDVELNDVWFAYPSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGK 454
Cdd:TIGR02204 318 EPDIKapAHPKTLPVPLR-GEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 455 ILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGL 534
Cdd:TIGR02204 397 ILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG-RPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 535 RLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEK 614
Cdd:TIGR02204 476 TLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQ 555
|
570 580
....*....|....*....|.
gi 22327455 615 GTHDELLSLNGIYTNLVKRQL 635
Cdd:TIGR02204 556 GTHAELIAKGGLYARLARLQF 576
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
396-634 |
1.63e-132 |
|
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: 388.44 E-value: 1.63e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPS 555
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYG-KPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 556 VLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLSLNGIYTNLVKRQ 634
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
74-370 |
8.61e-127 |
|
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: 376.21 E-value: 8.61e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 74 GTIALLIGSTTNLLVPKFGGMIIDIVSRDVKtpEQQTESLIAVRNAVVIILLIVVIGSICTALRAWLFNSASERVVARLR 153
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSG--SGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 154 KDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVISVA 233
Cdd:cd18780 79 KRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 234 VKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAAFTL 313
Cdd:cd18780 159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 314 SVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:cd18780 239 AIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
132-635 |
1.52e-116 |
|
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: 359.80 E-value: 1.52e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 132 ICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGF 211
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 212 MFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLK 291
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 292 LGLKQAVLVGLF--FGGLNAAFTLSVITVVSygAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRR 369
Cdd:TIGR02203 229 LAMKMTSAGSISspITQLIASLALAVVLFIA--LFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAES 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 370 VFQILDrvSSMSSSGDKCPVGNPDGDVELNDVWFAYPSRpSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYD 449
Cdd:TIGR02203 307 LFTLLD--SPPEKDTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 450 PLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGFDGEASFTDIENAAKMANAHEFIEAFPDKYNTVV 529
Cdd:TIGR02203 384 PDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPI 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 530 GERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDG 609
Cdd:TIGR02203 464 GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDG 543
|
490 500
....*....|....*....|....*.
gi 22327455 610 EVAEKGTHDELLSLNGIYTNLVKRQL 635
Cdd:TIGR02203 544 RIVERGTHNELLARNGLYAQLHNMQF 569
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
396-630 |
7.56e-111 |
|
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: 332.66 E-value: 7.56e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPSHmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILFNCSVEENIAYGFDGeASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPS 555
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPG-ATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 556 VLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLSLNGIYTNL 630
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
268-644 |
1.12e-109 |
|
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: 342.96 E-value: 1.12e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 268 TVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVG 347
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLY 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 348 SSVSSLSSLYTTaMKAAGAS-RRVFQILDRVSSMSSSGDKCPVGNPDGDVELNDVWFAY-PSRPshmILKGISLRLTPGS 425
Cdd:COG5265 310 IPLNFLGFVYRE-IRQALADmERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYdPERP---ILKGVSFEVPAGK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 426 KVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGFDGeASFTDI 505
Cdd:COG5265 386 TVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPD-ASEEEV 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 506 ENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGR 585
Cdd:COG5265 465 EAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR 544
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 586 TVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLSLNGIYTNLVKRQLQSSSSVTTL 644
Cdd:COG5265 545 TTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEAL 603
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
145-635 |
1.61e-108 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 339.30 E-value: 1.61e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 145 SERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAAttnlSEALRNVT---TALIGV-GFMFTSSWKLT 220
Cdd:PRK11176 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSS----SGALITVVregASIIGLfIMMFYYSWQLS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 221 LLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEE---------SFGA--VRTVRsFAKESYMVSQYSkkvdet 289
Cdd:PRK11176 169 LILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQmlkghkevlIFGGqeVETKR-FDKVSNRMRQQG------ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 290 LKLGLKQAVLVGL--FFGGLNAAFTLSVITVVSYGAYLTIyGSMTVgALTSFI-----LYSLTvgssvsSLSSLYTTAMk 362
Cdd:PRK11176 242 MKMVSASSISDPIiqLIASLALAFVLYAASFPSVMDTLTA-GTITV-VFSSMIalmrpLKSLT------NVNAQFQRGM- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 363 aaGASRRVFQILDrvssMSSSGD--KCPVGNPDGDVELNDVWFAYPSRpSHMILKGISLRLTPGSKVALVGPSGGGKTTI 440
Cdd:PRK11176 313 --AACQTLFAILD----LEQEKDegKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTI 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 441 ANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGFDGEASFTDIENAAKMANAHEFIEA 520
Cdd:PRK11176 386 ANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINK 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 521 FPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTA 600
Cdd:PRK11176 466 MDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKA 545
|
490 500 510
....*....|....*....|....*....|....*
gi 22327455 601 DCVAVISDGEVAEKGTHDELLSLNGIYTNLVKRQL 635
Cdd:PRK11176 546 DEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQF 580
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
396-634 |
2.58e-105 |
|
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: 318.79 E-value: 2.58e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPsrPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPS 555
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 556 VLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLSLNGIYTNLVKRQ 634
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
132-625 |
2.04e-100 |
|
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: 317.47 E-value: 2.04e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 132 ICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEdtQIiknaattnlsEALRN---------- 201
Cdd:COG4988 73 LLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTE--GV----------EALDGyfarylpqlf 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 202 ---VTTALIgVGFMFTSSWK--LTLL----------ALVVVPVISVAVKQFGRYLReLSH---------TTQAaaavaas 257
Cdd:COG4988 141 laaLVPLLI-LVAVFPLDWLsgLILLvtapliplfmILVGKGAAKASRRQWRALAR-LSGhfldrlrglTTLK------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 258 iaeeSFGAV-RTVRSFAKESymvSQYSKKVDETLKLglkqAVLVGLFfggLNAAFTLSVITVVSYGAYLTIYGSMTV-GA 335
Cdd:COG4988 212 ----LFGRAkAEAERIAEAS---EDFRKRTMKVLRV----AFLSSAV---LEFFASLSIALVAVYIGFRLLGGSLTLfAA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 336 LTSFIL---YSL---TVGSSvsslsslYTTAMKAAGASRRVFQILDRVSSMSSSGDKCPVGNPDGDVELNDVWFAYPSRP 409
Cdd:COG4988 278 LFVLLLapeFFLplrDLGSF-------YHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 410 ShmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVE 489
Cdd:COG4988 351 P--ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 490 ENIAYGfDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAE 569
Cdd:COG4988 429 ENLRLG-RPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAE 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 570 SEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLSLNG 625
Cdd:COG4988 508 TEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
394-625 |
3.58e-97 |
|
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: 297.21 E-value: 3.58e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 394 GDVELNDVWFAYpsRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQ 473
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 474 ISIVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTN 553
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327455 554 PSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLSLNG 625
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
134-634 |
1.76e-94 |
|
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: 305.90 E-value: 1.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 134 TALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQI---IKNAATTNLSEALrnVTTALIGVg 210
Cdd:TIGR01846 196 GGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRELEQIrnfLTGSALTVVLDLL--FVVVFLAV- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 211 fMFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETL 290
Cdd:TIGR01846 273 -MFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 291 KLGLKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:TIGR01846 352 AASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 371 FQILDRVSSMSSSGdKCPVGNPDGDVELNDVWFAY-PSRPShmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYD 449
Cdd:TIGR01846 432 GDILNSPTEPRSAG-LAALPELRGAITFENIRFRYaPDSPE--VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYT 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 450 PLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHEFIEAFPDKYNTVV 529
Cdd:TIGR01846 509 PQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALC-NPGAPFEHVIHAAKLAGAHDFISELPQGYNTEV 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 530 GERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDG 609
Cdd:TIGR01846 588 GEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKG 667
|
490 500
....*....|....*....|....*
gi 22327455 610 EVAEKGTHDELLSLNGIYTNLVKRQ 634
Cdd:TIGR01846 668 QIAESGRHEELLALQGLYARLWQQQ 692
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
306-634 |
3.07e-90 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 291.48 E-value: 3.07e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 306 GLN-AAFTLSVITVVSYGAYLTIYGSMTVGALTSFI-LYSLTVGSSVSSLSSLYTTAMKAAGAsRRVFQILDRVSSMSSS 383
Cdd:PRK13657 244 VLNrAASTITMLAILVLGAALVQKGQLRVGEVVAFVgFATLLIGRLDQVVAFINQVFMAAPKL-EEFFEVEDAVPDVRDP 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 384 GDKCPVGNPDGDVELNDVWFAYP-SRPShmiLKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSL 462
Cdd:PRK13657 323 PGAIDLGRVKGAVEFDDVSFSYDnSRQG---VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 463 MEISHQYLHKQISIVSQEPILFNCSVEENIAYGFDGeASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQ 542
Cdd:PRK13657 400 RTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD-ATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQ 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 543 RIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVA 558
|
330
....*....|..
gi 22327455 623 LNGIYTNLVKRQ 634
Cdd:PRK13657 559 RGGRFAALLRAQ 570
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
74-370 |
5.89e-90 |
|
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: 280.99 E-value: 5.89e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 74 GTIALLIGSTTNLLVPKFGGMIIDIVSRdvktpeqqTESLIAVRNAVVIILLIVVIGSICTALRAWLFNSASERVVARLR 153
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIK--------GGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 154 KDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVISVA 233
Cdd:cd18557 73 RDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 234 VKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAAFTL 313
Cdd:cd18557 153 SKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 314 SVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:cd18557 233 SLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
147-633 |
1.87e-88 |
|
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: 286.28 E-value: 1.87e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 147 RVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTqiiknaattnlsEALRN---------VTTALIGVGFMFTSSW 217
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV------------DALDNlylrvllplLVALLVILAAVAFLAF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 218 KLTLLALVVVPV-----------ISVAVKQFGRYLRELSHTTQAAAAvaasiaeESFGAVRTVRSFAKESYMVSQYSKKV 286
Cdd:COG4987 153 FSPALALVLALGlllaglllpllAARLGRRAGRRLAAARAALRARLT-------DLLQGAAELAAYGALDRALARLDAAE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 287 DETLKLGLKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGA 366
Cdd:COG4987 226 ARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 367 SRRVFQILDRVSSMSSSGDKcPVGNPDGDVELNDVWFAYPSRPsHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIER 446
Cdd:COG4987 306 ARRLNELLDAPPAVTEPAEP-APAPGGPSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 447 FYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHEFIEAFPDKYN 526
Cdd:COG4987 384 FLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLA-RPDATDEELWAALERVGLGDWLAALPDGLD 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 527 TVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVI 606
Cdd:COG4987 463 TWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVL 542
|
490 500
....*....|....*....|....*..
gi 22327455 607 SDGEVAEKGTHDELLSLNGIYTNLVKR 633
Cdd:COG4987 543 EDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
393-611 |
8.11e-87 |
|
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: 270.50 E-value: 8.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 393 DGDVELNDVWFAYPSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHK 472
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 QISIVSQEPILFNCSVEENIAYGFdGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLT 552
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGL-QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 553 NPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEV 611
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
396-634 |
6.14e-86 |
|
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: 268.59 E-value: 6.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAY-PSRPshMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQI 474
Cdd:cd03252 1 ITFEHVRFRYkPDGP--VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 475 SIVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNP 554
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALA-DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 555 SVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLSLNGIYTNLVKRQ 634
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
74-370 |
1.43e-82 |
|
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: 262.07 E-value: 1.43e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 74 GTIALLIGSTTNLLVPKFGGMIIDIVSRDVKTPEQQTESLiavRNAVVIILLIVVIGSICTALRAWLFNSASERVVARLR 153
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSL---KTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 154 KDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVISVA 233
Cdd:cd18573 78 KRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 234 VKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAAFTL 313
Cdd:cd18573 158 AVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 314 SVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:cd18573 238 SLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
396-610 |
2.99e-81 |
|
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: 253.84 E-value: 2.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPsHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILFNCSVEENIaygfdgeasftdienaakmanahefieafpdkyntvvgerglrLSGGQKQRIAIARALLTNPS 555
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 556 VLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGE 610
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
76-634 |
8.85e-80 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 263.50 E-value: 8.85e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 76 IALLIGSTTNLLVPKFGGMIIDIVSRDVKTPEQ-----QTESLIAVrnavviillivvigsICTALR----AWLFnSASE 146
Cdd:PRK10789 2 ALLIIIAMLQLIPPKVVGIIVDGVTEQHMTTGQilmwiGTMVLIAV---------------VVYLLRyvwrVLLF-GASY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 147 RVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAA---TTNLSEALRNVTTALIgvgFMFTS-SWKLTLL 222
Cdd:PRK10789 66 QLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAgegVLTLVDSLVMGCAVLI---VMSTQiSWQLTLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 223 ALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGL 302
Cdd:PRK10789 143 ALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDAR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 303 FFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRVFQILDRVSSMSS 382
Cdd:PRK10789 223 FDPTIYIAIGMANLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 383 SGDKCPVGNPDGDVELNDvwFAYPSRpSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSL 462
Cdd:PRK10789 303 GSEPVPEGRGELDVNIRQ--FTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 463 MEISHQYLHKQISIVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQ 542
Cdd:PRK10789 380 TKLQLDSWRSRLAVVSQTPFLFSDTVANNIALG-RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQ 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 543 RIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK10789 459 RISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
570
....*....|..
gi 22327455 623 LNGIYTNLVKRQ 634
Cdd:PRK10789 539 QSGWYRDMYRYQ 550
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
63-632 |
1.02e-76 |
|
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: 258.72 E-value: 1.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 63 LAKPDAGKLVIGTIalLIGSTTNLLVPKFGGMIIDIVSRDVKTPEQQTeSLIAVRNAVviillivvigSICTALRawlfn 142
Cdd:TIGR03796 171 LVIPAFSQIFVDEI--LVQGRQDWLRPLLLGMGLTALLQGVLTWLQLY-YLRRLEIKL----------AVGMSAR----- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 143 saservvarlrkdLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTnLSEALRNVTTALIGVGFMFTSSWKLTLL 222
Cdd:TIGR03796 233 -------------FLWHILRLPVRFFAQRHAGDIASRVQLNDQVAEFLSGQ-LATTALDAVMLVFYALLMLLYDPVLTLI 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 223 ALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIaeeSFGAVR---TVRSFAKESYMVSQ----YSKKVDETLKLGLK 295
Cdd:TIGR03796 299 GIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGV---AISGLQsieTLKASGLESDFFSRwagyQAKLLNAQQELGVL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 296 QAVLVGL--FFGGLNAAFTLSVitvvsyGAYLTIYGSMTVGALTSF--ILYSLTvgssvsslsSLYTTAMKAAGASRRVF 371
Cdd:TIGR03796 376 TQILGVLptLLTSLNSALILVV------GGLRVMEGQLTIGMLVAFqsLMSSFL---------EPVNNLVGFGGTLQELE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 372 QILDRVS-------------SMSSSGDKCPVGNPDGDVELNDVWFAYpSRPSHMILKGISLRLTPGSKVALVGPSGGGKT 438
Cdd:TIGR03796 441 GDLNRLDdvlrnpvdplleePEGSAATSEPPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 439 TIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYgFDGEASFTDIENAAKMANAHEFI 518
Cdd:TIGR03796 520 TIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTL-WDPTIPDADLVRACKDAAIHDVI 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 519 EAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVqdaMDSLMA-GRTVLVIAHRLSTV 597
Cdd:TIGR03796 599 TSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII---DDNLRRrGCTCIIVAHRLSTI 675
|
570 580 590
....*....|....*....|....*....|....*
gi 22327455 598 KTADCVAVISDGEVAEKGTHDELLSLNGIYTNLVK 632
Cdd:TIGR03796 676 RDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
303-633 |
3.57e-71 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 240.95 E-value: 3.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 303 FFGGLN-AAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRVFQILDRVSSMS 381
Cdd:TIGR01192 241 LASGLNrMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQRE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 382 SSGDKCPVGNPDGDVELNDVWFAYPSrpSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVS 461
Cdd:TIGR01192 321 EPADAPELPNVKGAVEFRHITFEFAN--SSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGID 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 462 LMEISHQYLHKQISIVSQEPILFNCSVEENIAYGFDGeASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQK 541
Cdd:TIGR01192 399 INTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREG-ATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGER 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 542 QRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELL 621
Cdd:TIGR01192 478 QRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELI 557
|
330
....*....|..
gi 22327455 622 SLNGIYTNLVKR 633
Cdd:TIGR01192 558 QKDGRFYKLLRR 569
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
74-370 |
3.93e-69 |
|
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: 226.66 E-value: 3.93e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 74 GTIALLIGSTTNLLVPKFGGMIIDIVSRDVKTPeqqtesliAVRNAVVIILLIVVIGSICTALRAWLFNSASERVVARLR 153
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSRE--------AFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 154 KDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVISVA 233
Cdd:cd18572 73 RDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 234 VKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAAFTL 313
Cdd:cd18572 153 TKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 314 SVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:cd18572 233 TQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
137-643 |
8.02e-68 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 232.30 E-value: 8.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 137 RAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRnvTTALIGVGF--MFT 214
Cdd:PRK10790 85 QSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLR--SAALIGAMLvaMFS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 215 SSWKLTLLALVVVPVISVAVKQFGRYlrelshttqaaaavaasiaeeSFGAVRTVRSFAKE---------SYM-VSQ--- 281
Cdd:PRK10790 163 LDWRMALVAIMIFPAVLVVMVIYQRY---------------------STPIVRRVRAYLADindgfneviNGMsVIQqfr 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 282 ----YSKKVDE-----------TLKL-GLKQAVLVGLFFG----GLNAAFTLSVItvvsygayltiyGSMTVGALTSFIL 341
Cdd:PRK10790 222 qqarFGERMGEasrshymarmqTLRLdGFLLRPLLSLFSAlilcGLLMLFGFSAS------------GTIEVGVLYAFIS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 342 YSLTVGSSVSSLSSLYTTAMKAAGASRRVFQILDRVSSMSSSGDKcPVGNpdGDVELNDVWFAYpsRPSHMILKGISLRL 421
Cdd:PRK10790 290 YLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDR-PLQS--GRIDIDNVSFAY--RDDNLVLQNINLSV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 422 TPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGFD-GEA 500
Cdd:PRK10790 365 PSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDiSEE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 501 SFTDIENAAKMAnahEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDS 580
Cdd:PRK10790 445 QVWQALETVQLA---ELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 581 LMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLSLNGIYTN-----LVKRQLQSSSSVTT 643
Cdd:PRK10790 522 VREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQmyqlqLAGEELAASVREEE 589
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
74-370 |
5.41e-65 |
|
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: 215.43 E-value: 5.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 74 GTIALLIGSTTNLLVPKFGGMIID--IVSRDVKTPEQQTESLIAVrnavviilliVVIGSICTALRAWLFNSASERVVAR 151
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDaaLGGGDTASLNQIALLLLGL----------FLLQAVFSFFRIYLFARVGERVVAD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 152 LRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVIS 231
Cdd:cd18576 71 LRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 232 VAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAAF 311
Cdd:cd18576 151 LVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 312 TLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:cd18576 231 FGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
357-606 |
5.67e-63 |
|
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: 217.54 E-value: 5.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 357 YTTAMKAAGASRRVFQILDRvSSMSSSGDKCPVGNPDGDVELNDVWFAYPSRPShmILKGISLRLTPGSKVALVGPSGGG 436
Cdd:TIGR02857 284 YHARADGVAAAEALFAVLDA-APRPLAGKAPVTAAPASSLEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPSGAG 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 437 KTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHE 516
Cdd:TIGR02857 361 KSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA-RPDASDAEIREALERAGLDE 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 517 FIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLST 596
Cdd:TIGR02857 440 FVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLAL 519
|
250
....*....|
gi 22327455 597 VKTADCVAVI 606
Cdd:TIGR02857 520 AALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
394-611 |
3.66e-62 |
|
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: 205.52 E-value: 3.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 394 GDVELNDVWFAYPSRPSHmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQ 473
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 474 ISIVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTN 553
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLG-APLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 554 PSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEV 611
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
394-616 |
5.45e-61 |
|
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: 202.72 E-value: 5.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 394 GDVELNDVWFAYpsRP-SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHK 472
Cdd:cd03244 1 GDIEFKNVSLRY--RPnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 QISIVSQEPILFNCSVEENIAygFDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLT 552
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD--PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 553 NPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGT 616
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
132-632 |
1.43e-60 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 219.90 E-value: 1.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 132 ICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKT--GELLSRLSEDTQIIKNAATTNL------------SE 197
Cdd:PTZ00265 881 ISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHLLKTGLVNNIvifthfivlflvSM 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 198 ALRN-----VTTALIGVGFMFTSSWKLTLLALVVVPVISVAVKQFGRYLreLSHTTQAAAAVAASIAEESFGAVRTVRSF 272
Cdd:PTZ00265 961 VMSFyfcpiVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVF--AYNSDDEIFKDPSFLIQEAFYNMNTVIIY 1038
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 273 AKESYMVSQYSKKVDETLKlGLKQAVLVGLFFGGLNAAFTLSVITVVS-YGAYLTIYGSMTVGALTSFILYSLTVGSSVS 351
Cdd:PTZ00265 1039 GLEDYFCNLIEKAIDYSNK-GQKRKTLVNSMLWGFSQSAQLFINSFAYwFGSFLIRRGTILVDDFMKSLFTFLFTGSYAG 1117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 352 SLSSLYTTAMKAAGASRRVFQILDRVSSMS---SSGDKCPVGNP-DGDVELNDVWFAYPSRPSHMILKGISLRLTPGSKV 427
Cdd:PTZ00265 1118 KLMSLKGDSENAKLSFEKYYPLIIRKSNIDvrdNGGIRIKNKNDiKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTT 1197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 428 ALVGPSGGGKTTIANLIERFYDpLK------------------------------------------------------- 452
Cdd:PTZ00265 1198 AIVGETGSGKSTVMSLLMRFYD-LKndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkns 1276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 453 GKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGFDgEASFTDIENAAKMANAHEFIEAFPDKYNTVVGER 532
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE-DATREDVKRACKFAAIDEFIESLPNKYDTNVGPY 1355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 533 GLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSL--MAGRTVLVIAHRLSTVKTADCVAVISDGE 610
Cdd:PTZ00265 1356 GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNPD 1435
|
570 580
....*....|....*....|....*...
gi 22327455 611 -----VAEKGTHDELLSL-NGIYTNLVK 632
Cdd:PTZ00265 1436 rtgsfVQAHGTHEELLSVqDGVYKKYVK 1463
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
132-631 |
2.20e-60 |
|
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: 214.22 E-value: 2.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 132 ICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRnvTTALIGVG- 210
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLD--MWILVIVGl 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 211 FMFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQ----YSKKV 286
Cdd:TIGR01193 289 FLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKidseFGDYL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 287 DETLKLGLKQAVLvglffGGLNAAFTLSVITVVSY-GAYLTIYGSMTVGALTSF---ILYSLTvgsSVSSLSSLYTTAMK 362
Cdd:TIGR01193 369 NKSFKYQKADQGQ-----QAIKAVTKLILNVVILWtGAYLVMRGKLTLGQLITFnalLSYFLT---PLENIINLQPKLQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 363 AAGASRRVFQILDRVSSMSSSGDKCPVGNPDGDVELNDVWFAYP-SRPshmILKGISLRLTPGSKVALVGPSGGGKTTIA 441
Cdd:TIGR01193 441 ARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGyGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 442 NLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGFDGEASFTDIENAAKMANAHEFIEAF 521
Cdd:TIGR01193 518 KLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENM 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 522 PDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEylvQDAMDSL--MAGRTVLVIAHRLSTVKT 599
Cdd:TIGR01193 598 PLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLlnLQDKTIIFVAHRLSVAKQ 674
|
490 500 510
....*....|....*....|....*....|..
gi 22327455 600 ADCVAVISDGEVAEKGTHDELLSLNGIYTNLV 631
Cdd:TIGR01193 675 SDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
55-635 |
9.82e-60 |
|
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: 212.12 E-value: 9.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 55 VGFGRVFALAKPDAGK-----LVIGTIALLIGsttnLLVPKFGGMIIDIVsrdvkTPEQQTESLIAVrnavviillivVI 129
Cdd:TIGR03797 121 LGLRDLLRFALRGARRdllaiLAMGLLGTLLG----MLVPIATGILIGTA-----IPDADRSLLVQI-----------AL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 130 GSICTALRAWLFNSASERVVARL--RKD------LFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALrN 201
Cdd:TIGR03797 181 ALLAAAVGAAAFQLAQSLAVLRLetRMDaslqaaVWDRLLRLPVSFFRQYSTGDLASRAMGISQIRRILSGSTLTTLL-S 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 202 VTTALIGVGFMFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQ 281
Cdd:TIGR03797 260 GIFALLNLGLMFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFAR 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 282 YSKKVDETLKLGLKqAVLVGLFFGGLNAAF-TLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTA 360
Cdd:TIGR03797 340 WAKLFSRQRKLELS-AQRIENLLTVFNAVLpVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISI 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 361 MKAAGASRRVFQILDrvSSMSSSGDKCPVGNPDGDVELNDVWFAYpSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTI 440
Cdd:TIGR03797 419 LAVIPLWERAKPILE--ALPEVDEAKTDPGKLSGAIEVDRVTFRY-RPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTL 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 441 ANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAygfdGEASFT--DIENAAKMANAHEFI 518
Cdd:TIGR03797 496 LRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA----GGAPLTldEAWEAARMAGLAEDI 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 519 EAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRtvLVIAHRLSTVK 598
Cdd:TIGR03797 572 RAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIR 649
|
570 580 590
....*....|....*....|....*....|....*..
gi 22327455 599 TADCVAVISDGEVAEKGTHDELLSLNGIYTNLVKRQL 635
Cdd:TIGR03797 650 NADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQL 686
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
322-622 |
2.29e-58 |
|
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: 205.75 E-value: 2.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 322 GAYLTIYGSMTVGAL--TSFIL------YSLTVGSSVSslsslYTTAMKAAgasRRVFQILDRVSSmssSGDKCPVGNPD 393
Cdd:COG4618 260 GAYLVIQGEITPGAMiaASILMgralapIEQAIGGWKQ-----FVSARQAY---RRLNELLAAVPA---EPERMPLPRPK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 394 GDVELNDVWFAYP--SRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLH 471
Cdd:COG4618 329 GRLSVENLTVVPPgsKRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 472 KQISIVSQEPILFNCSVEENIAyGFdGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALL 551
Cdd:COG4618 406 RHIGYLPQDVELFDGTIAENIA-RF-GDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALY 483
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327455 552 TNPSVLLLDEATSALDAESEYLVQDAMDSL-MAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
303-622 |
3.97e-58 |
|
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: 204.89 E-value: 3.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 303 FFGGLNAAFTLSV-ITVVSYGAYLTIYGSMTVGALtsfILYSLTVGSSVS---SLSSLYTTAMKAAGASRRVFQILDrvs 378
Cdd:TIGR01842 226 MLSNLSKYFRIVLqSLVLGLGAYLAIDGEITPGMM---IAGSILVGRALApidGAIGGWKQFSGARQAYKRLNELLA--- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 379 SMSSSGDKCPVGNPDGDVELNDVWFAYPSrPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLN 458
Cdd:TIGR01842 300 NYPSRDPAMPLPEPEGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 459 GVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYgFDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSG 538
Cdd:TIGR01842 379 GADLKQWDRETFGKHIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSG 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 539 GQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTH 617
Cdd:TIGR01842 458 GQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGER 537
|
....*
gi 22327455 618 DELLS 622
Cdd:TIGR01842 538 DEVLA 542
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
362-637 |
1.81e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 203.92 E-value: 1.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 362 KAAGASRRVFQILDRVSSMSSSGDKCPVGNPDGDVELNDVWFAYPSrpSHMILKGISLRLTPGSKVALVGPSGGGKTTIA 441
Cdd:PRK11174 316 QAVGAAESLVTFLETPLAHPQQGEKELASNDPVTIEAEDLEILSPD--GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 442 NLIERFYdPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHEFIEAF 521
Cdd:PRK11174 394 NALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG-NPDASDEQLQQALENAWVSEFLPLL 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 522 PDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTAD 601
Cdd:PRK11174 472 PQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWD 551
|
250 260 270
....*....|....*....|....*....|....*.
gi 22327455 602 CVAVISDGEVAEKGTHDELLSLNGIYTNLVKRQLQS 637
Cdd:PRK11174 552 QIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
147-594 |
2.11e-55 |
|
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: 196.81 E-value: 2.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 147 RVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVV 226
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 227 VPVISVAVKQFGRYLRELSHTT--QAAAAVAASIAEESFGAVRTVRSFAKESYmVSQYSKKVDETLKLGLKQAVLVGLFF 304
Cdd:TIGR02868 163 LLLAGFVAPLVSLRAARAAEQAlaRLRGELAAQLTDALDGAAELVASGALPAA-LAQVEEADRELTRAERRAAAATALGA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 305 GGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRVFQILD---RVSSMS 381
Cdd:TIGR02868 242 ALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDaagPVAEGS 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 382 SSGDKcPVGNPDGDVELNDVWFAYPsrPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVS 461
Cdd:TIGR02868 322 APAAG-AVGLGKPTLELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 462 LMEISHQYLHKQISIVSQEPILFNCSVEENIAYGfDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQK 541
Cdd:TIGR02868 399 VSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA-RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGER 477
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 22327455 542 QRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRL 594
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
260-640 |
1.01e-54 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 202.18 E-value: 1.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 260 EESFGAVRTVRSFAKESYMVSQYSkkVDETL--KLGLKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTV---- 333
Cdd:PTZ00265 240 EEALVGIRTVVSYCGEKTILKKFN--LSEKLysKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQqpnn 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 334 ----GALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRVFQILDRVSSMSSSGDKCPVGNPDgDVELNDVWFAYPSRP 409
Cdd:PTZ00265 318 dfhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 410 SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGV-SLMEISHQYLHKQISIVSQEPILFNCSV 488
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSI 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYGF---------------DGEASF-----------------------------------------TDIENAAKMA 512
Cdd:PTZ00265 477 KNNIKYSLyslkdlealsnyyneDGNDSQenknkrnscrakcagdlndmsnttdsneliemrknyqtikdSEVVDVSKKV 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 513 NAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVI 590
Cdd:PTZ00265 557 LIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGneNRITIII 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 591 AHRLSTVKTADCVAVISDGE-----------------------------------------------VAEKGTHDELL-S 622
Cdd:PTZ00265 637 AHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMkN 716
|
490
....*....|....*...
gi 22327455 623 LNGIYTNLVKRQLQSSSS 640
Cdd:PTZ00265 717 KNGIYYTMINNQKVSSKK 734
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
74-370 |
2.66e-54 |
|
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: 187.13 E-value: 2.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 74 GTIALLIGSTTNLLVPKFGGMIID-IVSRdvktpeqqtESLIAVRNAVVIILLIVVIGSICTALRAWLFNSASERVVARL 152
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDgIVIE---------KSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 153 RKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVISV 232
Cdd:cd18784 72 RNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 233 AVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAAFT 312
Cdd:cd18784 152 VSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTEL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 313 LSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:cd18784 232 ALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
366-634 |
1.25e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 193.12 E-value: 1.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 366 ASRRVFQILDRVSSMSSSGDKCPVGNPdGDVELNDVWFAYPSRPsHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIE 445
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQ-VSLTLNNVSFTYPDQP-QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 446 RFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYgfdgeasftdienAAKMANAHEFIEAF---- 521
Cdd:PRK11160 388 RAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL-------------AAPNASDEALIEVLqqvg 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 522 -------PDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRL 594
Cdd:PRK11160 455 leklledDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRL 534
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 22327455 595 STVKTADCVAVISDGEVAEKGTHDELLSLNGIYTNLVKRQ 634
Cdd:PRK11160 535 TGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
76-370 |
2.85e-53 |
|
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: 184.22 E-value: 2.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 76 IALLIGSTTNLLVPKFGGMIIDIVSrdvktpeqQTESLIAVRNAVVIILLIVVIGSICTALRAWLFNSASERVVARLRKD 155
Cdd:cd18575 3 IALLIAAAATLALGQGLRLLIDQGF--------AAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 156 LFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVISVAVK 235
Cdd:cd18575 75 VFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPII 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 236 QFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAAFTLSV 315
Cdd:cd18575 155 LFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 316 ITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:cd18575 235 VFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
71-342 |
3.86e-50 |
|
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: 175.82 E-value: 3.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 71 LVIGTIALLIGSTTNLLVPKFGGMIIDIVsrdvkTPEQQTESLIAVrnaVVIILLIVVIGSICTALRAWLFNSASERVVA 150
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV-----IPAGDLSLLLWI---ALLLLLLALLRALLSYLRRYLAARLGQRVVF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 151 RLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVI 230
Cdd:cd07346 73 DLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 231 SVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAA 310
Cdd:cd07346 153 VLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLL 232
|
250 260 270
....*....|....*....|....*....|..
gi 22327455 311 FTLSVITVVSYGAYLTIYGSMTVGALTSFILY 342
Cdd:cd07346 233 TALGTALVLLYGGYLVLQGSLTIGELVAFLAY 264
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
71-346 |
5.11e-50 |
|
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: 175.14 E-value: 5.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 71 LVIGTIALLIGSTTNLLVPKFGGMIIDIVSRDvKTPEQQTESLIAVrnavvIILLIVVIGSICTALRAWLFNSASERVVA 150
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPD-GDPETQALNVYSL-----ALLLLGLAQFILSFLQSYLLNHTGERLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 151 RLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVI 230
Cdd:pfam00664 75 RLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 231 SVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAA 310
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 22327455 311 FTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTV 346
Cdd:pfam00664 235 GYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQL 270
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
396-622 |
3.03e-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: 165.97 E-value: 3.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPsrPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPI--LFNCSVEENIAYG-----FDGEASFTDIENAAKMANAHEFIEAFPDkyntvvgerglRLSGGQKQRIAIAR 548
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlgLPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 549 ALLTNPSVLLLDEATSALDAESEYLVQDAMDSL-MAGRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFS 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
397-592 |
2.45e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 159.98 E-value: 2.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISI 476
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 477 VSQEPILFNCSVEENIAYGFDGEASFTDIENAAKMANAHEFIEAFPDKyntvvgeRGLRLSGGQKQRIAIARALLTNPSV 556
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDK-------PVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 22327455 557 LLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAH 592
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSH 189
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
393-616 |
4.66e-45 |
|
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: 159.50 E-value: 4.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 393 DGDVELNDVWFAY-PSRPShmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLH 471
Cdd:cd03369 4 HGEIEVENLSVRYaPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 472 KQISIVSQEPILFNCSVEENIaygfDGEASFTDIENAAKMAnahefieafpdkyntvVGERGLRLSGGQKQRIAIARALL 551
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNL----DPFDEYSDEEIYGALR----------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 552 TNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGT 616
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
71-342 |
1.56e-44 |
|
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: 160.67 E-value: 1.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 71 LVIGTIALLIGSTTNLLVPKFGGMIIDIVsrdvkTPEQQTESLI----------AVRnavviillivvigSICTALRAWL 140
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSV-----IGGGLRELLWllallilgvaLLR-------------GVFRYLQGYL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 141 FNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLT 220
Cdd:cd18542 63 AEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 221 LLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLV 300
Cdd:cd18542 143 LISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLL 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 22327455 301 GLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILY 342
Cdd:cd18542 223 AKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISY 264
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
85-370 |
9.60e-44 |
|
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: 158.48 E-value: 9.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 85 NLLVPKFGGMIIDIVSRDVKtpEQQTESLIAVRNAVVIILLIVVIGSICTALRAWLFNSASERVVARLRKDLFRHLMHQE 164
Cdd:cd18574 12 NIQIPLLLGDLVNVISRSLK--ETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 165 IAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVISVAVKQFGRYLREL 244
Cdd:cd18574 90 IAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 245 SHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAAFTLSVITVVSYGAY 324
Cdd:cd18574 170 SRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIVLGVLYYGGS 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 22327455 325 LTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:cd18574 250 LVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
396-636 |
4.95e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.84 E-value: 4.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLhKQIS 475
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILF-NCSVEENIAYgfdgEASFTDIENAAKMANAHEFIEAF--PDKYNTVVGErglrLSGGQKQRIAIARALLT 552
Cdd:COG1131 77 YVPQEPALYpDLTVRENLRF----FARLYGLPRKEARERIDELLELFglTDAADRKVGT----LSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 553 NPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS--LNGIYT 628
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKArlLEDVFL 228
|
....*...
gi 22327455 629 NLVKRQLQ 636
Cdd:COG1131 229 ELTGEEAR 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
363-622 |
5.42e-43 |
|
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: 161.99 E-value: 5.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 363 AAGASRRVF---QILDRVSSMSSSGDKCPVGNPDGD--VELNDVWFAYPSRPSH--MILKGISLRLTPGSKVALVGPSGG 435
Cdd:COG1123 223 EDGPPEEILaapQALAAVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGKGgvRAVDDVSLTLRRGETLGLVGESGS 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 436 GKTTIANLIERFYDPLKGKILLNGVSLMEISHQ---YLHKQISIVSQEPIL-FNC--SVEENIAYGFD--GEASFTDIEN 507
Cdd:COG1123 303 GKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRRRVQMVFQDPYSsLNPrmTVGDIIAEPLRlhGLLSRAERRE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 508 -AAKMANAHEFIEAFPDKYntvVGErglrLSGGQKQRIAIARALLTNPSVLLLDEATSALDaeseYLVQDAMDSLMA--- 583
Cdd:COG1123 383 rVAELLERVGLPPDLADRY---PHE----LSGGQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQILNLLRdlq 451
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 22327455 584 ---GRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDELLS 622
Cdd:COG1123 452 relGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
71-370 |
1.12e-42 |
|
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: 155.28 E-value: 1.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 71 LVIGTIALLIGSTTNLLVPKFGGMIIDIVSRDVKTPeQQTESLIAVrnavviilliVVIGSICTALRAWLFNSASERVVA 150
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSG-GLLALLVAL----------FLLQAVLSALSSYLLGRTGERVVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 151 RLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVI 230
Cdd:cd18551 70 DLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 231 SVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAA 310
Cdd:cd18551 150 FLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 311 FTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:cd18551 230 VQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
61-380 |
1.15e-42 |
|
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: 156.46 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 61 FALAKPDAGKLVIGTI-ALLIGSTTnllvPKFG---GMIIDIVSrDVKTPEQQTES--------LIAVrnavviillivv 128
Cdd:cd18578 1 LKLNKPEWPLLLLGLIgAIIAGAVF----PVFAilfSKLISVFS-LPDDDELRSEAnfwalmflVLAI------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 129 IGSICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTK--TGELLSRLSEDTQIIKNAATTNLSEALRNVTTAL 206
Cdd:cd18578 64 VAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 207 IGVGFMFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKV 286
Cdd:cd18578 144 AGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 287 DETLKLGLKQAVLVGLFFgGLNAAFTLSVITVV-SYGAYLTIYGSMTVGA-LTSFIlySLTVGSSVSSLSSLYTTAM-KA 363
Cdd:cd18578 224 EEPLKKGLRRALISGLGF-GLSQSLTFFAYALAfWYGGRLVANGEYTFEQfFIVFM--ALIFGAQSAGQAFSFAPDIaKA 300
|
330
....*....|....*..
gi 22327455 364 AGASRRVFQILDRVSSM 380
Cdd:cd18578 301 KAAAARIFRLLDRKPEI 317
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
396-615 |
2.08e-42 |
|
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: 150.93 E-value: 2.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPSHmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQyLHKQIS 475
Cdd:cd03247 1 LSINNVSFSYPEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILFNCSVEENIaygfdgeasftdienaakmanahefieafpdkyntvvgerGLRLSGGQKQRIAIARALLTNPS 555
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 556 VLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKG 615
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
397-611 |
5.98e-42 |
|
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: 149.67 E-value: 5.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRpSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISI 476
Cdd:cd03246 2 EVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 477 VSQEPILFNCSVEENIaygfdgeasftdienaakmanahefieafpdkyntvvgerglrLSGGQKQRIAIARALLTNPSV 556
Cdd:cd03246 81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 557 LLLDEATSALDAESEYLVQDAMDSL-MAGRTVLVIAHRLSTVKTADCVAVISDGEV 611
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
414-564 |
1.29e-41 |
|
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: 147.79 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFN-CSVEENI 492
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327455 493 AYGFDGEAsFTDIENAAKMANAHEFIeAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATS 564
Cdd:pfam00005 81 RLGLLLKG-LSKREKDARAEEALEKL-GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
397-610 |
6.45e-41 |
|
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: 148.00 E-value: 6.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRPSHmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISI 476
Cdd:cd03225 1 ELKNLSFSYPDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 477 VSQEP--ILFNCSVEENIAYGF-----DGEASFTDIENAAKMANAHEFIEAFPDkyntvvgerglRLSGGQKQRIAIARA 549
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLenlglPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 550 LLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTVKT-ADCVAVISDGE 610
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
71-340 |
6.46e-41 |
|
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: 150.65 E-value: 6.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 71 LVIGTIALLIGSTTNLLVPKFGGMIIDIVsrdvkTPEQQTESLI----------AVRNavviillivvigsICTALRAWL 140
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDI-----FVEKDLEALLlvplaiiglfLLRG-------------LASYLQTYL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 141 FNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLT 220
Cdd:cd18552 63 MAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 221 LLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLV 300
Cdd:cd18552 143 LIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARAR 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 22327455 301 GL------FFGGlnaaftLSVITVVSYGAYLTIYGSMTVGALTSFI 340
Cdd:cd18552 223 ALssplmeLLGA------IAIALVLWYGGYQVISGELTPGEFISFI 262
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
396-611 |
1.21e-40 |
|
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: 147.64 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPS-RPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQ----YL 470
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 471 HKQISIVSQE----PILfncSVEENIAYGfdgeASFTDIENAAKMANAHEFIEAF--PDKYNTVVGErglrLSGGQKQRI 544
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELP----LLLAGVPKKERRERAEELLERVglGDRLNHYPSE----LSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 545 AIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSL--MAGRTVLVIAHRLSTVKTADCVAVISDGEV 611
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
151-632 |
1.53e-40 |
|
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: 159.34 E-value: 1.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 151 RLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNA---ATTNLSEALRNVTTALIgvgFMFTSSWKLTLLALVVV 227
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMippVIKMFMGSLFNVIGALI---VILLATPIAAVIIPPLG 1115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 228 PVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAV-----LVGL 302
Cdd:TIGR00957 1116 LLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVanrwlAVRL 1195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 303 FFGGlNAaftlsvitVVSYGAYLTIYG--SMTVGALTSFILYSLTVgssvsSLSSLYTTAMKAAGASRRVfqILDRVSSM 380
Cdd:TIGR00957 1196 ECVG-NC--------IVLFAALFAVISrhSLSAGLVGLSVSYSLQV-----TFYLNWLVRMSSEMETNIV--AVERLKEY 1259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 381 SSS---------GDKCPVGNPD-GDVELNDVWFAYpsRPS-HMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYD 449
Cdd:TIGR00957 1260 SETekeapwqiqETAPPSGWPPrGRVEFRNYCLRY--REDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 450 PLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIaygfDGEASFTDIE--NAAKMANAHEFIEAFPDKYNT 527
Cdd:TIGR00957 1338 SAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL----DPFSQYSDEEvwWALELAHLKTFVSALPDKLDH 1413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 528 VVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVIS 607
Cdd:TIGR00957 1414 ECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLD 1493
|
490 500
....*....|....*....|....*
gi 22327455 608 DGEVAEKGTHDELLSLNGIYTNLVK 632
Cdd:TIGR00957 1494 KGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
396-615 |
7.51e-40 |
|
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: 145.73 E-value: 7.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPSHM-ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNG---VSLMEISHQYLH 471
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 472 KQISIVSQEPIL-FN--CSVEENIA------YGFDGEASFTDIENAAKMA--NAHEFIEAFPDkyntvvgerglRLSGGQ 540
Cdd:cd03257 82 KEIQMVFQDPMSsLNprMTIGEQIAeplrihGKLSKKEARKEAVLLLLVGvgLPEEVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 541 KQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTVK-TADCVAVISDGEVAEKG 615
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAkIADRVAVMYAGKIVEEG 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
396-610 |
8.16e-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: 144.92 E-value: 8.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRP--SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLI--ErfYDPLKGKILLNGvslmeishqylh 471
Cdd:cd03250 1 ISVEDASFTWDSGEqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 472 kQISIVSQEPILFNCSVEENIAYG--FDGEASFTDIENAAkmanAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARA 549
Cdd:cd03250 67 -SIAYVSQEPWIQNGTIRENILFGkpFDEERYEKVIKACA----LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 550 LLTNPSVLLLDEATSALDAE-SEYLVQDA-MDSLMAGRTVLVIAHRLSTVKTADCVAVISDGE 610
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHvGRHIFENCiLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
396-620 |
1.07e-39 |
|
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: 145.40 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSrpsHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYD-----PLKGKILLNGVSLMEISHQ-- 468
Cdd:cd03260 1 IELRDLNVYYGD---KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 469 YLHKQISIVSQEPILFNCSVEENIAYGF------DGEASFTDIENAAKMAnahefieAFPDKyntvVGER--GLRLSGGQ 540
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLrlhgikLKEELDERVEEALRKA-------ALWDE----VKDRlhALGLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 541 KQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVK-TADCVAVISDGEVAEKGTHDE 619
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 22327455 620 L 620
Cdd:cd03260 227 I 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
396-622 |
1.94e-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: 151.98 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPSHmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDP---LKGKILLNGVSLMEISHQYLHK 472
Cdd:COG1123 5 LEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 QISIVSQEPI--LFNCSVEENIAYGFD-GEASFTDIENAAKMANAHEFIEAFPDKYNTvvgerglRLSGGQKQRIAIARA 549
Cdd:COG1123 84 RIGMVFQDPMtqLNPVTVGDQIAEALEnLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 550 LLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
397-610 |
5.06e-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: 140.84 E-value: 5.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISI 476
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 477 VSQepilfncsveeniaygfdgeasftdienaakmanahefieafpdkyntvvgerglrLSGGQKQRIAIARALLTNPSV 556
Cdd:cd00267 78 VPQ--------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 557 LLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTVKTA-DCVAVISDGE 610
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
396-615 |
7.33e-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: 142.27 E-value: 7.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSlmeISHQYLHKQ-I 474
Cdd:cd03259 1 LELKGLSKTYGSVR---ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD---VTGVPPERRnI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 475 SIVSQEPILF-NCSVEENIAYGFD----GEASFTD-IENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQRIAIAR 548
Cdd:cd03259 75 GMVFQDYALFpHLTVAENIAFGLKlrgvPKAEIRArVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 549 ALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLS-TVKTADCVAVISDGEVAEKG 615
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
132-370 |
2.57e-38 |
|
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: 143.77 E-value: 2.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 132 ICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGF 211
Cdd:cd18577 62 VLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFII 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 212 MFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLK 291
Cdd:cd18577 142 AFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARK 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 292 LGLKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSfILYSLTVGSSVSSLSSLYTTAM-KAAGASRRV 370
Cdd:cd18577 222 AGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLT-VFFAVLIGAFSLGQIAPNLQAFaKARAAAAKI 300
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
396-607 |
3.06e-38 |
|
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: 141.07 E-value: 3.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPS-RPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEIshqylHKQI 474
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 475 SIVSQEPILFN-CSVEENIAYGFDgeasFTDIENAAKMANAHEFIEAfpdkyntvVGERGLR------LSGGQKQRIAIA 547
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLE----LQGVPKAEARERAEELLEL--------VGLSGFEnayphqLSGGMRQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 548 RALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLS-TVKTADCVAVIS 607
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLS 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
397-622 |
3.77e-38 |
|
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: 141.53 E-value: 3.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLhKQISI 476
Cdd:COG4555 3 EVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 477 VSQEPILF-NCSVEENI-----AYGFDGEASFTDIENAAKMANahefIEAFPDKYntvVGErglrLSGGQKQRIAIARAL 550
Cdd:COG4555 79 LPDERGLYdRLTVRENIryfaeLYGLFDEELKKRIEELIELLG----LEEFLDRR---VGE----LSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 551 LTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
396-622 |
1.02e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 140.22 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTT----IANLIErfydPLKGKILLNGVSLMEISHQ--Y 469
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTllkaILGLLP----PTSGTVRLFGKPPRRARRRigY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 470 LHKQISIVSQEPIlfncSVEENIAYGFDGEASFTDIENAAKMANAHEFIEAfpdkyntvVGERGLR------LSGGQKQR 543
Cdd:COG1121 80 VPQRAEVDWDFPI----TVRDVVLMGRYGRRGLFRRPSRADREAVDEALER--------VGLEDLAdrpigeLSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 544 IAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSL-MAGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEkGTHDELL 621
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVL 226
|
.
gi 22327455 622 S 622
Cdd:COG1121 227 T 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
396-622 |
1.60e-37 |
|
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: 140.18 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPIL-FNCSVEENIAYG---------FDGEASFTDIENAAKMANahefIEAFPDKYntvVGErglrLSGGQKQRIA 545
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlglfgRPSAEDREAVEEALERTG----LEHLADRP---VDE----LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 546 IARALLTNPSVLLLDEATSALDAESEYLVQDAMDSL--MAGRTVLVIAHRLS-TVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
71-342 |
2.25e-37 |
|
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: 141.01 E-value: 2.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 71 LVIGTIALLIGSTTNLLVPKFGGMIIDIVSRDVKTPEQQTESLIAVrnavviillivvigsICTAL---------RAWLF 141
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLI---------------LLLALligifrflwRYLIF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 142 NsASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTL 221
Cdd:cd18541 66 G-ASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 222 LALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVG 301
Cdd:cd18541 145 IALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 22327455 302 LFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILY 342
Cdd:cd18541 225 LFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
396-610 |
3.13e-37 |
|
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: 136.55 E-value: 3.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSrpsHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSL--MEISHQYLHKQ 473
Cdd:cd03229 1 LELKNVSKRYGQ---KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 474 ISIVSQEPILF-NCSVEENIAYGfdgeasftdienaakmanahefieafpdkyntvvgerglrLSGGQKQRIAIARALLT 552
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 553 NPSVLLLDEATSALDAESEYLVQDAMDSL--MAGRTVLVIAHRLSTVKT-ADCVAVISDGE 610
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
397-624 |
4.45e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 137.96 E-value: 4.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRPSHmilkgISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSlmeISHQYLHKQ-IS 475
Cdd:COG3840 3 RLDDLTYRYGDFPLR-----FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---LTALPPAERpVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILFN-CSVEENIAYGFD-----GEASFTDIENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQRIAIARA 549
Cdd:COG3840 75 MLFQENNLFPhLTVAQNIGLGLRpglklTAEQRAQVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 550 LLTNPSVLLLDEATSALD----AESEYLVQDAMDSLmaGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDELLSLN 624
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
396-611 |
7.19e-37 |
|
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: 135.60 E-value: 7.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLhKQIS 475
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILF-NCSVEENiaygfdgeasftdienaakmanahefieafpdkyntvvgergLRLSGGQKQRIAIARALLTNP 554
Cdd:cd03230 77 YLPEEPSLYeNLTVREN------------------------------------------LKLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 555 SVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEV 611
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
86-370 |
1.81e-36 |
|
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: 138.24 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 86 LLVPKFGGMIIDIVSRDVktpeQQTESLIAVrnavVIILLIVVIGSICTALRAWLFNSASERVVARLRKDLFRHLMHQEI 165
Cdd:cd18590 13 TFIPYYTGRVIDILGGEY----QHNAFTSAI----GLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 166 AFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVISVAVKQFGRYLRELS 245
Cdd:cd18590 85 GFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 246 HTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLgLKQAVLVGLFFGGLNAAFTLSV-ITVVSYGAY 324
Cdd:cd18590 165 QAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNL-KDRRDTVRAVYLLVRRVLQLGVqVLMLYCGRQ 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 22327455 325 LTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:cd18590 244 LIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
377-632 |
2.01e-36 |
|
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: 137.35 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 377 VSSMSSSGDKCPVGnPDGDVELNDVWFAYPS--RPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGK 454
Cdd:cd03288 2 IASISGSSNSGLVG-LGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 455 ILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIaygfDGEASFTD--IENAAKMANAHEFIEAFPDKYNTVVGER 532
Cdd:cd03288 78 IVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL----DPECKCTDdrLWEALEIAQLKNMVKSLPGGLDAVVTEG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 533 GLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVA 612
Cdd:cd03288 154 GENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILV 233
|
250 260
....*....|....*....|.
gi 22327455 613 EKGTHDELLSL-NGIYTNLVK 632
Cdd:cd03288 234 ECDTPENLLAQeDGVFASLVR 254
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
397-597 |
5.96e-36 |
|
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: 134.20 E-value: 5.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQ--YLHKQI 474
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 475 SIVSQEPIlfncSVEENIAYGFDGEASFTDIENAAKMANAHEFIEAfpdkyntvVGERGLR------LSGGQKQRIAIAR 548
Cdd:cd03235 78 SIDRDFPI----SVRDVVLMGLYGHKGLFRRLSKADKAKVDEALER--------VGLSELAdrqigeLSGGQQQRVLLAR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22327455 549 ALLTNPSVLLLDEATSALDAESEYLVQDAMDSL-MAGRTVLVIAHRLSTV 597
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLV 195
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
396-613 |
8.82e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.40 E-value: 8.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPS-RPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLI---ERfydPLKGKILLNGVSLMEISH---- 467
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILgglDR---PTSGEVLIDGQDISSLSErela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 468 QYLHKQISIVSQEPILFNC-SVEENIAY-----GFDGEASFTDIENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQK 541
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVALplllaGVSRKERRERARELLERVGLGDRLDHRPSQ-----------LSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 542 QRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTVKTADCVAVISDGEVAE 613
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
396-622 |
1.57e-35 |
|
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: 133.86 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRP-SHMILKGISLRLTPGSKVALVGPSGGGKTT---IANLIERfydPLKGKILLNGVSLMEISHQYL- 470
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER---PTSGSVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 471 --HKQISIVSQEPILFNC-SVEENIAY-----GFDGEASFTDIENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQ 542
Cdd:cd03258 79 kaRRRIGMIFQHFNLLSSrTVFENVALpleiaGVPKAEIEERVLELLELVGLEDKADAYPAQ-----------LSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 543 RIAIARALLTNPSVLLLDEATSALDAESEY----LVQDAMDSLmaGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTH 617
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQsilaLLRDINREL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*
gi 22327455 618 DELLS 622
Cdd:cd03258 226 EEVFA 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
396-592 |
1.73e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 134.45 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRP-SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQylhkqI 474
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 475 SIVSQEPILFN-CSVEENIAYGFDgeasFTDIENAAKMANAHEFIE-----AFPDKYntvVGErglrLSGGQKQRIAIAR 548
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLE----LRGVPKAERRERARELLElvglaGFEDAY---PHQ----LSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22327455 549 ALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAH 592
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTH 197
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
414-622 |
2.64e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 136.36 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIA---NLIERfydPLKGKILLNGVSLMEISHQYLH---KQISIVSQEPILFN-C 486
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLER---PTSGSVLVDGVDLTALSERELRaarRKIGMIFQHFNLLSsR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 SVEENIAY-----GFDGEasftDIEnaakmANAHEFIE---------AFPDkyntvvgerglRLSGGQKQRIAIARALLT 552
Cdd:COG1135 98 TVAENVALpleiaGVPKA----EIR-----KRVAELLElvglsdkadAYPS-----------QLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 553 NPSVLLLDEATSALDAESEY----LVQDAMDSLmaGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDELLS 622
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRsildLLKDINREL--GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDVFA 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
139-625 |
3.80e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 142.81 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 139 WLFNSaSERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDT-QIIKNAAttNLSEALRNV------TTALIGVgF 211
Cdd:PLN03232 973 WLISS-SLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIgDIDRNVA--NLMNMFMNQlwqllsTFALIGT-V 1048
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 212 MFTSSWKLTLLaLVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASiaeESFGAVRTVRSFAKESYMVSQYSKKVDETLK 291
Cdd:PLN03232 1049 STISLWAIMPL-LILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFG---EALNGLSSIRAYKAYDRMAKINGKSMDNNIR 1124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 292 LGLKQAVLVGLF------FGGLNAAFTLSvITVVSYGAYLTIYG-SMTVGALTSfilYSLTVGSSVSSLSSLYTTAMKAA 364
Cdd:PLN03232 1125 FTLANTSSNRWLtirletLGGVMIWLTAT-FAVLRNGNAENQAGfASTMGLLLS---YTLNITTLLSGVLRQASKAENSL 1200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 365 GASRRVFQILDRVSSMSS--SGDKCPVGNP-DGDVELNDVWFAY-PSRPShmILKGISLRLTPGSKVALVGPSGGGKTTI 440
Cdd:PLN03232 1201 NSVERVGNYIDLPSEATAiiENNRPVSGWPsRGSIKFEDVHLRYrPGLPP--VLHGLSFFVSPSEKVGVVGRTGAGKSSM 1278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 441 ANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIaygfD--GEASFTDIENAAKMANAHEFI 518
Cdd:PLN03232 1279 LNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI----DpfSEHNDADLWEALERAHIKDVI 1354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 519 EAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVK 598
Cdd:PLN03232 1355 DRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTII 1434
|
490 500
....*....|....*....|....*..
gi 22327455 599 TADCVAVISDGEVAEKGTHDELLSLNG 625
Cdd:PLN03232 1435 DCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
414-622 |
5.58e-35 |
|
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: 132.46 E-value: 5.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQylHKQISIVSQEPILF-NCSVEENI 492
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 493 AYGF-----DGEASFTDIENAAKMANAHEFIEAFPdkyntvvgergLRLSGGQKQRIAIARALLTNPSVLLLDEATSALD 567
Cdd:cd03299 93 AYGLkkrkvDKKEIERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 568 AESE----YLVQDAMDSLmaGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDELLS 622
Cdd:cd03299 162 VRTKeklrEELKKIRKEF--GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
396-622 |
7.75e-35 |
|
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: 7.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYP--SRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISH-QYLHK 472
Cdd:TIGR04520 1 IEVENVSFSYPesEKP---ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlWEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 QISIVSQEP--ILFNCSVEENIAYG-----FDGEASFTDIENAAKMANAHEFIEAFPdkyntvvgergLRLSGGQKQRIA 545
Cdd:TIGR04520 78 KVGMVFQNPdnQFVGATVEDDVAFGlenlgVPREEMRKRVDEALKLVGMEDFRDREP-----------HLLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 546 IARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
396-639 |
1.90e-34 |
|
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: 131.08 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRP-SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQI 474
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 475 SIVSQEPIL-FN--CSVEENIA-----YGFDGEAsftdiENAAKMANAHEFIEAFPDKYntvVGErglrLSGGQKQRIAI 546
Cdd:COG1124 82 QMVFQDPYAsLHprHTVDRILAeplriHGLPDRE-----ERIAELLEQVGLPPSFLDRY---PHQ----LSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 547 ARALLTNPSVLLLDEATSALDAeseyLVQDAMDSLMA------GRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDE 619
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDV----SVQAEILNLLKdlreerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
250 260
....*....|....*....|.
gi 22327455 620 LLS-LNGIYTnlvkRQLQSSS 639
Cdd:COG1124 226 LLAgPKHPYT----RELLAAS 242
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
396-613 |
2.68e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 130.17 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPsrPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQ---YLHK 472
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 QISIVSQE-PILFNCSVEENIAY-----GFDGEASFTDIENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQRIAI 546
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVLDLVGLSDKAKALPHE-----------LSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327455 547 ARALLTNPSVLLLDEATSALDAEseyLVQDAMDSLM----AGRTVLVIAHRLSTVKTADC-VAVISDGEVAE 613
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPE---TSWEIMELLEeinrRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
396-620 |
4.10e-34 |
|
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: 129.93 E-value: 4.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGV---SLMEISHQYLHK 472
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 QISIVSQEPILFNC-SVEENIAYGF--DGEASFTDIENAAKMANAHEFIEAFPDKYntvVGErglrLSGGQKQRIAIARA 549
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLreHTRLSEEEIREIVLEKLEAVGLRGAEDLY---PAE----LSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 550 LLTNPSVLLLDEATSALDAESEYLVQDAMDSL--MAGRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDEL 620
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
396-622 |
7.83e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 129.34 E-value: 7.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDV--WFAypsrpSHMILKGISLRLTPGSKVALVGPSGGGKTTI---ANLIERfydPLKGKILLNGVSLMEISHQ-- 468
Cdd:COG1126 2 IEIENLhkSFG-----DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLTDSKKDin 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 469 YLHKQISIVSQEPILF-NCSVEENIAYGfdgeasftDI-------ENAAKMANAH-------EFIEAFPDkyntvvgerg 533
Cdd:COG1126 74 KLRRKVGMVFQQFNLFpHLTVLENVTLA--------PIkvkkmskAEAEERAMELlervglaDKADAYPA---------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 534 lRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAEseyLVQ---DAMDSLMA-GRTVLVIAHRLSTVKT-ADCVAVISD 608
Cdd:COG1126 136 -QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGevlDVMRDLAKeGMTMVVVTHEMGFAREvADRVVFMDG 211
|
250
....*....|....
gi 22327455 609 GEVAEKGTHDELLS 622
Cdd:COG1126 212 GRIVEEGPPEEFFE 225
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
71-342 |
8.78e-34 |
|
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: 130.71 E-value: 8.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 71 LVIGTIALLIGSTTNLLVPKFGGMIIDIVSRdVKTPEQQTESLIAVrnaVVIILLIVVIGSICTALRAWLFNSASERVVA 150
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLI-QLGPGGNTSLLLLL---VLGLAGAYVLSALLGILRGRLLARLGERITA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 151 RLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTaLIGVG-FMFTSSWKLTLLALVVVPV 229
Cdd:cd18563 77 DLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILM-IIGIGvVLFSLNWKLALLVLIPVPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 230 ISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNA 309
Cdd:cd18563 156 VVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTF 235
|
250 260 270
....*....|....*....|....*....|...
gi 22327455 310 AFTLSVITVVSYGAYLTIYGSMTVGALTSFILY 342
Cdd:cd18563 236 LTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSY 268
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
136-342 |
8.89e-34 |
|
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: 130.68 E-value: 8.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 136 LRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTS 215
Cdd:cd18550 58 VQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 216 SWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGA--VRTVRSFAKESYMVSQYSKKVDETLKLG 293
Cdd:cd18550 138 DWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLG 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22327455 294 LKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILY 342
Cdd:cd18550 218 VRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTAL 266
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
396-621 |
1.25e-33 |
|
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: 128.56 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISH---QYLHK 472
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 QISIVSQEPILF-NCSVEENIAYGFDgEasFTDIENAAKMANAHEFIEAfpdkyntvVGERGLR------LSGGQKQRIA 545
Cdd:COG1127 83 RIGMLFQGGALFdSLTVFENVAFPLR-E--HTDLSEAEIRELVLEKLEL--------VGLPGAAdkmpseLSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 546 IARALLTNPSVLLLDEATSALD----AESEYLVQDAMDSLmaGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDEL 620
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpitsAVIDELIRELRDEL--GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
.
gi 22327455 621 L 621
Cdd:COG1127 230 L 230
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
71-342 |
1.83e-33 |
|
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: 130.32 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 71 LVIGTIALLIGSTTNLLVP---KFggmIIDIVSRDVKTPEQQTESLIAVRN-------AVVIILLIVVIGSICTALRAWL 140
Cdd:cd18564 1 LALALLALLLETALRLLEPwplKV---VIDDVLGDKPLPGLLGLAPLLGPDplallllAAAALVGIALLRGLASYAGTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 141 FNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLT 220
Cdd:cd18564 78 TALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 221 LLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLV 300
Cdd:cd18564 158 LIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQ 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 22327455 301 GLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILY 342
Cdd:cd18564 238 ALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
397-592 |
1.99e-33 |
|
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: 126.99 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRPShmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSlmeISHQYLHKQISI 476
Cdd:cd03226 1 RIENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 477 VSQEP--ILFNCSVEENIAYGF-DGEASFTDIENAAKMANAHEFIEAFPdkyntvvgergLRLSGGQKQRIAIARALLTN 553
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGLkELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 22327455 554 PSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAH 592
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITH 184
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
396-621 |
3.93e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.18 E-value: 3.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRpSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEP--ILFNCSVEENIAYG-----FDGEASFTDIENAAKMANAHEFIEAFPdkyntvvgergLRLSGGQKQRIAIAR 548
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGlenkkVPPKKMKDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 549 ALLTNPSVLLLDEATSALDAESEYLVQDAMDSL--MAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELL 621
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
395-620 |
8.55e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.45 E-value: 8.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 395 DVELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVslmEISHQYLHK-Q 473
Cdd:COG3842 5 ALELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR---DVTGLPPEKrN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 474 ISIVSQEPILF-NCSVEENIAYG--FDGEASfTDIEnaAKMANAHEF--IEAFPDKYntvVGErglrLSGGQKQRIAIAR 548
Cdd:COG3842 79 VGMVFQDYALFpHLTVAENVAFGlrMRGVPK-AEIR--ARVAELLELvgLEGLADRY---PHQ----LSGGQQQRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 549 ALLTNPSVLLLDEATSALDAEseyLVQDAMDSLMA-----GRTVLVIAHRLS---TVktADCVAVISDGEVAEKGTHDEL 620
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAK---LREEMREELRRlqrelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
70-342 |
9.04e-32 |
|
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: 124.89 E-value: 9.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 70 KLVIGTIALLIGSTTNLLVPKFGGMIID--IVSRDVKtpeqqteSLIAVrnaVVIILLIVVIGSICTALRAWLFNSASER 147
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDeyIPNGDLS-------GLLII---ALLFLALNLVNWVASRLRIYLMAKVGQR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 148 VVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTaLIG-VGFMFTSSWKLTLLALVV 226
Cdd:cd18545 71 ILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLT-LVGiVIIMFSLNVRLALVTLAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 227 VPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGG 306
Cdd:cd18545 150 LPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPL 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 22327455 307 LNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILY 342
Cdd:cd18545 230 VELISALGTALVYWYGGKLVLGGAITVGVLVAFIGY 265
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
397-615 |
1.09e-31 |
|
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: 121.39 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISI 476
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 477 VSQepilfncsveeniaygfdgeasftdienAAKMANAHEFIEAFpdkYNTvvgerglrLSGGQKQRIAIARALLTNPSV 556
Cdd:cd03214 78 VPQ----------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327455 557 LLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLS-TVKTADCVAVISDGEVAEKG 615
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
396-621 |
2.88e-31 |
|
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: 122.02 E-value: 2.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRpsHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:cd03295 1 IEFENVTKRYGGG--KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILF-NCSVEENIAY-----GFDGEASFTDIENAAKMAN--AHEFIEAFPDKyntvvgerglrLSGGQKQRIAIA 547
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALvpkllKWPKEKIRERADELLALVGldPAEFADRYPHE-----------LSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 548 RALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRL-STVKTADCVAVISDGEVAEKGTHDELL 621
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
396-624 |
4.04e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.82 E-value: 4.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYP--SRPShmiLKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQ 473
Cdd:PRK13635 6 IRVEHISFRYPdaATYA---LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 474 ISIVSQEP--ILFNCSVEENIAYGFDG-----EASFTDIENAAKMANAHEFIEAFPDkyntvvgerglRLSGGQKQRIAI 546
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLENigvprEEMVERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 547 ARALLTNPSVLLLDEATSALDAE--SEYL--VQDAMDSLMAgrTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRgrREVLetVRQLKEQKGI--TVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
..
gi 22327455 623 LN 624
Cdd:PRK13635 230 SG 231
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
71-343 |
1.37e-30 |
|
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: 121.74 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 71 LVIGTIALLIGSTTNLLVPKFGGMIIDIVSRDVKTPEQQteSLIAVRNAVVIILLIVVIGSICTALRAWLFNSASERVVA 150
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGV--DFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 151 RLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVI 230
Cdd:cd18547 79 DLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 231 SVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDEtlklgLKQAVLVGLFFGGLNAA 310
Cdd:cd18547 159 LLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEE-----LYKASFKAQFYSGLLMP 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 22327455 311 FT-----LSVITVVSYGAYLTIYGSMTVGALTSFILYS 343
Cdd:cd18547 234 IMnfinnLGYVLVAVVGGLLVINGALTVGVIQAFLQYS 271
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
413-620 |
1.55e-30 |
|
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: 119.65 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEI-SHQylhKQISIVSQEPILF-NCSVEE 490
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLpPHK---RPVNTVFQNYALFpHLTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 491 NIAYGF-----DGEASFTDIENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQRIAIARALLTNPSVLLLDEATSA 565
Cdd:cd03300 92 NIAFGLrlkklPKAEIKERVAEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 566 LDAESEYLVQDAMDSL--MAGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDEL 620
Cdd:cd03300 161 LDLKLRKDMQLELKRLqkELGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEI 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
401-622 |
1.96e-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: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 401 VWFAYPSRPSHmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPL---KGKILLNGVSLMEISH----QYLHKQ 473
Cdd:COG0444 9 VYFPTRRGVVK-AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEkelrKIRGRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 474 ISIVSQEPilFNC-----SVEENIAYGFD--GEASFTDIENAAK-------MANAHEFIEAFPdkyntvvGErglrLSGG 539
Cdd:COG0444 88 IQMIFQDP--MTSlnpvmTVGDQIAEPLRihGGLSKAEARERAIellervgLPDPERRLDRYP-------HE----LSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 540 QKQRIAIARALLTNPSVLLLDEATSALDAeseyLVQ----DAMDSLMA--GRTVLVIAHRLSTVK-TADCVAVISDGEVA 612
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDV----TIQaqilNLLKDLQRelGLAILFITHDLGVVAeIADRVAVMYAGRIV 230
|
250
....*....|
gi 22327455 613 EKGTHDELLS 622
Cdd:COG0444 231 EEGPVEELFE 240
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
71-342 |
5.11e-30 |
|
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: 120.19 E-value: 5.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 71 LVIGTIALLIGSTTNLLVPKFGGMIIDivsRDVKTPEQQTESLIavrNAVVIILLIVVIGSICTALRAWLFNSASERVVA 150
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAID---DYIVPGQGDLQGLL---LLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 151 RLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTaLIGV-GFMFTSSWKLTLLALVVVPV 229
Cdd:cd18544 75 DLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLL-LIGIlIAMFLLNWRLALISLLVLPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 230 ISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNA 309
Cdd:cd18544 154 LLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVEL 233
|
250 260 270
....*....|....*....|....*....|...
gi 22327455 310 AFTLSVITVVSYGAYLTIYGSMTVGALTSFILY 342
Cdd:cd18544 234 LSSLALALVLWYGGGQVLSGAVTLGVLYAFIQY 266
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
414-615 |
6.79e-30 |
|
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: 117.40 E-value: 6.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRL---TPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEiSHQYLH-----KQISIVSQEPILF- 484
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD-SRKKINlppqqRKIGLVFQQYALFp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 485 NCSVEENIAYGFDGEASFTDIENAAKMA---NAHEFIEAFPDKyntvvgerglrLSGGQKQRIAIARALLTNPSVLLLDE 561
Cdd:cd03297 89 HLNVRENLAFGLKRKRNREDRISVDELLdllGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 562 ATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKG 615
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
413-622 |
8.39e-30 |
|
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: 117.15 E-value: 8.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEI-SHQYLHKQISIVSQEPILF-NCSVEE 490
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERARAGIGYVPEGRRIFpELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 491 NI---AYGFDGEASFTDIEnaakmanahEFIEAFP---DKYNTVVGErglrLSGGQKQRIAIARALLTNPSVLLLDEATS 564
Cdd:cd03224 95 NLllgAYARRRAKRKARLE---------RVYELFPrlkERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 565 ALdaeSEYLVQDAMDSLMA----GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:cd03224 162 GL---APKIVEEIFEAIRElrdeGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
414-621 |
1.64e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 119.87 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLI---ERfydPLKGKILLNGVSLMeISHQYLHKQISIVSQEPILF-NCSVE 489
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIaglET---PDSGRIVLNGRDLF-TNLPPRERRVGFVFQHYALFpHMTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 490 ENIAYGFD-GEASFTDIEnaakmANAHEFIEAfpdkyntvVGERGL--R----LSGGQKQRIAIARALLTNPSVLLLDEA 562
Cdd:COG1118 94 ENIAFGLRvRPPSKAEIR-----ARVEELLEL--------VQLEGLadRypsqLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 563 TSALDAeseYLVQDAMDSLMA-----GRTVLVIAH------RLstvktADCVAVISDGEVAEKGTHDELL 621
Cdd:COG1118 161 FGALDA---KVRKELRRWLRRlhdelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVY 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
388-622 |
2.11e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 124.85 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 388 PVGNPD-GDVELNDVWFAY-PSRPShmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEI 465
Cdd:PLN03130 1229 PPGWPSsGSIKFEDVVLRYrPELPP--VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 466 SHQYLHKQISIVSQEPILFNCSVEENIaygfD--GEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQR 543
Cdd:PLN03130 1307 GLMDLRKVLGIIPQAPVLFSGTVRFNL----DpfNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQL 1382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 544 IAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PLN03130 1383 LSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
413-615 |
4.81e-29 |
|
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: 114.19 E-value: 4.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLI--ERFYDPLKGKILLNGVSLMEIShqyLHKQISIVSQEPILFNC-SVE 489
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRS---FRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 490 ENIAYgfdgeasftdienAAKManahefieafpdkyntvvgeRGlrLSGGQKQRIAIARALLTNPSVLLLDEATSALDAE 569
Cdd:cd03213 101 ETLMF-------------AAKL--------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22327455 570 SEYLVqdaMDSLMA----GRTVLVIAHRLST--VKTADCVAVISDGEVAEKG 615
Cdd:cd03213 146 SALQV---MSLLRRladtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
396-611 |
9.10e-29 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 115.15 E-value: 9.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRpsHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHK--- 472
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 QISIVSQEPILF-NCSVEENIAYGFDGEASF----------TDIENAakmanaHEFIEAF--PDKYNtvvgERGLRLSGG 539
Cdd:COG3638 81 RIGMIFQQFNLVpRLSVLTNVLAGRLGRTSTwrsllglfppEDRERA------LEALERVglADKAY----QRADQLSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 540 QKQRIAIARALLTNPSVLLLDEATSALDAES-----EYLVQDAMDSlmaGRTVLVIAHRLSTVKT-ADCVAVISDGEV 611
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTarqvmDLLRRIARED---GITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
417-621 |
9.44e-29 |
|
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: 115.82 E-value: 9.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 417 ISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYL----HKQISIVSQEPILF-NCSVEEN 491
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 492 IAYGFD--GEASFTDIENAAK---MANAHEFIEAFPDKyntvvgerglrLSGGQKQRIAIARALLTNPSVLLLDEATSAL 566
Cdd:cd03294 123 VAFGLEvqGVPRAEREERAAEaleLVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327455 567 DAeseyLVQDAM-DSLMA-----GRTVLVIAHRLS-TVKTADCVAVISDGEVAEKGTHDELL 621
Cdd:cd03294 192 DP----LIRREMqDELLRlqaelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
132-370 |
1.52e-28 |
|
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: 115.66 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 132 ICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKnAATTNLSEALRNVTTALIGVGF 211
Cdd:cd18543 54 VLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQ-RFLAFGPFLLGNLLTLVVGLVV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 212 MFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLK 291
Cdd:cd18543 133 MLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRA 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 292 LGLKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:cd18543 213 TRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
261-632 |
1.77e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 122.01 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 261 ESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAafTLSVITVVSYGAYLTIYGSMTVG-ALTSF 339
Cdd:PLN03232 484 EILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNS--IPVVVTLVSFGVFVLLGGDLTPArAFTSL 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 340 ILYSLtVGSSVSSLSSLYTTAMKAAGASRRVFQILDRVSSMSSSGDKCPVGNPDgdVELNDVWFAYPSRPSHMILKGISL 419
Cdd:PLN03232 562 SLFAV-LRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGAPA--ISIKNGYFSWDSKTSKPTLSDINL 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 420 RLTPGSKVALVGPSGGGKTTIANlierfydplkgkILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIAYGFDGE 499
Cdd:PLN03232 639 EIPVGSLVAIVGGTGEGKTSLIS------------AMLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFE 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 500 ASftDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDA-M 578
Cdd:PLN03232 707 SE--RYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScM 784
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 22327455 579 DSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLSLNGIYTNLVK 632
Cdd:PLN03232 785 KDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLME 838
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
414-616 |
3.11e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 116.05 E-value: 3.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTT---IANLIERfydPLKGKILLNGVSLMEISHQYLHK---QISIVSQEpilFNC- 486
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKarrQIGMIFQH---FNLl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 ---SVEENIAygFDGEASFT---DIEnaakmANAHEFIE-----AFPDKYNTvvgerglRLSGGQKQRIAIARALLTNPS 555
Cdd:PRK11153 95 ssrTVFDNVA--LPLELAGTpkaEIK-----ARVTELLElvglsDKADRYPA-------QLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 556 VLLLDEATSALDAESeylvQDAMDSLMA------GRTVLVIAHRLSTVK-TADCVAVISDGEVAEKGT 616
Cdd:PRK11153 161 VLLCDEATSALDPAT----TRSILELLKdinrelGLTIVLITHEMDVVKrICDRVAVIDAGRLVEQGT 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
397-620 |
3.61e-28 |
|
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: 113.05 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSrpSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLH---KQ 473
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 474 ISIVSQEPILFN-CSVEENIAYGFDGEASFtdIENAAKMANAHEFIEAFP--------DKYNTVVGErglrLSGGQKQRI 544
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRLGRRST--WRSLFGLFPKEEKQRALAalervgllDKAYQRADQ----LSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 545 AIARALLTNPSVLLLDEATSALDAES-----EYLVQDAMDSlmaGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHD 618
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASsrqvmDLLKRINREE---GITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPA 230
|
..
gi 22327455 619 EL 620
Cdd:cd03256 231 EL 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
416-620 |
3.66e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 115.60 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 416 GISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYL---HKQISIVSQEPilFNC-----S 487
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP--YASlnprmT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 488 VEENIAYGFDgeaSFTDIENAAKMANAHEFIEafpdkynTVvgerGLR----------LSGGQKQRIAIARALLTNPSVL 557
Cdd:COG4608 114 VGDIIAEPLR---IHGLASKAERRERVAELLE-------LV----GLRpehadrypheFSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 558 LLDEATSALD----AESEYLVQDAMDSLmaGRTVLVIAHRLSTVK-TADCVAVISDGEVAEKGTHDEL 620
Cdd:COG4608 180 VCDEPVSALDvsiqAQVLNLLEDLQDEL--GLTYLFISHDLSVVRhISDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
396-611 |
1.04e-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: 111.08 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDV--WFAypsrpSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLmEISHQYLH-- 471
Cdd:cd03262 1 IEIKNLhkSFG-----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINel 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 472 -KQISIVSQEPILF-NCSVEENIAYGF-------DGEASFTDIENAAKMANAHeFIEAFPDkyntvvgerglRLSGGQKQ 542
Cdd:cd03262 75 rQKVGMVFQQFNLFpHLTVLENITLAPikvkgmsKAEAEERALELLEKVGLAD-KADAYPA-----------QLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 543 RIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEV 611
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
410-620 |
1.12e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 112.44 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 410 SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYD--P---LKGKILLNG-------VSLMEishqyLHKQISIV 477
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGediydpdVDVVE-----LRRRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 478 SQEPILFNCSVEENIAYGF--DGEASFTDI----ENAAKMAnahefieAFPDKYNTVVGERGLRLSGGQKQRIAIARALL 551
Cdd:COG1117 98 FQKPNPFPKSIYDNVAYGLrlHGIKSKSELdeivEESLRKA-------ALWDEVKDRLKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 552 TNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAH------RLStvktaDCVAVISDGEVAEKGTHDEL 620
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
410-621 |
1.52e-27 |
|
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: 111.10 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 410 SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVslmEISHQYLHKQ----ISIVSQEPILF- 484
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ---DITKLPMHKRarlgIGYLPQEASIFr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 485 NCSVEENIaygfDGEASFTDIENAAKMANAHEFIEAFpdKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATS 564
Cdd:cd03218 89 KLTVEENI----LAVLEIRGLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327455 565 ALD----AESEYLVQDAMDSlmaGRTVLVIAHRLS-TVKTADCVAVISDGEVAEKGTHDELL 621
Cdd:cd03218 163 GVDpiavQDIQKIIKILKDR---GIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
414-632 |
1.55e-27 |
|
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: 119.28 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGvslmeishqylhkQISIVSQEPILFNCSVEENIA 493
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 494 YGFDGEASF--TDIENAAKMANahefIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAE-S 570
Cdd:TIGR00957 721 FGKALNEKYyqQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvG 796
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 571 EYLVQDAM--DSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLSLNGIYTNLVK 632
Cdd:TIGR00957 797 KHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLR 860
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
417-622 |
1.55e-27 |
|
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: 114.44 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 417 ISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEiSHQYL----HKQ-ISIVSQEPILF-NCSVEE 490
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD-SRKGIflppEKRrIGYVFQEARLFpHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 491 NIAYGF---DGEASFTDIENAAKMANAHEFIEAFPDkyntvvgerglRLSGGQKQRIAIARALLTNPSVLLLDEATSALD 567
Cdd:TIGR02142 95 NLRYGMkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 568 AESEYLVQDAMDSLMA--GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:TIGR02142 164 DPRKYEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
396-615 |
1.90e-27 |
|
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: 110.28 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPSHMILKgislrLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSL--MEISHqylhKQ 473
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLT-----FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtaAPPAD----RP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 474 ISIVSQEPILF-NCSVEENIAYGFDGEASFTD-----IENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQRIAIA 547
Cdd:cd03298 72 VSMLFQENNLFaHLTVEQNVGLGLSPGLKLTAedrqaIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 548 RALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGR--TVLVIAHRLSTV-KTADCVAVISDGEVAEKG 615
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAkRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
72-342 |
3.79e-27 |
|
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: 111.86 E-value: 3.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 72 VIGTIALLIGST-TNLLVPKFGGMIIDIVsrdvktpEQQTESLIAVRNAVVIILLIVVIGSICTALRAWLFNSASERVVA 150
Cdd:cd18778 1 LILTLLCALLSTlLGLVPPWLIRELVDLV-------TIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 151 RLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAattnLSEALRNVTTA---LIGVG-FMFTSSWKLTLLALVV 226
Cdd:cd18778 74 DLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERL----IADGIPQGITNvltLVGVAiILFSINPKLALLTLIP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 227 VPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGG 306
Cdd:cd18778 150 IPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPL 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 22327455 307 LNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILY 342
Cdd:cd18778 230 MEFLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLY 265
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
394-568 |
5.09e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.86 E-value: 5.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 394 GDVELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNG--VSLMEISHqylh 471
Cdd:COG3839 2 ASLELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdVTDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 472 KQISIVSQEPILF-NCSVEENIAYG-----FDGEasftDIE----NAAKMANahefIEAFPDKYntvVGErglrLSGGQK 541
Cdd:COG3839 75 RNIAMVFQSYALYpHMTVYENIAFPlklrkVPKA----EIDrrvrEAAELLG----LEDLLDRK---PKQ----LSGGQR 139
|
170 180
....*....|....*....|....*..
gi 22327455 542 QRIAIARALLTNPSVLLLDEATSALDA 568
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDA 166
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
414-620 |
1.24e-26 |
|
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: 108.58 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGvslMEISHQYLHK-QISIVSQEPILF-NCSVEEN 491
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQErNVGFVFQHYALFrHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 492 IAYGFDGEASFTDIENAAKMANAHEFI-----EAFPDKYNTvvgerglRLSGGQKQRIAIARALLTNPSVLLLDEATSAL 566
Cdd:cd03296 95 VAFGLRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 567 DAESEYLVQDAMDSL---MAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDEL 620
Cdd:cd03296 168 DAKVRKELRRWLRRLhdeLHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
396-592 |
1.37e-26 |
|
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: 107.56 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTT----IANLIErfydPLKGKILLNGVSLMEISHQYlH 471
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRDAREDY-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 472 KQISIVSQEPILF-NCSVEENIAY--GFDGEAsftdienaAKMANAHEFIEAFpdkyntvvgerGLR---------LSGG 539
Cdd:COG4133 75 RRLAYLGHADGLKpELTVRENLRFwaALYGLR--------ADREAIDEALEAV-----------GLAgladlpvrqLSAG 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22327455 540 QKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDS-LMAGRTVLVIAH 592
Cdd:COG4133 136 QKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
140-370 |
1.82e-26 |
|
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: 109.48 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 140 LFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKL 219
Cdd:cd18589 59 IYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 220 TLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVL 299
Cdd:cd18589 139 ALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAA 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 300 --VGLFFGGLNAAFtLSViTVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:cd18589 219 yaVSMWTSSFSGLA-LKV-GILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
396-615 |
2.65e-26 |
|
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: 106.89 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRpshMILKGISLRLTPGSkVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEiSHQYLHKQIS 475
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILF-NCSVEENIAYgfdgEASFTDIENAAKMANAHEFIEA--FPDKYNTVVGErglrLSGGQKQRIAIARALLT 552
Cdd:cd03264 76 YLPQEFGVYpNFTVREFLDY----IAWLKGIPSKEVKARVDEVLELvnLGDRAKKKIGS----LSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 553 NPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVK-TADCVAVISDGEVAEKG 615
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
414-622 |
9.90e-26 |
|
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: 105.98 E-value: 9.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVslmEIS----HQYLHKQISIVSQEPILF-NCSV 488
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE---DITglppHEIARLGIGRTFQIPRLFpELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENI---AYGFDGEASFTDI---ENAAKMANAHEFIEAF--PDKYNTVVGErglrLSGGQKQRIAIARALLTNPSVLLLD 560
Cdd:cd03219 93 LENVmvaAQARTGSGLLLARarrEEREARERAEELLERVglADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 561 EATSALDAEseyLVQDAMDSLMA----GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:cd03219 169 EPAAGLNPE---ETEELAELIRElrerGITVLLVEHDMDVVmSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
412-631 |
1.09e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 113.34 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 412 MILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEEN 491
Cdd:PTZ00243 1324 LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 492 IaygfDG--EASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPS-VLLLDEATSALDA 568
Cdd:PTZ00243 1404 V----DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDP 1479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 569 ESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDEL-LSLNGIYTNLV 631
Cdd:PTZ00243 1480 ALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
396-611 |
1.26e-25 |
|
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: 105.18 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPsrPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQ---YLHK 472
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 QISIVSQE-PILFNCSVEENIAYGFD-GEASFTDIENAAKMANAHEFIEafpDKYNTVVGErglrLSGGQKQRIAIARAL 550
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEvTGVPPREIRKRVPAALELVGLS---HKHRALPAE----LSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 551 LTNPSVLLLDEATSALDAESEYLVQDAMDSL-MAGRTVLVIAHRLSTV-KTADCVAVISDGEV 611
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
396-615 |
1.65e-25 |
|
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: 104.64 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQylHKQIS 475
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILF-NCSVEENIAYG-----FDGEASFTDIENAAKMANahefIEAFPDKYNTvvgerglRLSGGQKQRIAIARA 549
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlklrkVPKDEIDERVREVAELLQ----IEHLLDRKPK-------QLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 550 LLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKG 615
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
396-621 |
2.48e-25 |
|
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: 105.17 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKG---KIL---LNGVSLMEIshqy 469
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 470 lHKQISIVS---QEPILFNCSVEENIAYGFDG------EASFTDIENAAKMAnaHEF-IEAFPDK-YNTvvgerglrLSG 538
Cdd:COG1119 77 -RKRIGLVSpalQLRFPRDETVLDVVLSGFFDsiglyrEPTDEQRERARELL--ELLgLAHLADRpFGT--------LSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 539 GQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLStvktaDCVAVIS------DGE 610
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVE-----EIPPGIThvlllkDGR 220
|
250
....*....|.
gi 22327455 611 VAEKGTHDELL 621
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
398-592 |
5.65e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.00 E-value: 5.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 398 LNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGvslmeishqylHKQISIV 477
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 478 SQEPILF-NCSVEENIAYGFDG-----------EASFTDI-ENAAKMANAHEFIEA------------------FP-DKY 525
Cdd:COG0488 67 PQEPPLDdDLTVLDTVLDGDAElraleaeleelEAKLAEPdEDLERLAELQEEFEAlggweaearaeeilsglgFPeEDL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327455 526 NTVVGErglrLSGGQKQRIAIARALLTNPSVLLLDEATSALDAES-----EYLVQdamdslMAGrTVLVIAH 592
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKN------YPG-TVLVVSH 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
396-636 |
5.70e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.20 E-value: 5.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEP--ILFNCSVEENIAYGFDGEA-SFTDIENAAKMANAHEFIEAFPDKYNTvvgerglRLSGGQKQRIAIARALLT 552
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGiPHEEMKERVNEALELVGMQDFKEREPA-------RLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 553 NPSVLLLDEATSALDAESEY----LVQDAMDSLmaGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDEL-------- 620
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLelikTIKGIRDDY--QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELfsrgndll 235
|
250
....*....|....*..
gi 22327455 621 -LSLNGIYTNLVKRQLQ 636
Cdd:PRK13650 236 qLGLDIPFTTSLVQSLR 252
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
397-592 |
5.73e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.56 E-value: 5.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYP-SRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVslmeishqylhkQIS 475
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV------------PVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 -------IVSQEPILFN-CSVEENIAYGFdgeaSFTDIENAAKMANAHEFIEAfpdkyntvVGERGL------RLSGGQK 541
Cdd:COG4525 73 gpgadrgVVFQKDALLPwLNVLDNVAFGL----RLRGVPKAERRARAEELLAL--------VGLADFarrriwQLSGGMR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 542 QRIAIARALLTNPSVLLLDEATSALDAeseyLVQDAMDSLM------AGRTVLVIAH 592
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDA----LTREQMQELLldvwqrTGKGVFLITH 193
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
414-615 |
6.17e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.09 E-value: 6.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYD-----PLKGKILLNGVSLM--EISHQYLHKQISIVSQEPILFNC 486
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYspRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 SVEENIAYGF------DGEASFTDIENAAKMAnahefieAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLD 560
Cdd:PRK14239 101 SIYENVVYGLrlkgikDKQVLDEAVEKSLKGA-------SIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 561 EATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTV-KTADCVAVISDGEVAEKG 615
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYN 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
410-567 |
6.19e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.96 E-value: 6.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 410 SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQylHKQISIVSQEPILF-NCSV 488
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYGFDGE-ASFTDIE----NAAKMANAHEFIEAFPdkyntvvgergLRLSGGQKQRIAIARALLTNPSVLLLDEAT 563
Cdd:PRK09452 104 FENVAFGLRMQkTPAAEITprvmEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
....
gi 22327455 564 SALD 567
Cdd:PRK09452 173 SALD 176
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
414-622 |
7.13e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.43 E-value: 7.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLH----KQISIVSQE-PILFNCSV 488
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSfALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYGFD-----GEASFTDIENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQRIAIARALLTNPSVLLLDEAT 563
Cdd:PRK10070 124 LDNTAFGMElaginAEERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327455 564 SALDAESEYLVQDAMDSLMAG--RTVLVIAHRL-STVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
396-622 |
1.20e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 102.74 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPSHMilkgiSLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGvslmeISHQYL---HK 472
Cdd:PRK10771 2 LKLTDITWLYHHLPMRF-----DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG-----QDHTTTppsRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 QISIVSQEPILFN-CSVEENIAYGFD--------GEASFTDIenAAKMAnAHEFIEAFPDKyntvvgerglrLSGGQKQR 543
Cdd:PRK10771 72 PVSMLFQENNLFShLTVAQNIGLGLNpglklnaaQREKLHAI--ARQMG-IEDLLARLPGQ-----------LSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 544 IAIARALLTNPSVLLLDEATSALD----AESEYLVQDAMDSlmAGRTVLVIAHRLS-TVKTADCVAVISDGEVAEKGTHD 618
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQE--RQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTD 215
|
....
gi 22327455 619 ELLS 622
Cdd:PRK10771 216 ELLS 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
396-609 |
1.35e-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: 102.41 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPShmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQ-- 473
Cdd:cd03290 1 VQVTNGYFSWGSGLA--TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 474 --ISIVSQEPILFNCSVEENIAYG--FDGEASFTDIENAAKMANahefIEAFPDKYNTVVGERGLRLSGGQKQRIAIARA 549
Cdd:cd03290 79 ysVAYAAQKPWLLNATVEENITFGspFNKQRYKAVTDACSLQPD----IDLLPFGDQTEIGERGINLSGGQRQRICVARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 550 LLTNPSVLLLDEATSALDAE-SEYLVQDAMDSLMAG--RTVLVIAHRLSTVKTADCVAVISDG 609
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
397-622 |
1.71e-24 |
|
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: 102.37 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPsrPSHmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEIS-HQYLHKQIS 475
Cdd:COG0410 5 EVENLHAGYG--GIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILF-NCSVEENI---AYGFDGEASFtdienAAKMANAHEFieaFPdkyntVVGER----GLRLSGGQKQRIAIA 547
Cdd:COG0410 82 YVPEGRRIFpSLTVEENLllgAYARRDRAEV-----RADLERVYEL---FP-----RLKERrrqrAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 548 RALLTNPSVLLLDEATSALdaeSEYLVQDAMDSLMA----GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGL---APLIVEEIFEIIRRlnreGVTILLVEQNARFAlEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
383-622 |
1.96e-24 |
|
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: 107.46 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 383 SGDKCPVGnPDGDV--ELND--VWFAYP-----SRPSHM-ILKGISLRLTPGSKVALVGPSGGGKTTIA----NLIerfy 448
Cdd:COG4172 262 RGDPRPVP-PDAPPllEARDlkVWFPIKrglfrRTVGHVkAVDGVSLTLRRGETLGLVGESGSGKSTLGlallRLI---- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 449 dPLKGKILLNGVSLMEISH---QYLHKQISIVSQEPilFNC-----SVEENIAYGF---DGEASFTDIENAAKMANA--- 514
Cdd:COG4172 337 -PSEGEIRFDGQDLDGLSRralRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGLrvhGPGLSAAERRARVAEALEevg 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 515 ----------HEFieafpdkyntvvgerglrlSGGQKQRIAIARALLTNPSVLLLDEATSALDAeseyLVQDAMDSLMA- 583
Cdd:COG4172 414 ldpaarhrypHEF-------------------SGGQRQRIAIARALILEPKLLVLDEPTSALDV----SVQAQILDLLRd 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 22327455 584 -----GRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDELLS 622
Cdd:COG4172 471 lqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
393-622 |
2.15e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.34 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 393 DGDVELNDVWFAYPSRPShMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDP---LKGKILLNGVSLMEISHQY 469
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 470 LHKQISIVSQEP--ILFNCSVEENIAYGFDGEA-----SFTDIENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQ 542
Cdd:PRK13640 82 IREKVGIVFQNPdnQFVGATVGDDVAFGLENRAvprpeMIKIVRDVLADVGMLDYIDSEPAN-----------LSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 543 RIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDEL 620
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
..
gi 22327455 621 LS 622
Cdd:PRK13640 231 FS 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
396-620 |
2.30e-24 |
|
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: 101.81 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPSHmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQyLHKQIS 475
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA-ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILF-NCSVEENIAYgfdgEASFTDIENAAKMANAHEFIEAF--PDKYNTVVGErglrLSGGQKQRIAIARALLT 552
Cdd:cd03263 79 YCPQFDALFdELTVREHLRF----YARLKGLPKSEIKEEVELLLRVLglTDKANKRART----LSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 553 NPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAH------RLstvktADCVAVISDGEVAEKGTHDEL 620
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeaeAL-----CDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
411-622 |
2.34e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.52 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 411 HMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSL---MEISHQ-----YLHKQISIVSQEPI 482
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQkglirQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 483 LF-NCSVEENIaygFDGEASFTDIENAAKMANAHEFI---------EAFPDkyntvvgerglRLSGGQKQRIAIARALLT 552
Cdd:PRK11264 96 LFpHRTVLENI---IEGPVIVKGEPKEEATARARELLakvglagkeTSYPR-----------RLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 553 NPSVLLLDEATSALDAEseyLVQDAMDSLMA----GRTVLVIAHRLSTVK-TADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK11264 162 RPEVILFDEPTSALDPE---LVGEVLNTIRQlaqeKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
413-622 |
4.07e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.01 E-value: 4.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQ-----EPIlfncS 487
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQhhltpEGI----T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 488 VEENIAYG------FDGEASFTD---IENAakMANAHefIEAFPDKyntvvgeRGLRLSGGQKQRIAIARALLTNPSVLL 558
Cdd:PRK11231 93 VRELVAYGrspwlsLWGRLSAEDnarVNQA--MEQTR--INHLADR-------RLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 559 LDEATSALDAESEYLVQDAMDSL-MAGRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
413-622 |
4.19e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 101.32 E-value: 4.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLM--EISHQYLHKQISIVSQEPILF-NCSVE 489
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFpHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 490 ENIAYGFdgeasfTDIENAAKmANAHEFIEAFPDKyntvVG--ERG----LRLSGGQKQRIAIARALLTNPSVLLLDEAT 563
Cdd:PRK09493 96 ENVMFGP------LRVRGASK-EEAEKQARELLAK----VGlaERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 564 SALDAESEYLVQDAMDSLM-AGRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK09493 165 SALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
396-615 |
6.60e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.74 E-value: 6.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSrpSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEP--ILFNCSVEENIAYG-----FDGEASFTDIENAAKMANAHEFIEAFPdkyntvvgergLRLSGGQKQRIAIAR 548
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 549 ALLTNPSVLLLDEATSALDAESEYLVQDAMDSL-MAGRTVLVIAHRLS-TVKTADCVAVISDGEVAEKG 615
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
414-623 |
7.61e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.49 E-value: 7.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNG--VSLMEIsHQYLHKQISIVSQEPILF-NCSVEE 490
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP-RDAQAAGIAIIHQELNLVpNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 491 NIAYGFdgEASFTDIENAAKM-ANAHEFIEAF-----PDkynTVVGErglrLSGGQKQRIAIARALLTNPSVLLLDEATS 564
Cdd:COG1129 99 NIFLGR--EPRRGGLIDWRAMrRRARELLARLgldidPD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 565 AL-DAESEYLVqDAMDSLMA-GRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKG-----THDELLSL 623
Cdd:COG1129 170 SLtEREVERLF-RIIRRLKAqGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVRL 235
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
407-569 |
7.81e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.86 E-value: 7.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 407 SRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDP---LKGKILLNGVSLMEIshQYLHKQISIVSQEPIL 483
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAL--PAEQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 484 F-NCSVEENIAYG----FDGEASFTDIENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQRIAIARALLTNPSVLL 558
Cdd:COG4136 88 FpHLSVGENLAFAlpptIGRAQRRARVEQALEEAGLAGFADRDPAT-----------LSGGQRARVALLRALLAEPRALL 156
|
170
....*....|.
gi 22327455 559 LDEATSALDAE 569
Cdd:COG4136 157 LDEPFSKLDAA 167
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
417-622 |
1.22e-23 |
|
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: 102.87 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 417 ISLRLTPGSKVALVGPSGGGKTTIANLI---ERfydPLKGKILLNGVSLMEISH-QYL--HK-QISIVSQEPILF-NCSV 488
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEVLQDSARgIFLppHRrRIGYVFQEARLFpHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYGF---DGEASFTDIENAAKMANAHEFIEAFPDkyntvvgerglRLSGGQKQRIAIARALLTNPSVLLLDEATSA 565
Cdd:COG4148 95 RGNLLYGRkraPRAERRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 566 LDAES-----EYL--VQDAMDslmagRTVLVIAH------RLstvktADCVAVISDGEVAEKGTHDELLS 622
Cdd:COG4148 164 LDLARkaeilPYLerLRDELD-----IPILYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLS 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
414-619 |
1.34e-23 |
|
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: 100.50 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEIS-HQYLHKQISIVSQEPILF-NCSVEEN 491
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpHRIARLGIARTFQNPRLFpELTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 492 I---AYGFDGEASFTDI--------ENAAKMANAHEFIEAF--PDKYNTVVGErglrLSGGQKQRIAIARALLTNPSVLL 558
Cdd:COG0411 100 VlvaAHARLGRGLLAALlrlprarrEEREARERAEELLERVglADRADEPAGN----LSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 559 LDEATSAL-DAESEYLVqDAMDSLMA--GRTVLVIAHRLSTV-KTADCVAVISDGEV-AEkGTHDE 619
Cdd:COG0411 176 LDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVmGLADRIVVLDFGRViAE-GTPAE 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
413-622 |
1.51e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 100.37 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIAN----LIERFYDP-LKGKILLNGVSLMEISHQYLHKQISIVSQEP-ILFNC 486
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEArVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 SVEENIAYGFDGE---ASFTDIENAAKMA-NAHEFIEAFPDKYNTVVGerglRLSGGQKQRIAIARALLTNPSVLLLDEA 562
Cdd:PRK14247 98 SIFENVALGLKLNrlvKSKKELQERVRWAlEKAQLWDEVKDRLDAPAG----KLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 563 TSALDAESEYLVQDAMDSLMAGRTVLVIAH-RLSTVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
396-622 |
1.71e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.60 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPShMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:PRK13648 8 IVFKNVSFQYQSDAS-FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEP--ILFNCSVEENIAYGFDGEASFTD-----IENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQRIAIAR 548
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENHAVPYDemhrrVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 549 ALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGR--TVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
315-625 |
1.97e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 105.98 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 315 VITVVSYGAYLTIYGSMT-VGALTSFILYSltVGSSVSSLSSLYTTAMKAAGASrrvfqiLDRVSSMSSSGDKCPVGNPD 393
Cdd:PLN03130 536 LVTVVSFGVFTLLGGDLTpARAFTSLSLFA--VLRFPLFMLPNLITQAVNANVS------LKRLEELLLAEERVLLPNPP 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 394 GDVEL-----NDVWFAYPSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIerfydplkgkilLNGVSLMEISHQ 468
Cdd:PLN03130 608 LEPGLpaisiKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM------------LGELPPRSDASV 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 469 YLHKQISIVSQEPILFNCSVEENIAYGFDGEASftDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIAR 548
Cdd:PLN03130 676 VIRGTVAYVPQVSWIFNATVRDNILFGSPFDPE--RYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMAR 753
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 549 ALLTNPSVLLLDEATSALDAESEYLVQDA--MDSLMAGRTVLVI--AHRLSTVktaDCVAVISDGEVAEKGTHDELLSlN 624
Cdd:PLN03130 754 AVYSNSDVYIFDDPLSALDAHVGRQVFDKciKDELRGKTRVLVTnqLHFLSQV---DRIILVHEGMIKEEGTYEELSN-N 829
|
.
gi 22327455 625 G 625
Cdd:PLN03130 830 G 830
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
398-611 |
2.85e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 99.37 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 398 LNDVWFAYPSRpshMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEIShqylhKQISIV 477
Cdd:PRK11247 15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR-----EDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 478 SQEPILFNC-SVEENIAYGFDGEASftdienaakmANAHEFIEA--FPDKYNtvvgERGLRLSGGQKQRIAIARALLTNP 554
Cdd:PRK11247 87 FQDARLLPWkKVIDNVGLGLKGQWR----------DAALQALAAvgLADRAN----EWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 555 SVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLS-TVKTADCVAVISDGEV 611
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
413-622 |
4.06e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.97 E-value: 4.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERF---YDP---LKGKILLNGVSLMEISHQYLHKQISIVSQEPILF-N 485
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 486 CSVEENIAYGFDGEASFTDIENAAKMANAHEFIEAFPDKYNTVvGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSA 565
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 566 LDAESEYLVQDAMDSLMAGRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
396-622 |
4.82e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.38 E-value: 4.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSrpSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGV-------SLMEIshq 468
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkkSLLEV--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 469 ylHKQISIVSQEP--ILFNCSVEENIAYG-FDGEASFTDIENAAKMANAHEFIEAFPDKYNTvvgerglRLSGGQKQRIA 545
Cdd:PRK13639 77 --RKTVGIVFQNPddQLFAPTVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPH-------HLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 546 IARALLTNPSVLLLDEATSALDAESEYLVQDAMDSL-MAGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
414-622 |
5.03e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 100.42 E-value: 5.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQY---LHKQISIVSQ----------- 479
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQnpygslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 480 ------EPILFNcsveeniaygfdgeasfTDIENAAKMANAHEFIEafpdkynTVvgerGLR----------LSGGQKQR 543
Cdd:PRK11308 111 vgqileEPLLIN-----------------TSLSAAERREKALAMMA-------KV----GLRpehydryphmFSGGQRQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 544 IAIARALLTNPSVLLLDEATSALDAEseylVQDAMDSLMA------GRTVLVIAHRLSTVK-TADCVAVISDGEVAEKGT 616
Cdd:PRK11308 163 IAIARALMLDPDVVVADEPVSALDVS----VQAQVLNLMMdlqqelGLSYVFISHDLSVVEhIADEVMVMYLGRCVEKGT 238
|
....*.
gi 22327455 617 HDELLS 622
Cdd:PRK11308 239 KEQIFN 244
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
413-593 |
5.19e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 103.35 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTT----IANL-------IERfydPLKGKILLngvslmeishqylhkqisiVSQEP 481
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTllraIAGLwpygsgrIAR---PAGARVLF-------------------LPQRP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 482 ILFNCSVEENIAYGfDGEASFTD--IENAAKMANAHEFIEAFpdkynTVVGERGLRLSGGQKQRIAIARALLTNPSVLLL 559
Cdd:COG4178 436 YLPLGTLREALLYP-ATAEAFSDaeLREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190
....*....|....*....|....*....|....
gi 22327455 560 DEATSALDAESEYLVQDAMDSLMAGRTVLVIAHR 593
Cdd:COG4178 510 DEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
410-620 |
6.24e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.56 E-value: 6.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 410 SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQylHKQISIVSQEPILF-NCSV 488
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYGFDGEA-SFTDIENAAKMANAHEFIEAFPDKYntvVGErglrLSGGQKQRIAIARALLTNPSVLLLDEATSALD 567
Cdd:PRK11432 96 GENVGYGLKMLGvPKEERKQRVKEALELVDLAGFEDRY---VDQ----ISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 568 AESEYLVQDAMDSLMA--GRTVLVIAHRLS-TVKTADCVAVISDGEVAEKGTHDEL 620
Cdd:PRK11432 169 ANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
130-342 |
9.40e-23 |
|
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: 98.72 E-value: 9.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 130 GSICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGV 209
Cdd:cd18546 52 GWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 210 GFMFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDET 289
Cdd:cd18546 132 VVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDY 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22327455 290 LKLGLKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILY 342
Cdd:cd18546 212 RDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLY 264
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
410-616 |
9.97e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.32 E-value: 9.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 410 SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPL-----KGKILLNGVSLM--EISHQYLHKQISIVSQEPI 482
Cdd:PRK14243 22 SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLYapDVDPVEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 483 LFNCSVEENIAYG--FDGEASFTD--IENAAKMAnahefieAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLL 558
Cdd:PRK14243 102 PFPKSIYDNIAYGarINGYKGDMDelVERSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 559 LDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTV-KTADCVAVISdGEVAEKGT 616
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFFN-VELTEGGG 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
396-629 |
1.06e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.19 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYD-----PLKGKILLNGVSLME--ISHQ 468
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYErrVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 469 YLHKQISIVSQEPILFNCSVEENIAYG-----FDGEASFTDI-ENAAKMANahefieaFPDKYNTVVGERGLRLSGGQKQ 542
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgWRPKLEIDDIvESALKDAD-------LWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 543 RIAIARALLTNPSVLLLDEATSALDAES----EYLVQDAmdSLMAGRTVLVIAHRLSTV-KTADCVAVISDGEvAEKGTH 617
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSL--RLRSELTMVIVSHNLHQVsRLSDFTAFFKGNE-NRIGQL 234
|
250
....*....|..
gi 22327455 618 DELLSLNGIYTN 629
Cdd:PRK14258 235 VEFGLTKKIFNS 246
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
390-623 |
1.15e-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: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 390 GNPDGDvelNDVWFAYPSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGvslmeishqy 469
Cdd:cd03291 32 KHSSDD---NNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 470 lhkQISIVSQEPILFNCSVEENIAYG--FDgEASFTDIENAAKManaHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIA 547
Cdd:cd03291 99 ---RISFSSQFSWIMPGTIKENIIFGvsYD-EYRYKSVVKACQL---EEDITKFPEKDNTVLGEGGITLSGGQRARISLA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 548 RALLTNPSVLLLDEATSALDAESEYLVQDA-MDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLSL 623
Cdd:cd03291 172 RAVYKDADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
390-620 |
1.17e-22 |
|
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: 103.84 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 390 GNPDGDVELndvWFAYPSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGvslmeishqy 469
Cdd:TIGR01271 421 KQPNGDDGL---FFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG---------- 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 470 lhkQISIVSQEPILFNCSVEENIAYGFD-GEASFTDIENAAKManaHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIAR 548
Cdd:TIGR01271 488 ---RISFSPQTSWIMPGTIKDNIIFGLSyDEYRYTSVIKACQL---EEDIALFPEKDKTVLGEGGITLSGGQRARISLAR 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 549 ALLTNPSVLLLDEATSALDAESEY-LVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDEL 620
Cdd:TIGR01271 562 AVYKDADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
396-619 |
1.20e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLnGVSLmeishqylhkQIS 475
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILFNC--SVEENIAYGFDGEasfTDIEnaakmanAHEFIEAF---PDKYNTVVGerglRLSGGQKQRIAIARAL 550
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGAPGG---TEQE-------VRGYLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 551 LTNPSVLLLDEATSALDAESEYLVQDAMDSLmAGrTVLVIAH-R--LSTVktADCVAVISDGEVAEK-GTHDE 619
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYpGGYDD 516
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
397-592 |
1.29e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.46 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYlhkqiSI 476
Cdd:PRK11248 3 QISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 477 VSQ-EPILFNCSVEENIAYGFDgeasFTDIENAAKMANAHEFIEAfpdkyntvVGERGL------RLSGGQKQRIAIARA 549
Cdd:PRK11248 75 VFQnEGLLPWRNVQDNVAFGLQ----LAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22327455 550 LLTNPSVLLLDEATSALDAeseyLVQDAMDSLM------AGRTVLVIAH 592
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDA----FTREQMQTLLlklwqeTGKQVLLITH 187
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
409-612 |
1.81e-22 |
|
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: 94.42 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 409 PSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGvslmeishqylhkqisivsqEPILFNCSV 488
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EeniaygfdgeasftdienaakmANAHefieafpdkyntvvgerGLR----LSGGQKQRIAIARALLTNPSVLLLDEATS 564
Cdd:cd03216 71 D----------------------ARRA-----------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22327455 565 AL-DAESEYLVqDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEVA 612
Cdd:cd03216 112 ALtPAEVERLF-KVIRRLRAqGVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
397-603 |
2.20e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.94 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISI 476
Cdd:PRK10247 9 QLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 477 VSQEPILFNCSVEENIAYGFdgeasftDIENAAKMANAhefIEAFPDKY---NTVVGERGLRLSGGQKQRIAIARALLTN 553
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFPW-------QIRNQQPDPAI---FLDDLERFalpDTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22327455 554 PSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTVKTADCV 603
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVReqNIAVLWVTHDKDEINHADKV 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
401-622 |
4.23e-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: 100.53 E-value: 4.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 401 VWFAYPSRPSHmILKGISLRLTPGSKVALVGPSGGGKT----TIANLIERFYDPLKGKILLNGVSLMEISHQYLHK---- 472
Cdd:COG4172 14 VAFGQGGGTVE-AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 QISIVSQEPI-----LFncSVEENIA------YGFDGEAS---------FTDIENAAKMANA--HEfieafpdkyntvvg 530
Cdd:COG4172 93 RIAMIFQEPMtslnpLH--TIGKQIAevlrlhRGLSGAAAraralelleRVGIPDPERRLDAypHQ-------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 531 erglrLSGGQKQRIAIARALLTNPSVLLLDEATSALDAeseyLVQ----DAMDSL-----MAgrtVLVIAHRLSTV-KTA 600
Cdd:COG4172 157 -----LSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaqilDLLKDLqrelgMA---LLLITHDLGVVrRFA 224
|
250 260
....*....|....*....|..
gi 22327455 601 DCVAVISDGEVAEKGTHDELLS 622
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFA 246
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
396-622 |
6.16e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.32 E-value: 6.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEP--ILFNCSVEENIAYGFDG-----EASFTDIENAAKMANAHEFIEAFPdkyntvvgergLRLSGGQKQRIAIAR 548
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgiprEEMIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 549 ALLTNPSVLLLDEATSALD----AESEYLVQDAMDSLMAgrTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
147-342 |
7.48e-22 |
|
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: 96.36 E-value: 7.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 147 RVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIknaatTNLS----EALRNVTTALIG-VGFMFTSSWKLTL 221
Cdd:cd18549 72 RIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDI-----SELAhhgpEDLFISIITIIGsFIILLTINVPLTL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 222 LALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVG 301
Cdd:cd18549 147 IVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMA 226
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22327455 302 LFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILY 342
Cdd:cd18549 227 YFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLY 267
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
414-615 |
1.08e-21 |
|
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: 93.97 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEiSHQYLHKQISIVSQEPILFN-CSVEENI 492
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDrLTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 493 AY-----GFDGEASFTDIENAAKMANAHEFIEafpdkyntvvgERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALD 567
Cdd:cd03266 100 EYfaglyGLKGDELTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22327455 568 AESEYLVQDAMDSLM-AGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKG 615
Cdd:cd03266 169 VMATRALREFIRQLRaLGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
408-638 |
1.44e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 94.75 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 408 RPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEIS---HQYLHKQISIVSQEPI-L 483
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSIsA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 484 FNC--SVEENIAygfDGEASFTDIENAAKMANAHEFIEAFpDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDE 561
Cdd:PRK10419 102 VNPrkTVREIIR---EPLRHLLSLDKAERLARASEMLRAV-DLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 562 ATSALDaeseYLVQDAMDSLMA------GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLSLngiyTNLVKRQ 634
Cdd:PRK10419 178 AVSNLD----LVLQAGVIRLLKklqqqfGTACLFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKLTF----SSPAGRV 249
|
....
gi 22327455 635 LQSS 638
Cdd:PRK10419 250 LQNA 253
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
413-638 |
1.48e-21 |
|
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: 94.87 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEI---SHQYLHKQISIVSQE-PILFN--C 486
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQDsPSAVNprM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 SVEENIAYGFDgeaSFTDIENAAKMANAHEFIEAFpDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSAL 566
Cdd:TIGR02769 106 TVRQIIGEPLR---HLTSLDESEQKARIAELLDMV-GLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 567 DAESEYLVQDAMDSLMA--GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLSlngiYTNLVKRQLQSS 638
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQafGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQLLS----FKHPAGRNLQSA 252
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
131-346 |
1.54e-21 |
|
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: 95.21 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 131 SICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSeDTQIIKNAATTNLSEALRNVTTALIGVG 210
Cdd:cd18570 56 SLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 211 FMFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETL 290
Cdd:cd18570 135 ILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLL 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 291 KLGLKQAVLvGLFFGGLNAAF-TLSVITVVSYGAYLTIYGSMTVGALTSFilYSLTV 346
Cdd:cd18570 215 KKSFKLGKL-SNLQSSIKGLIsLIGSLLILWIGSYLVIKGQLSLGQLIAF--NALLG 268
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
405-622 |
1.66e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.94 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 405 YPSRPshmILKGISLRLTPGSKVALVGPSGGGKTT----IANLIErfydPLKGKILLNGvslMEISHQYLHKQ----ISI 476
Cdd:COG1137 13 YGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDG---EDITHLPMHKRarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 477 VSQEPILF-NCSVEENIAygfdgeA--SFTDIENAAKMANAHEFIEAFpdKYNTVVGERGLRLSGGQKQRIAIARALLTN 553
Cdd:COG1137 83 LPQEASIFrKLTVEDNIL------AvlELRKLSKKEREERLEELLEEF--GITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 554 PSVLLLDEATSALD----AESEYLVQDAMDslmAGRTVLVIAH--RlSTVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:COG1137 155 PKFILLDEPFAGVDpiavADIQKIIRHLKE---RGIGVLITDHnvR-ETLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
411-622 |
1.74e-21 |
|
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: 94.92 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 411 HMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDpLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEE 490
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 491 NI-AYGfdgEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAE 569
Cdd:cd03289 96 NLdPYG---KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22327455 570 SEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:cd03289 173 TYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
407-644 |
2.30e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 407 SRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPIL-FN 485
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 486 CSVEENIAYG-------FDGEASfTDiENAAKMANAHEFIEAFPDKYNTvvgerglRLSGGQKQRIAIARALLTNPSVLL 558
Cdd:PRK09536 92 FDVRQVVEMGrtphrsrFDTWTE-TD-RAAVERAMERTGVAQFADRPVT-------SLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 559 LDEATSALDAESEY----LVQDAMDSlmaGRTVLVIAHRLS-TVKTADCVAVISDGEVAEKG------THDELLSLNGIY 627
Cdd:PRK09536 163 LDEPTASLDINHQVrtleLVRRLVDD---GKTAVAAIHDLDlAARYCDELVLLADGRVRAAGppadvlTADTLRAAFDAR 239
|
250
....*....|....*..
gi 22327455 628 TNLVKRQLQSSSSVTTL 644
Cdd:PRK09536 240 TAVGTDPATGAPTVTPL 256
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
414-618 |
2.37e-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: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLmEIS--HQYLHKQISIVSQEPILF-NCSVEE 490
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRspRDAIALGIGMVHQHFMLVpNLTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 491 NIAYGFDGEASFtdienAAKMANAHEFIEAFPDKY------NTVVGErglrLSGGQKQRIAIARALLTNPSVLLLDEATS 564
Cdd:COG3845 100 NIVLGLEPTKGG-----RLDRKAARARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 565 AL-DAESEYLVqDAMDSLMA-GRTVLVIAHRLSTVKT-ADCVAVISDGEVAekGTHD 618
Cdd:COG3845 171 VLtPQEADELF-EILRRLAAeGKSIIFITHKLREVMAiADRVTVLRRGKVV--GTVD 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
396-618 |
2.53e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSrpsHMILKGISLRLTPGSKVALVGPSGGGKTT---IANLIERfydPLKGKILLNGVSL---MEISH-- 467
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLLET---PDSGQLNIAGHQFdfsQKPSEka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 468 -QYLHKQISIVSQEPILF-NCSVEENI------AYGFDGEASftdIENAAKMANA---HEFIEAFPdkyntvvgergLRL 536
Cdd:COG4161 77 iRLLRQKVGMVFQQYNLWpHLTVMENLieapckVLGLSKEQA---REKAMKLLARlrlTDKADRFP-----------LHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 537 SGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEVAEK 614
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFArKVASQVVYMEKGRIIEQ 222
|
....
gi 22327455 615 GTHD 618
Cdd:COG4161 223 GDAS 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
414-615 |
3.68e-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: 91.89 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYlhKQISIVSQEPILF-NCSVEENI 492
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYpNLTARENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 493 AYGfdgeASFTDIENAakmaNAHEFIEafpdkyntVVGERGLR------LSGGQKQRIAIARALLTNPSVLLLDEATSAL 566
Cdd:cd03268 94 RLL----ARLLGIRKK----RIDEVLD--------VVGLKDSAkkkvkgFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22327455 567 DAESEYLVQDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKG 615
Cdd:cd03268 158 DPDGIKELRELILSLRDqGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
413-622 |
3.77e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.30 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPIL-FNCSVEEN 491
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 492 IAYGfdgeasftdienAAKMANAHEFIEAFPDKYNTVVGERGLR------LSGGQKQRIAIARAL--LTN----PSVLLL 559
Cdd:PRK13548 97 VAMG------------RAPHGLSRAEDDALVAAALAQVDLAHLAgrdypqLSGGEQQRVQLARVLaqLWEpdgpPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 560 DEATSALD-AESEYLVQDAMD-SLMAGRTVLVIAHRLS-TVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK13548 165 DEPTSALDlAHQHHVLRLARQlAHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
396-622 |
8.06e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.74 E-value: 8.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPS-RPShmiLKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISH-QYLHKQ 473
Cdd:PRK13644 2 IRLENVSYSYPDgTPA---LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 474 ISIVSQEP--ILFNCSVEENIAYGFDGEA-SFTDIENAAKMANAHEFIEAFPDKYNTVvgerglrLSGGQKQRIAIARAL 550
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGPENLClPPIEIRKRVDRALAEIGLEKYRHRSPKT-------LSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 551 LTNPSVLLLDEATSALDAESEYLVQDAMDSLM-AGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
358-618 |
1.17e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.74 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 358 TTAMKAAGASRRVFQILDRVSSMSSSGDKCPVGN-PDGDVELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGG 436
Cdd:PRK13536 3 TRAVAEEAPRRLELSPIERKHQGISEAKASIPGSmSTVAIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 437 KTTIANLIERFYDPLKGKILLNGVSLMEIShQYLHKQISIVSQEPIL-FNCSVEEN-IAYGFDGEASFTDIEnaAKMANA 514
Cdd:PRK13536 80 KSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQFDNLdLEFTVRENlLVFGRYFGMSTREIE--AVIPSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 515 HEFIEaFPDKYNTVVGErglrLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHR 593
Cdd:PRK13536 157 LEFAR-LESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHF 231
|
250 260
....*....|....*....|....*..
gi 22327455 594 LSTV-KTADCVAVISDG-EVAEKGTHD 618
Cdd:PRK13536 232 MEEAeRLCDRLCVLEAGrKIAEGRPHA 258
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
136-370 |
1.19e-20 |
|
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: 93.11 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 136 LRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTS 215
Cdd:cd18558 78 IQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 216 SWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLK 295
Cdd:cd18558 158 GWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIK 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 296 QAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGASRRV 370
Cdd:cd18558 238 KAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
413-622 |
1.80e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.70 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKG-----KILLNGVSLMEISHQY-LHKQISIVSQEPILFNC 486
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 SVEENIAYGFDGEASFTDIENAAkMANAHEFIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSAL 566
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRG-VAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 567 DAESEYLVQDAMDSLMAGRTVLVIAHRLS-TVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
404-606 |
2.10e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.22 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 404 AYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKIllngvslmeisHQYLHKQISIVSQ---E 480
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 481 PILFNCSVEENIAYGFDGEASFTDIENAAKMANAHEFIEAfpdkyntvVGERGLR------LSGGQKQRIAIARALLTNP 554
Cdd:NF040873 67 PDSLPLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALER--------VGLADLAgrqlgeLSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22327455 555 SVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTVKTADCVAVI 606
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
408-623 |
2.43e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.11 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 408 RPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIErFYDP----LKGKILLNGvslMEISHQYLHKQISIVSQEPIL 483
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNG---MPIDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 484 F-NCSVEENIAYgfdgEASF---TDIENAAKMANAHEFIEA--FPDKYNTVVGERGLR--LSGGQKQRIAIARALLTNPS 555
Cdd:TIGR00955 111 IpTLTVREHLMF----QAHLrmpRRVTKKEKRERVDEVLQAlgLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 556 VLLLDEATSALDAESEYLVQDAMDSL-MAGRTVLVIAHRLST--VKTADCVAVISDGEVAEKGTHDELLSL 623
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVPF 257
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
413-615 |
3.56e-20 |
|
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: 89.64 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLK---GKILLNGvslMEISHQYLHKQISIVSQEPILFNC-SV 488
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYgfdgeasftdienAAKMANAHEFIEAFPDK----------YNTVVGERGLR-LSGGQKQRIAIARALLTNPSVL 557
Cdd:cd03234 99 RETLTY-------------TAILRLPRKSSDAIRKKrvedvllrdlALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 558 LLDEATSALDAESEY-LVQDAMDSLMAGRTVLVIAH--RLSTVKTADCVAVISDGEVAEKG 615
Cdd:cd03234 166 ILDEPTSGLDSFTALnLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
396-622 |
4.59e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 90.63 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYpsRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEP--ILFNCSVEENIAYG-----FDGEASFTDIENAAKMANAHEFIEAFPDkyntvvgerglRLSGGQKQRIAIAR 548
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGpinlgLDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 549 ALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
414-620 |
5.43e-20 |
|
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: 88.97 E-value: 5.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQyLHKQISIVSQEPILFN-CSVEENI 492
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSVDDeLTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 493 A-----YGFDGEasftdiENAAKMANAHEFIE--AFPDKYntvVGerglRLSGGQKQRIAIARALLTNPSVLLLDEATSA 565
Cdd:cd03265 95 YiharlYGVPGA------ERRERIDELLDFVGllEAADRL---VK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 566 LDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDEL 620
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
413-615 |
5.66e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 95.23 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTianlierfydpLKGKILlngvSLMEISHQ--YLHKQISIVSQEPILFNCSVEE 490
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKST-----------LLQSLL----SQFEISEGrvWAERSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 491 NIAygfdgeasFTDIENAAKMANAHEF--IEA----FPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATS 564
Cdd:PTZ00243 740 NIL--------FFDEEDAARLADAVRVsqLEAdlaqLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22327455 565 ALDAE-SEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKG 615
Cdd:PTZ00243 812 ALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
397-620 |
7.52e-20 |
|
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: 88.74 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSrpSHmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEIS-HQYLHKQIS 475
Cdd:TIGR03410 2 EVSNLNVYYGQ--SH-ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILF-NCSVEENIAYGFDGEAsftdienAAKMANAHEFIEAFPdKYNTVVGERGLRLSGGQKQRIAIARALLTNP 554
Cdd:TIGR03410 79 YVPQGREIFpRLTVEENLLTGLAALP-------RRSRKIPDEIYELFP-VLKEMLGRRGGDLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 555 SVLLLDEATSALDAESEYLVQDAMDSL--MAGRTVLVIAHRLSTVK-TADCVAVISDGEVAEKGTHDEL 620
Cdd:TIGR03410 151 KLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFAReLADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
134-347 |
8.75e-20 |
|
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: 90.31 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 134 TALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEdTQIIKNAATTNLSEALRNVTTALIGVGFMF 213
Cdd:cd18568 59 SAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQE-NQKIRRFLTRSALTTILDLLMVFIYLGLMF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 214 TSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLG 293
Cdd:cd18568 138 YYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTR 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 294 LKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSF-ILYSLTVG 347
Cdd:cd18568 218 FRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFnMLFGSVIN 272
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
413-620 |
1.01e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 91.30 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGvslMEISHqyLH---KQISIVSQEPILF-NCSV 488
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG---TDVSR--LHardRKVGFVFQHYALFrHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYGF---------DGEASFTDIENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQRIAIARALLTNPSVLLL 559
Cdd:PRK10851 92 FDNIAFGLtvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQ-----------LSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 560 DEATSALDAE-----SEYLVQdaMDSLMAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDEL 620
Cdd:PRK10851 161 DEPFGALDAQvrkelRRWLRQ--LHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
137-342 |
1.27e-19 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). 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. 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: 349998 [Multi-domain] Cd Length: 299 Bit Score: 89.79 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 137 RAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSS 216
Cdd:cd18554 66 RQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 217 WKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQ 296
Cdd:cd18554 146 PKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKH 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 22327455 297 AVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILY 342
Cdd:cd18554 226 TRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGY 271
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
414-619 |
1.31e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 89.72 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLME--ISHQYLHKQISIVSQEP--ILFNCSVE 489
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPeyQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 490 ENIAYGFDGEA-SFTDIENAAKMAnahefIEAFPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDA 568
Cdd:PRK13637 103 KDIAFGPINLGlSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 569 ----ESEYLVQDAMDSLmaGRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDE 619
Cdd:PRK13637 178 kgrdEILNKIKELHKEY--NMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
414-615 |
1.47e-19 |
|
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: 87.91 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLhkqisIVSQEPILFN-CSVEENI 492
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 493 AYGFDgeASFTDIENAAKMANAHEFIE-----AFPDKYNTvvgerglRLSGGQKQRIAIARALLTNPSVLLLDEATSALD 567
Cdd:TIGR01184 76 ALAVD--RVLPDLSKSERRAIVEEHIAlvgltEAADKRPG-------QLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22327455 568 AESEYLVQdamDSLM-----AGRTVLVIAHRL-STVKTADCVAVISDGEVAEKG 615
Cdd:TIGR01184 147 ALTRGNLQ---EELMqiweeHRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
413-622 |
1.95e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERF-------YdpLKGKILLNGVSLMEISHQYLHK----QISIVSQEP 481
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvvY--PSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 482 IL-FNC--SVEENIA------YGFDGEASFTD---------IENAAKMANahefieAFPDKyntvvgerglrLSGGQKQR 543
Cdd:PRK15134 102 MVsLNPlhTLEKQLYevlslhRGMRREAARGEilncldrvgIRQAAKRLT------DYPHQ-----------LSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 544 IAIARALLTNPSVLLLDEATSALDAEseylVQDAMDSLMA------GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGT 616
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVS----VQAQILQLLRelqqelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNR 240
|
....*.
gi 22327455 617 HDELLS 622
Cdd:PRK15134 241 AATLFS 246
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
411-622 |
2.21e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.10 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 411 HMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISH-------------QYLHKQISIV 477
Cdd:PRK10619 18 HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqlRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 478 SQEPILFN-CSVEENIAygfdgEASFTDIenAAKMANAHEFIEAFPDKYNTVVGERG---LRLSGGQKQRIAIARALLTN 553
Cdd:PRK10619 98 FQHFNLWShMTVLENVM-----EAPIQVL--GLSKQEARERAVKYLAKVGIDERAQGkypVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 554 PSVLLLDEATSALDAESEYLVQDAMDSLM-AGRTVLVIAHRLSTVK-TADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
396-622 |
2.34e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.61 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAY---PSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQY-LH 471
Cdd:PRK13633 5 IKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 472 KQISIVSQEP--ILFNCSVEENIAYG-----FDGEASFTDIENAAKMANAHEFIEAFPDkyntvvgerglRLSGGQKQRI 544
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGpenlgIPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 545 AIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSL--MAGRTVLVIAHRLSTVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
414-622 |
3.24e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 87.97 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEP-ILFNCSVeeNI 492
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDPnTSLNPRL--NI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 493 AYGFDGEASF-TDIENAAKmanaHEFIEA-------FPDKYNTVVGErglrLSGGQKQRIAIARALLTNPSVLLLDEATS 564
Cdd:COG4167 107 GQILEEPLRLnTDLTAEER----EERIFAtlrlvglLPEHANFYPHM----LSSGQKQRVALARALILQPKIIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 565 ALDAEseylVQDAMDSLM------AGRTVLVIAHRLSTVK-TADCVAVISDGEVAEKGTHDELLS 622
Cdd:COG4167 179 ALDMS----VRSQIINLMlelqekLGISYIYVSQHLGIVKhISDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
134-343 |
3.42e-19 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins 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. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 88.29 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 134 TALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEdTQIIKNAATTNLSEALRNVTTALIGVGFMF 213
Cdd:cd18567 59 SALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFVEALLDGLMAILTLVMMF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 214 TSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLG 293
Cdd:cd18567 138 LYSPKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINAD 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22327455 294 LKQAVLvGLFFGGLNAA-FTLSVITVVSYGAYLTIYGSMTVGALTSFILYS 343
Cdd:cd18567 218 IRLQRL-QILFSAANGLlFGLENILVIYLGALLVLDGEFTVGMLFAFLAYK 267
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
396-622 |
6.71e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.53 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAY-PSRP-SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLM------EISH 467
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 468 qyLHKQISIVSQ--EPILFNCSVEENIAYGfdgEASF-TDIENAAkmANAHEFIEAFPDKYNtVVGERGLRLSGGQKQRI 544
Cdd:PRK13646 83 --VRKRIGMVFQfpESQLFEDTVEREIIFG---PKNFkMNLDEVK--NYAHRLLMDLGFSRD-VMSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 545 AIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELL 621
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELF 234
|
.
gi 22327455 622 S 622
Cdd:PRK13646 235 K 235
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
148-622 |
6.97e-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: 91.51 E-value: 6.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 148 VVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEAlrnVTTALIGVGFMFTSS--WKLTLLALV 225
Cdd:TIGR01271 956 VSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDF---IQLTLIVLGAIFVVSvlQPYIFIAAI 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 226 VVPVISVAVKQ-FGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFF 304
Cdd:TIGR01271 1033 PVAVIFIMLRAyFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQ 1112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 305 GGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTVGSSVSSLSSLYTTAMKAAGasrRVFQILD---RVSSMS 381
Cdd:TIGR01271 1113 MRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVS---RVFKFIDlpqEEPRPS 1189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 382 SSGDKCPVG------NP--------DGDVELNDVWFAYPSrPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERF 447
Cdd:TIGR01271 1190 GGGGKYQLStvlvieNPhaqkcwpsGGQMDVQGLTAKYTE-AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL 1268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 448 YDPlKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSVEENIaygfDGEASFTDIE--NAAKMANAHEFIEAFPDKY 525
Cdd:TIGR01271 1269 LST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL----DPYEQWSDEEiwKVAEEVGLKSVIEQFPDKL 1343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 526 NTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCVAV 605
Cdd:TIGR01271 1344 DFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLV 1423
|
490
....*....|....*..
gi 22327455 606 ISDGEVAEKGTHDELLS 622
Cdd:TIGR01271 1424 IEGSSVKQYDSIQKLLN 1440
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
396-618 |
7.20e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.22 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSrpsHMILKGISLRLTPGSKVALVGPSGGGKTT---IANLIERfydPLKGKILLNGvSLMEISHQYLHK 472
Cdd:PRK11124 3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEM---PRSGTLNIAG-NHFDFSKTPSDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 QISIVSQE-----------PILfncSVEENI------AYGFDGEASFTDIENAAKMANAHEFIEAFPdkyntvvgergLR 535
Cdd:PRK11124 76 AIRELRRNvgmvfqqynlwPHL---TVQQNLieapcrVLGLSKDQALARAEKLLERLRLKPYADRFP-----------LH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 536 LSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEVAE 613
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVArKTASRVVYMENGHIVE 221
|
....*
gi 22327455 614 KGTHD 618
Cdd:PRK11124 222 QGDAS 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
396-620 |
7.58e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 7.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHK-QI 474
Cdd:PRK15439 12 LCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 475 SIVSQEPILF-NCSVEENIAYGFDGEAsftdiENAAKMAnahEFIEAFPDKYNTVVGERGLRLSggQKQRIAIARALLTN 553
Cdd:PRK15439 89 YLVPQEPLLFpNLSVKENILFGLPKRQ-----ASMQKMK---QLLAALGCQLDLDSSAGSLEVA--DRQIVEILRGLMRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 554 PSVLLLDEATSALD-AESEYLVQDAMDSLMAGRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDEL 620
Cdd:PRK15439 159 SRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
417-620 |
1.25e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.35 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 417 ISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEIShQYLhKQISIVSQEPILF-NCSVEENIAYG 495
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQ-RPINMMFQSYALFpHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 496 FDGE----ASFTD-IENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQRIAIARALLTNPSVLLLDEATSALDAES 570
Cdd:PRK11607 116 LKQDklpkAEIASrVNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22327455 571 EYLVQ-DAMDSL-MAGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDEL 620
Cdd:PRK11607 185 RDRMQlEVVDILeRVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
400-622 |
1.38e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.21 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 400 DVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLmEISHQ---YLHKQISI 476
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 477 VSQEPilfncsvEENIAYgfdgeasfTDIEN--AAKMAN---AHEFIEAFPDKYNTVVGERGLR------LSGGQKQRIA 545
Cdd:PRK13638 82 VFQDP-------EQQIFY--------TDIDSdiAFSLRNlgvPEAEITRRVDEALTLVDAQHFRhqpiqcLSHGQKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 546 IARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAqGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
411-615 |
2.37e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 411 HMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYdPLKGKILLNGVSLMEISHQYL---HKQISIVSQEPilfNCS 487
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP---NSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 488 ------VEENIAYGFD-GEASFTDIENAAKMANAHEFIEAFPDKYNTVVGErglrLSGGQKQRIAIARALLTNPSVLLLD 560
Cdd:PRK15134 375 lnprlnVLQIIEEGLRvHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 561 EATSALDAESEYLVQDAMDSLMAGRTV--LVIAHRLSTVKtADC--VAVISDGEVAEKG 615
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVR-ALChqVIVLRQGEVVEQG 508
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
410-611 |
4.93e-18 |
|
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: 83.10 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 410 SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLmeishQYLHKQ-ISIVSQEPILF-NCS 487
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-----DIAARNrIGYLPEERGLYpKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 488 VEENIAYgfdgEASFTDIENAAKMANAHEFIEAF--PDKYNTVVGErglrLSGGQKQRIAIARALLTNPSVLLLDEATSA 565
Cdd:cd03269 87 VIDQLVY----LAQLKGLKKEEARRRIDEWLERLelSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22327455 566 LDAESEYLVQDAMDSLM-AGRTVLVIAHRLSTV-KTADCVAVISDGEV 611
Cdd:cd03269 159 LDPVNVELLKDVIRELArAGKTVILSTHQMELVeELCDRVLLLNKGRA 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
411-618 |
6.33e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.86 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 411 HMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQyLHKQISIVSQ----EPilfNC 486
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGVVPQfdnlDP---DF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 SVEENIAYgFDGEASFTDIENAAKMANAHEFIEaFPDKYNTVVGErglrLSGGQKQRIAIARALLTNPSVLLLDEATSAL 566
Cdd:PRK13537 96 TVRENLLV-FGRYFGLSAAAARALVPPLLEFAK-LENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 567 DAESEYLVQDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDG-EVAEKGTHD 618
Cdd:PRK13537 170 DPQARHLMWERLRSLLArGKTILLTTHFMEEAeRLCDRLCVIEEGrKIAEGAPHA 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
413-616 |
9.99e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.19 E-value: 9.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLI---ERfYDPLKGKILLNGVSLMEIS-HQYLHKQISIVSQEPilfncsV 488
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSpDERARAGIFLAFQYP------V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EeniaygFDGeASFTDIENAAKMANAHEFIEA--FPDKYNTVVGERGLR-----------LSGGQKQRIAIARALLTNPS 555
Cdd:COG0396 88 E------IPG-VSVSNFLRTALNARRGEELSAreFLKLLKEKMKELGLDedfldryvnegFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 556 VLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAH--RLSTVKTADCVAVISDGEVAEKGT 616
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
392-622 |
1.27e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 83.74 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 392 PDGDVELNDVWFAYPSrPSHMiLKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGV-------SLME 464
Cdd:PRK13636 2 EDYILKVEELNYNYSD-GTHA-LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 465 ishqyLHKQISIVSQEP--ILFNCSVEENIAYG-FDGEASFTDIENAAKMANAHEFIEAFPDKYNTVvgerglrLSGGQK 541
Cdd:PRK13636 80 -----LRESVGMVFQDPdnQLFSASVYQDVSFGaVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 542 QRIAIARALLTNPSVLLLDEATSALD----AESEYLVQDAMDSLmaGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGT 616
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGN 225
|
....*.
gi 22327455 617 HDELLS 622
Cdd:PRK13636 226 PKEVFA 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
413-591 |
1.54e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGV-----SLMEISHqYL-HKQisivSQEPILfnc 486
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddpDVAEACH-YLgHRN----AMKPAL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 SVEENIAY--GFDGEASfTDIENAAK-MANAHefIEAFPDKYntvvgerglrLSGGQKQRIAIARALLTNPSVLLLDEAT 563
Cdd:PRK13539 89 TVAENLEFwaAFLGGEE-LDIAAALEaVGLAP--LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180
....*....|....*....|....*...
gi 22327455 564 SALDAESEYLVQDAMDSLMAGRTVLVIA 591
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
403-615 |
1.57e-17 |
|
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: 81.81 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 403 FAYPSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNG--VSLMEISHQyLHKQISivSQE 480
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLGLGGG-FNPELT--GRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 481 PILFNCSVeeniaYGFDGEasftdiENAAKManahEFIEAF---PDKYNTVVGErglrLSGGQKQRIAIARALLTNPSVL 557
Cdd:cd03220 104 NIYLNGRL-----LGLSRK------EIDEKI----DEIIEFselGDFIDLPVKT----YSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 558 LLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTVK-TADCVAVISDGEVAEKG 615
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLRELLKqGKTVILVSHDPSSIKrLCDRALVLEKGKIRFDG 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
414-609 |
1.58e-17 |
|
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: 82.10 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLN----GVSLMEIS-HQYLH---KQISIVSQ------ 479
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpREILAlrrRTIGYVSQflrvip 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 480 ---------EPILfncsveeniAYGFDgeasftdiENAAKmANAHEFIEAFpdkyNtvVGERGLRL-----SGGQKQRIA 545
Cdd:COG4778 107 rvsaldvvaEPLL---------ERGVD--------REEAR-ARARELLARL----N--LPERLWDLppatfSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 546 IARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTVKT-ADCVAVISDG 609
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKArGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
413-615 |
1.87e-17 |
|
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: 81.03 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERF--YDPLKGKILLNGVSLMEIS-HQYLHKQISIVSQEPIlfncsve 489
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPpEERARLGIFLAFQYPP------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 490 eniaygfdgeaSFTDIENAakmanahEFIeafpdkyntvvgeRGLR--LSGGQKQRIAIARALLTNPSVLLLDEATSALD 567
Cdd:cd03217 88 -----------EIPGVKNA-------DFL-------------RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 22327455 568 AESEYLVQDAMDSLM-AGRTVLVIAH--RLSTVKTADCVAVISDGEVAEKG 615
Cdd:cd03217 137 IDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
407-592 |
2.03e-17 |
|
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: 80.87 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 407 SRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYlHKQISIVSQEPILFN- 485
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 486 CSVEENIAYgfdgeasFTDIENAAKMaNAHEFIEAfpdkyntvVGERGL------RLSGGQKQRIAIARALLTNPSVLLL 559
Cdd:TIGR01189 88 LSALENLHF-------WAAIHGGAQR-TIEDALAA--------VGLTGFedlpaaQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 22327455 560 DEATSALDAESEYLVQDAMDS-LMAGRTVLVIAH 592
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
423-567 |
2.30e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.16 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 423 PGSKV-ALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQ-YL--HKQ-ISIVSQEPILF-NCSVEENIAYGF 496
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLppEKRrIGYVFQDARLFpHYKVRGNLRYGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 497 dgeasftdienAAKManahefieafPDKYNTVVGERGL---------RLSGGQKQRIAIARALLTNPSVLLLDEATSALD 567
Cdd:PRK11144 102 -----------AKSM----------VAQFDKIVALLGIeplldrypgSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
131-346 |
2.76e-17 |
|
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: 82.64 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 131 SICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEdTQIIKNAATTNLSEALRNVTTALIGVG 210
Cdd:cd18782 56 AVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRISE-LDTIRGFLTGTALTTLLDVLFSVIYIA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 211 FMFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESY----MVSQYSKKV 286
Cdd:cd18782 135 VLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKarwrWQNRYARSL 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 287 DETLKLGlkqavLVGLFFGGLNAAFT-LSVITVVSYGAYLTIYGSMTVGALTSFILYSLTV 346
Cdd:cd18782 215 GEGFKLT-----VLGTTSGSLSQFLNkLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYV 270
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
396-593 |
3.18e-17 |
|
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: 79.51 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSrpSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKIllngvslmeisHQYLHKQIS 475
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILFNCSVEENIAYGFDGEasftdienaakmanahefieafpdkyntvvgerglrLSGGQKQRIAIARALLTNPS 555
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDDV------------------------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 22327455 556 VLLLDEATSALDAESEYLVQDAMDSLMAgrTVLVIAHR 593
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
395-620 |
3.30e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.22 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 395 DVELNDVWFAYPSRpSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLH--- 471
Cdd:PRK15079 19 DIKDGKQWFWQPPK-TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRavr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 472 KQISIVSQEPIL-FN--CSVEENIA---YGFDGEASFTDIENAAK--MANA-----------HEFieafpdkyntvvger 532
Cdd:PRK15079 98 SDIQMIFQDPLAsLNprMTIGEIIAeplRTYHPKLSRQEVKDRVKamMLKVgllpnlinrypHEF--------------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 533 glrlSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTVK-TADCVAVISDG 609
Cdd:PRK15079 163 ----SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKhISDRVLVMYLG 238
|
250
....*....|.
gi 22327455 610 EVAEKGTHDEL 620
Cdd:PRK15079 239 HAVELGTYDEV 249
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
410-620 |
3.31e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.46 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 410 SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVslmEISHQYLHKqISIVSQEPILF-NCSV 488
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---PLDPEDRRR-IGYLPEERGLYpKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYgFdgeASFTDIENAAKMANAHEFIEAF--PDKYNTVVGErglrLSGGQKQRIAIARALLTNPSVLLLDEATSAL 566
Cdd:COG4152 89 GEQLVY-L---ARLKGLSKAEAKRRADEWLERLglGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 567 DAESEYLVQDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDEL 620
Cdd:COG4152 161 DPVNVELLKDVIRELAAkGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
413-609 |
4.74e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.93 E-value: 4.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIE-RFY-DPLKGKILLNGvslMEISHQYLhKQISIVSQEPILF-NCSVE 489
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANN---RKPTKQIL-KRTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 490 ENIAYgfdgeASFTDIENA----AKMANAHEFIE--AFPDKYNTVVGERGLR-LSGGQKQRIAIARALLTNPSVLLLDEA 562
Cdd:PLN03211 159 ETLVF-----CSLLRLPKSltkqEKILVAESVISelGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22327455 563 TSALDAESEY-LVQDAMDSLMAGRTVLVIAHRLST--VKTADCVAVISDG 609
Cdd:PLN03211 234 TSGLDATAAYrLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEG 283
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
413-567 |
5.23e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.29 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVslmEISHQYLHK---QISIVSQEPILFNC--- 486
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK---DVTKLPEYKrakYIGRVFQDPMMGTApsm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 SVEEN--IAYGFDGEASFTDIENAAKMANAHEFIEAF----PDKYNTVVGErglrLSGGQKQRIAIARALLTNPSVLLLD 560
Cdd:COG1101 98 TIEENlaLAYRRGKRRGLRRGLTKKRRELFRELLATLglglENRLDTKVGL----LSGGQRQALSLLMATLTKPKLLLLD 173
|
....*..
gi 22327455 561 EATSALD 567
Cdd:COG1101 174 EHTAALD 180
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
429-628 |
5.93e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.21 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 429 LVGPSGGGKTTIAN----LIERFYDPLKGKILLNG----VSLMEISH--------QYLHKQISIVSQEP--ILFNCSVEE 490
Cdd:PRK13631 57 IIGNSGSGKSTLVThfngLIKSKYGTIQVGDIYIGdkknNHELITNPyskkiknfKELRRRVSMVFQFPeyQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 491 NIAYG--FDGEASFTDIENAA----KMANAHEFIEAFPdkyntvvgergLRLSGGQKQRIAIARALLTNPSVLLLDEATS 564
Cdd:PRK13631 137 DIMFGpvALGVKKSEAKKLAKfylnKMGLDDSYLERSP-----------FGLSGGQKRRVAIAGILAIQPEILIFDEPTA 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 565 ALDAESEY-LVQDAMDSLMAGRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLSLNGIYT 628
Cdd:PRK13631 206 GLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
403-611 |
6.41e-17 |
|
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: 79.61 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 403 FAYPSRPSHMILKGISLRLTPGSKVALVGPSGGGKTT----IANLIERFYDPlKGKILLNGVSLMEISHQYlHKQISIVS 478
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 479 QEPILF-NCSVEENIaygfdgeasftdiENAAKMaNAHEFIeafpdkyntvvgeRGLrlSGGQKQRIAIARALLTNPSVL 557
Cdd:cd03233 90 EEDVHFpTLTVRETL-------------DFALRC-KGNEFV-------------RGI--SGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 558 LLDEATSALDAESeylvqdAMDSLMAGRTvlvIAHRLSTVKTA-------------DCVAVISDGEV 611
Cdd:cd03233 141 CWDNSTRGLDSST------ALEILKCIRT---MADVLKTTTFVslyqasdeiydlfDKVLVLYEGRQ 198
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
407-592 |
6.92e-17 |
|
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: 79.46 E-value: 6.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 407 SRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNC 486
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 SVEENIAYgFDGEASFTDIENAAKMANAHEFiEAFPDKYntvvgerglrLSGGQKQRIAIARALLTNPSVLLLDEATSAL 566
Cdd:cd03231 89 SVLENLRF-WHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*..
gi 22327455 567 DAESEYLVQDAMDS-LMAGRTVLVIAH 592
Cdd:cd03231 157 DKAGVARFAEAMAGhCARGGMVVLTTH 183
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
397-611 |
8.01e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 84.39 E-value: 8.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRPSHM-ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:PRK10535 6 ELKDIRRSYPSGEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 -----IVSQEPILFNCSVEENIaygfDGEASFTDIENAAKMANAHEFIE--AFPDKyntvVGERGLRLSGGQKQRIAIAR 548
Cdd:PRK10535 86 ehfgfIFQRYHLLSHLTAAQNV----EVPAVYAGLERKQRLLRAQELLQrlGLEDR----VEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 549 ALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTVKTADCVAVISDGEV 611
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
396-592 |
8.24e-17 |
|
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: 77.49 E-value: 8.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNgvSLMEISHqylhkqis 475
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG--STVKIGY-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 iVSQepilfncsveeniaygfdgeasftdienaakmanahefieafpdkyntvvgerglrLSGGQKQRIAIARALLTNPS 555
Cdd:cd03221 68 -FEQ--------------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*..
gi 22327455 556 VLLLDEATSALDAESEYLVQDAMDSLmaGRTVLVIAH 592
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSH 125
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
396-622 |
1.01e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.03 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAY-PSRPSHMI-LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSL-MEISHQYL-- 470
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 471 -HKQISIVSQ--EPILFNCSVEENIAYG------FDGEASFTDIENAAKMANAHEFIEAFPdkyntvvgergLRLSGGQK 541
Cdd:PRK13641 83 lRKKVSLVFQfpEAQLFENTVLKDVEFGpknfgfSEDEAKEKALKWLKKVGLSEDLISKSP-----------FELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 542 QRIAIARALLTNPSVLLLDEATSALDAES-EYLVQDAMDSLMAGRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDE 619
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKE 231
|
...
gi 22327455 620 LLS 622
Cdd:PRK13641 232 IFS 234
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
71-346 |
1.07e-16 |
|
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: 80.91 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 71 LVIGTIALLIGSTTNLLVPKFGGMIID--IVSRDVKTPEQQTESLIAVrnavviilliVVIGSICTALRAWLFNSASERV 148
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDegIANGDLSYILRTGLLMLLL----------ALLGLIAGILAGYFAAKASQGF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 149 VARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTL------- 221
Cdd:cd18548 71 GRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALillvaip 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 222 -LALVVVPVISVAVKQFGRYLR---ELSHTTQaaaavaasiaeESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQA 297
Cdd:cd18548 151 iLALVVFLIMKKAIPLFKKVQKkldRLNRVVR-----------ENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAG 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 22327455 298 VLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSLTV 346
Cdd:cd18548 220 RLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQI 268
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
396-621 |
1.33e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.55 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAY-PSRP-SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQY---- 469
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 470 LHKQISIVSQEP--ILFNCSVEENIAYGFDG------EASFTDIENAAKMANAHEFIEAFPdkyntvvgergLRLSGGQK 541
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgipkeKAEKIAAEKLEMVGLADEFWEKSP-----------FELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 542 QRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSL-MAGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDE 619
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230
|
..
gi 22327455 620 LL 621
Cdd:PRK13643 231 VF 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
414-637 |
2.35e-16 |
|
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: 82.18 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFY--DPLKGKILLNGVSLMEIS-HQYLHKQISIVSQEPILF-NCSVE 489
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNiRDTERAGIVIIHQELTLVpELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 490 ENIAYGFDGEASFTDIENAAKMANAHEFIE--AFPDKYNT-VVGERGlrlsGGQKQRIAIARALLTNPSVLLLDEATSAL 566
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMYLRAKNLLRelQLDADNVTrPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 567 -DAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKT-ADCVAVISDGEvaEKGTHD-ELLSLNGIYTNLVKRQLQS 637
Cdd:TIGR02633 173 tEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ--HVATKDmSTMSEDDIITMMVGREITS 244
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
410-615 |
4.94e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.35 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 410 SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYD-----PLKGKILLNGVSLM--EISHQYLHKQISIVSQEPI 482
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYspDVDPIEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 483 LF-NCSVEENIAYG--FDGEASFTD-----IENAAKMANAHEFIEafpDKYNTVVGErglrLSGGQKQRIAIARALLTNP 554
Cdd:PRK14267 96 PFpHLTIYDNVAIGvkLNGLVKSKKelderVEWALKKAALWDEVK---DRLNDYPSN----LSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327455 555 SVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHR-LSTVKTADCVAVISDGEVAEKG 615
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
413-613 |
5.00e-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: 77.86 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTT----IANLiERfydPLKGKILLNGVSLMEISH----QYLHKQISIVSQ-EPIL 483
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTllglLAGL-DR---PTSGTVRLAGQDLFALDEdaraRLRARHVGFVFQsFQLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 484 FNCSVEENIAygfdgeasfTDIENAAkMANAHEFIEAFPDKYNtvVGERgLR-----LSGGQKQRIAIARALLTNPSVLL 558
Cdd:COG4181 103 PTLTALENVM---------LPLELAG-RRDARARARALLERVG--LGHR-LDhypaqLSGGEQQRVALARAFATEPAILF 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 559 LDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTVKTADCVAVISDGEVAE 613
Cdd:COG4181 170 ADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
414-637 |
5.77e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYdP---LKGKILLNGVSLmEISH--QYLHKQISIVSQEPILF-NCS 487
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEEL-QASNirDTERAGIAIIHQELALVkELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 488 VEENIAYGfdGEASFTDIENAAKM-ANAHEFIEAFpdKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSAL 566
Cdd:PRK13549 99 VLENIFLG--NEITPGGIMDYDAMyLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 567 -DAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKT-ADCVAVISDGEvaEKGTHD-ELLSLNGIYTNLVKRQLQS 637
Cdd:PRK13549 175 tESETAVLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR--HIGTRPaAGMTEDDIITMMVGRELTA 246
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
416-620 |
7.21e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.72 E-value: 7.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 416 GISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEI-SHQYLHKQISIVSQEPILF-NCSVEEN-- 491
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVRTFQHVRLFrEMTVIENll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 492 ----------IAYGFDGEASFTDIENAAkMANAHEFIEafpdkyntVVGERGL------RLSGGQKQRIAIARALLTNPS 555
Cdd:PRK11300 103 vaqhqqlktgLFSGLLKTPAFRRAESEA-LDRAATWLE--------RVGLLEHanrqagNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 556 VLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDEL 620
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
71-343 |
8.10e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 78.76 E-value: 8.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 71 LVIGTIALLIGSTTNLLVPKFGGMIIDIVSRDVKT----------PEQQTESLIAVrnaVVIILLIVVIGSICTALRAWL 140
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASflplvpaslgPADPRGQLWLL---GGLTVAAFLLESLFQYLSGVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 141 FNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLT 220
Cdd:cd18565 78 WRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 221 LLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLV 300
Cdd:cd18565 158 LVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLR 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 22327455 301 GLFFGGLNAAFTLSVITVVSYGAYLTIYG------SMTVGALTSFILYS 343
Cdd:cd18565 238 AAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYT 286
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
391-627 |
9.18e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.91 E-value: 9.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 391 NPDGDVELNDVWFAYPSRpshMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYL 470
Cdd:PRK10575 7 HSDTTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 471 HKQISIVSQE-PILFNCSVEENIA---YGFDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGerglrLSGGQKQRIAI 546
Cdd:PRK10575 84 ARKVAYLPQQlPAAEGMTVRELVAigrYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDS-----LSGGERQRAWI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 547 ARALLTNPSVLLLDEATSALDAESEYlvqdamdslmagrTVLVIAHRLSTVKTADCVAVISD----------------GE 610
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQV-------------DVLALVHRLSQERGLTVIAVLHDinmaarycdylvalrgGE 225
|
250 260
....*....|....*....|
gi 22327455 611 VAEKGTHDELL---SLNGIY 627
Cdd:PRK10575 226 MIAQGTPAELMrgeTLEQIY 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
414-637 |
1.63e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.83 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQ-ISIVSQEPILFN-CSVEEN 491
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDeLTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 492 IAYGFDGEASF--TDIENAAKMANAHEFIEAFPD---KYNTVVGErglrLSGGQKQRIAIARALLTNPSVLLLDEATSAL 566
Cdd:PRK09700 101 LYIGRHLTKKVcgVNIIDWREMRVRAAMMLLRVGlkvDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 567 -DAESEYLVQdAMDSLMA-GRTVLVIAHRLSTVK-TADCVAVISDGEVAEKGTHDElLSLNGIYTNLVKRQLQS 637
Cdd:PRK09700 177 tNKEVDYLFL-IMNQLRKeGTAIVYISHKLAEIRrICDRYTVMKDGSSVCSGMVSD-VSNDDIVRLMVGRELQN 248
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
414-592 |
2.66e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQ---YLHKQISIVSQEP-ILFNCSVE 489
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 490 ENIAYGFdgeasftdIENAAKMANAHEFIEAFPDKYNTVVGERG--LRLSGGQKQRIAIARALLTNPSVLLLDEATSALD 567
Cdd:PRK10908 98 DNVAIPL--------IIAGASGDDIRRRVSAALDKVGLLDKAKNfpIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180
....*....|....*....|....*.
gi 22327455 568 -AESEYLVQDAMDSLMAGRTVLVIAH 592
Cdd:PRK10908 170 dALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
414-616 |
2.94e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 76.71 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISH----QYLHKQISIVSQ--EPILFNCS 487
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGLVFQfpESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 488 VEENIAYGFDG------EASFTDIENAAKMANAHEFIEAFPdkyntvvgergLRLSGGQKQRIAIARALLTNPSVLLLDE 561
Cdd:PRK13649 103 VLKDVAFGPQNfgvsqeEAEALAREKLALVGISESLFEKNP-----------FELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 562 ATSALDAESEYLVQDAMDSL-MAGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGT 616
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
396-620 |
6.82e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.19 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLH---K 472
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYtvrK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 QISIVSQEPILF-NCSVEENIAYGFDGEASFTD--IENAAKMAnahefIEAfpdkyntvVGERGL------RLSGGQKQR 543
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAYPLREHTQLPAplLHSTVMMK-----LEA--------VGLRGAaklmpsELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 544 IAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSL--MAGRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDEL 620
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVlSIADHAYIVADKKIVAHGSAQAL 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
394-622 |
9.54e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.04 E-value: 9.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 394 GDVELNDVWFAYPSRP--SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNG----VSLMEISH 467
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 468 -QYLHKQISIVSQEP--ILFNCSVEENIAYG-----FDGEASFTDIENAAKMANahefieaFPDKYntvVGERGLRLSGG 539
Cdd:PRK13645 85 vKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpvnlgENKQEAYKKVPELLKLVQ-------LPEDY---VKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 540 QKQRIAIARALLTNPSVLLLDEATSALDAESEylvQDAMDSLM-----AGRTVLVIAHRLSTV-KTADCVAVISDGEVAE 613
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE---EDFINLFErlnkeYKKRIIMVTHNMDQVlRIADEVIVMHEGKVIS 231
|
....*....
gi 22327455 614 KGTHDELLS 622
Cdd:PRK13645 232 IGSPFEIFS 240
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
395-622 |
1.65e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 74.29 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 395 DVELNDVWFAY-PSRP-SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILL------NGVSLMEIs 466
Cdd:PRK13634 2 DITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 467 hQYLHKQISIVSQ--EPILFNCSVEENIAYGfdgEASFTDIENAAKmANAHEFIEafpdkyntVVG------ERG-LRLS 537
Cdd:PRK13634 81 -KPLRKKVGIVFQfpEHQLFEETVEKDICFG---PMNFGVSEEDAK-QKAREMIE--------LVGlpeellARSpFELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 538 GGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLM--AGRTVLVIAHRLSTV-KTADCVAVISDGEVAEK 614
Cdd:PRK13634 148 GGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQ 227
|
....*...
gi 22327455 615 GTHDELLS 622
Cdd:PRK13634 228 GTPREIFA 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
414-620 |
2.03e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 74.35 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTT-IANL----------IERFY--DPLKGKILLNGVSLMEISHQY----------- 469
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTfIEHLnalllpdtgtIEWIFkdEKNKKKTKEKEKVLEKLVIQKtrfkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 470 LHKQISIVSQ--EPILFNCSVEENIAYGfdgEASF-TDIENAAKMANahefieafpdKYNTVVG------ERG-LRLSGG 539
Cdd:PRK13651 103 IRRRVGVVFQfaEYQLFEQTIEKDIIFG---PVSMgVSKEEAKKRAA----------KYIELVGldesylQRSpFELSGG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 540 QKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSL-MAGRTVLVIAHRLSTV-KTADCVAVISDGEVAEKG-T 616
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGdT 249
|
....
gi 22327455 617 HDEL 620
Cdd:PRK13651 250 YDIL 253
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
414-611 |
2.05e-14 |
|
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: 73.14 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHkQISIV--SQEPILFNCSVEEn 491
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKTQLWWDLPVID- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 492 iayGFDGEASFTDIENAAKMANAHEFIEAFpdKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESE 571
Cdd:cd03267 115 ---SFYLLAAIYDLPPARFKKRLDELSELL--DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22327455 572 YLVQDAMDSLMAGR--TVLVIAHRLSTV-KTADCVAVISDGEV 611
Cdd:cd03267 190 ENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRL 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
412-597 |
2.07e-14 |
|
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: 71.89 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 412 MILKGISLRLTPGSKVALVGPSGGGKTTIAN-LIERFYDPL-KGKILLNGVSLMEishqYLHKQISIVSQEPILFNCS-V 488
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAGViTGEILINGRPLDK----NFQRSTGYVEQQDVHSPNLtV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYgfdgeasftdienAAKManahefieafpdkyntvvgeRGLRLSggQKQRIAIARALLTNPSVLLLDEATSALDA 568
Cdd:cd03232 97 REALRF-------------SALL--------------------RGLSVE--QRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190
....*....|....*....|....*....|
gi 22327455 569 ESEYLVQDAMDSL-MAGRTVLVIAHRLSTV 597
Cdd:cd03232 142 QAAYNIVRFLKKLaDSGQAILCTIHQPSAS 171
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
395-620 |
2.84e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 74.68 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 395 DVELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQylHKQI 474
Cdd:PRK11000 3 SVTLRNVTKAYGDVV---ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 475 SIVSQEPILF-NCSVEENIAYGFD-GEASFTDI----ENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQRIAIAR 548
Cdd:PRK11000 78 GMVFQSYALYpHLSVAENMSFGLKlAGAKKEEInqrvNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 549 ALLTNPSVLLLDEATSALDAESEylVQdaMDSLMA------GRTVLVIAH-RLSTVKTADCVAVISDGEVAEKGTHDEL 620
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDAALR--VQ--MRIEISrlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
404-622 |
2.86e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.00 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 404 AYPSRpshMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLN--GVSLMEIsHQYLHKQISIVSQEP 481
Cdd:PRK10895 12 AYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdeDISLLPL-HARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 482 ILFN-CSVEENIAYGFDGEasfTDIENAAKMANAHEFIEAFpdKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLD 560
Cdd:PRK10895 88 SIFRrLSVYDNLMAVLQIR---DDLSAEQREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 561 EATSALDAESEYLVQDAMDSLM-AGRTVLVIAHRL-STVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
412-615 |
2.87e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.20 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 412 MILKGISLRLTPGSKVALVGPSGGGKT-TIANLIERFydP-----LKGKILLNGvslMEISHQYLH-KQISIVSQEP-IL 483
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PagvrqTAGRVLLDG---KPVAPCALRgRKIATIMQNPrSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 484 FNC-------SVEENIAYGFDG-EASFTDIENAAKMANAHEFIEAFPdkyntvvgergLRLSGGQKQRIAIARALLTNPS 555
Cdd:PRK10418 92 FNPlhtmhthARETCLALGKPAdDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 556 VLLLDEATSALDAESEYLVQDAMDSLMAGRT--VLVIAHRLSTV-KTADCVAVISDGEVAEKG 615
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
412-622 |
3.07e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.04 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 412 MILKGISL--RLTP-------GSKVALVGPSGGGKTT----IANLIerfydPLKGKILLNGVSLMEISHQYLHKQISIVS 478
Cdd:PRK03695 1 MQLNDVAVstRLGPlsaevraGEILHLVGPNGAGKSTllarMAGLL-----PGSGSIQFAGQPLEAWSAAELARHRAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 479 QE-PILFNCSVEENIA-YGFDGEASftdienAAKMANAHEFIEAF--PDKYNTVVGerglRLSGGQKQRIAIARALL--- 551
Cdd:PRK03695 76 QQqTPPFAMPVFQYLTlHQPDKTRT------EAVASALNEVAEALglDDKLGRSVN----QLSGGEWQRVRLAAVVLqvw 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 552 --TNPS--VLLLDEATSALD-AEseylvQDAMDSLM-----AGRTVLVIAHRLS-TVKTADCVAVISDGEVAEKGTHDEL 620
Cdd:PRK03695 146 pdINPAgqLLLLDEPMNSLDvAQ-----QAALDRLLselcqQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEV 220
|
..
gi 22327455 621 LS 622
Cdd:PRK03695 221 LT 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
407-615 |
3.73e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.66 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 407 SRPSHMILKgISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISH---QYLHKQISIVSQEPIl 483
Cdd:PRK10261 334 TREVHAVEK-VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPY- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 484 fnCSVEENIAYGF------------DGEASftdienAAKMANAHEFIEAFPdkyntvvgERGLR----LSGGQKQRIAIA 547
Cdd:PRK10261 412 --ASLDPRQTVGDsimeplrvhgllPGKAA------AARVAWLLERVGLLP--------EHAWRypheFSGGQRQRICIA 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 548 RALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKG 615
Cdd:PRK10261 476 RALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
413-598 |
1.26e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.61 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISH----QYLHKQISIVSQEPILFncsv 488
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaELRNQKLGFIYQFHHLL---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 eeniaygfdgeASFTDIENAA----------KMAN--AHEFIEAfpdkyntvVG------ERGLRLSGGQKQRIAIARAL 550
Cdd:PRK11629 100 -----------PDFTALENVAmplligkkkpAEINsrALEMLAA--------VGlehranHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22327455 551 LTNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTVK 598
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRlqGTAFLVVTHDLQLAK 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
396-568 |
2.76e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 71.80 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRpsHMILKGISLRLTPGSKVALVGPSGGGKTT----IANLiERFYDplkGKILLNG--VSLMEISHqy 469
Cdd:PRK11650 4 LKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTllrmVAGL-ERITS---GEIWIGGrvVNELEPAD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 470 lhKQISIVSQEPILF-NCSVEENIAYG-----FDGEASFTDIENAAKMANahefIEAFPDKyntvvgeRGLRLSGGQKQR 543
Cdd:PRK11650 76 --RDIAMVFQNYALYpHMSVRENMAYGlkirgMPKAEIEERVAEAARILE----LEPLLDR-------KPRELSGGQRQR 142
|
170 180
....*....|....*....|....*
gi 22327455 544 IAIARALLTNPSVLLLDEATSALDA 568
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
411-611 |
2.99e-13 |
|
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: 68.23 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 411 HMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQ-ISIVSQEP----ILFN 485
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkregLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 486 CSVEENIAYGFdgeasftdienaakmanahefieafpdkyntvvgerglRLSGGQKQRIAIARALLTNPSVLLLDEATSA 565
Cdd:cd03215 93 LSVAENIALSS--------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22327455 566 LDAESEYLVQDAMDSL-MAGRTVLVIAHRLSTV-KTADCVAVISDGEV 611
Cdd:cd03215 135 VDVGAKAEIYRLIRELaDAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
414-622 |
4.59e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.82 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPilfncsveeniA 493
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP-----------S 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 494 YGFDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGLR----------LSGGQKQRIAIARALLTNPSVLLLDEAT 563
Cdd:PRK15112 98 TSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLpdhasyyphmLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327455 564 SALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTVK-TADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKhISDQVLVMHQGEVVERGSTADVLA 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
414-636 |
4.92e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSlmeisHQY------LHKQISIVSQE----PIL 483
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-----MRFasttaaLAAGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 484 fncSVEENIAYG-FDGEASFtdIENAAKMANAHEFIEAFPDKY--NTVVGerglRLSGGQKQRIAIARALLTNPSVLLLD 560
Cdd:PRK11288 95 ---TVAENLYLGqLPHKGGI--VNRRLLNYEAREQLEHLGVDIdpDTPLK----YLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 561 EATSALDA-ESEYLVQdAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEVAEkgTHDELLSLN--GIYTNLVKRQL 635
Cdd:PRK11288 166 EPTSSLSArEIEQLFR-VIRELRAeGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDMAQVDrdQLVQAMVGREI 242
|
.
gi 22327455 636 Q 636
Cdd:PRK11288 243 G 243
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
70-346 |
1.02e-12 |
|
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: 69.08 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 70 KLVIGTIALLIGST-TNLLVPKFGGMIIDIVSrdvktPEQQTESLIAVrnavviillivVIGSICTALRAWLFNSASERV 148
Cdd:cd18555 2 KLLISILLLSLLLQlLTLLIPILTQYVIDNVI-----VPGNLNLLNVL-----------GIGILILFLLYGLFSFLRGYI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 149 VARLRK--------DLFRHLMHQEIAFYDVTKTGELLSRLSEDTqIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLT 220
Cdd:cd18555 66 IIKLQTkldkslmsDFFEHLLKLPYSFFENRSSGDLLFRANSNV-YIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 221 LLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLV 300
Cdd:cd18555 145 LIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLS 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 22327455 301 GLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFilYSLTV 346
Cdd:cd18555 225 NILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAF--SSLAG 268
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
410-622 |
1.05e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.86 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 410 SHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPIL-FNCSV 488
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYG-FDGEASFT-----DIENAAKMANAHEFIEAFPDKYNTvvgerglrLSGGQKQRIAIARALLTNPSVLLLDEA 562
Cdd:PRK10253 99 QELVARGrYPHQPLFTrwrkeDEEAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 563 TSALDAESEYLVQDAMDSL--MAGRTVLVIAHRLS-TVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
398-570 |
1.08e-12 |
|
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: 70.73 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 398 LNDVWFAYPsrPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLN-GVSlmeishqylhkqISI 476
Cdd:TIGR03719 7 MNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIK------------VGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 477 VSQEPIL-FNCSVEENIAYGF----DGEASFTDIEN------------AAKMANAHEFIEAfPDKYNTvvgER------- 532
Cdd:TIGR03719 73 LPQEPQLdPTKTVRENVEEGVaeikDALDRFNEISAkyaepdadfdklAAEQAELQEIIDA-ADAWDL---DSqleiamd 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22327455 533 GLR----------LSGGQKQRIAIARALLTNPSVLLLDEATSALDAES 570
Cdd:TIGR03719 149 ALRcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
134-339 |
2.10e-12 |
|
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: 68.29 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 134 TALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQI---IKNAATTnlseALRNVTTALIGVG 210
Cdd:cd18588 59 SGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARVRELESIrqfLTGSALT----LVLDLVFSVVFLA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 211 FMFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETL 290
Cdd:cd18588 135 VMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYV 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22327455 291 KLGLKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSF 339
Cdd:cd18588 215 KASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAF 263
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
413-593 |
2.27e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFY--DPLKGKIllngvslmeishqylhkqisIVSQEPILFNCSVEE 490
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV--------------------DVPDNQFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 491 NIAYGFDGEASfTDIENAAKMANAHEFIEAFPdkyntvvgerglRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAES 570
Cdd:COG2401 105 AIGRKGDFKDA-VELLNAVGLSDAVLWLRRFK------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....*
gi 22327455 571 EYLVQDAMDSLM--AGRTVLVIAHR 593
Cdd:COG2401 172 AKRVARNLQKLArrAGITLVVATHH 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
423-600 |
4.20e-12 |
|
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: 64.32 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 423 PGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLngvslmeishqylhkqisivsqepilfncsveeniaygFDGEASF 502
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------IDGEDIL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 503 TDIENAAKmanahefieafpdkyNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLM 582
Cdd:smart00382 43 EEVLDQLL---------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180
....*....|....*....|....*
gi 22327455 583 -------AGRTVLVIAHRLSTVKTA 600
Cdd:smart00382 108 llllkseKNLTVILTTNDEKDLGPA 132
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
414-622 |
7.20e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEI-SHQYLHKQISIVSQEPILFN-CSVEEN 491
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVAIVPEGRRVFSrMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 492 IAYGfdgeASFTDIEN-AAKMANAHEFieaFPDKYNTVVgERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALdaeS 570
Cdd:PRK11614 101 LAMG----GFFAERDQfQERIKWVYEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---A 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 571 EYLVQDAMDSLM----AGRTVLVIAHRLS-TVKTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK11614 170 PIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
407-616 |
1.18e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.62 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 407 SRPSHMILKGISLRLTPGSKVALVGPSGGGKTT-IANLIERFYDP-------LKGKILLNGVSLMEISHQYLHKQISIVS 478
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTlLKALAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 479 Q--EPIlFNCSVEENIAYG------FDGEASFTD---IENAAKMANAhefieafpdkyNTVVGERGLRLSGGQKQRIAIA 547
Cdd:PRK13547 90 QaaQPA-FAFSAREIVLLGrypharRAGALTHRDgeiAWQALALAGA-----------TALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 548 RAL---------LTNPSVLLLDEATSALDAESEYLVQDAMDSLmaGRT----VLVIAHRLS-TVKTADCVAVISDGEVAE 613
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRL--ARDwnlgVLAIVHDPNlAARHADRIAMLADGAIVA 235
|
...
gi 22327455 614 KGT 616
Cdd:PRK13547 236 HGA 238
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
413-622 |
1.25e-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: 67.52 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERF--YDPLKGKILLNgVSLMEiSHQYLHKQI-----------SIVSQ 479
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYH-VALCE-KCGYVERPSkvgepcpvcggTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 480 EPILFNCS------VEENIA---------YGFDGE-----ASFTDIENAAKMA--NAHEFIEAFPDKYNTVVGERglRLS 537
Cdd:TIGR03269 93 EVDFWNLSdklrrrIRKRIAimlqrtfalYGDDTVldnvlEALEEIGYEGKEAvgRAVDLIEMVQLSHRITHIAR--DLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 538 GGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLM--AGRTVLVIAHRLSTV-KTADCVAVISDGEVAEK 614
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIeDLSDKAIWLENGEIKEE 250
|
....*...
gi 22327455 615 GTHDELLS 622
Cdd:TIGR03269 251 GTPDEVVA 258
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
411-594 |
1.28e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.42 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 411 HMILKGISLRLTPGSKVALVGPSGGGKTTI----ANLI------ERFYDPLKGKILLNGVSLMEISHQYLHKQIsIVSQE 480
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlSGLItgdksaGSHIELLGRTVQREGRLARDIRKSRANTGY-IFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 481 PILFNCSVEENIAYGFDGEASF--TDIENAAKMANAHEFiEAFpdkynTVVG------ERGLRLSGGQKQRIAIARALLT 552
Cdd:PRK09984 96 NLVNRLSVLENVLIGALGSTPFwrTCFSWFTREQKQRAL-QAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22327455 553 NPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRL 594
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQV 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
428-633 |
1.45e-11 |
|
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: 68.12 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 428 ALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLmEISHQYLHKQISIVSQEPILFN-CSVEENIAY-----GFDGEAS 501
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAEHILFyaqlkGRSWEEA 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 502 FTDIENAAKMANAHEfieafpdKYNtvvgERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSL 581
Cdd:TIGR01257 1039 QLEMEAMLEDTGLHH-------KRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 582 MAGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDELLSL--NGIYTNLVKR 633
Cdd:TIGR01257 1108 RSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGTPLFLKNCfgTGFYLTLVRK 1162
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
396-597 |
1.48e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRpshMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGvslmEISHQYLHKQIS 475
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPIlfncSVEENIAygFDGEASFTDIENAAKMANAHEFIEAFPDKyntvvgerglrLSGGQKQRIAIARALLTNPS 555
Cdd:PRK09544 78 LDTTLPL----TVNRFLR--LRPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22327455 556 VLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTV 597
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLV 184
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
413-616 |
2.05e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.66 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERF--YDPLKGKILLNGVSLMEIS-HQYLHKQISIVSQEPILFN-CSV 488
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIEIPgVSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYGFDGEASFTDIENaakmANAHEFIEAFPDKYNTV----------VGErglRLSGGQKQRIAIARALLTNPSVLL 558
Cdd:CHL00131 102 ADFLRLAYNSKRKFQGLPE----LDPLEFLEIINEKLKLVgmdpsflsrnVNE---GFSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 559 LDEATSALDAESEYLVQDAMDSLM-AGRTVLVIAH--RLSTVKTADCVAVISDGEVAEKGT 616
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
404-592 |
2.44e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.68 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 404 AYPsrPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGK-ILLNGVSlmeishqylhkqISIVSQEPI 482
Cdd:PRK11819 15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIK------------VGYLPQEPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 483 L-FNCSVEENIAYGFdGE-----ASFTDI------------ENAAKMANAHEFIEAF------------------PDKyN 526
Cdd:PRK11819 81 LdPEKTVRENVEEGV-AEvkaalDRFNEIyaayaepdadfdALAAEQGELQEIIDAAdawdldsqleiamdalrcPPW-D 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 527 TVVGerglRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAES-----EYLVQdamdslMAGrTVLVIAH 592
Cdd:PRK11819 159 AKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawleQFLHD------YPG-TVVAVTH 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
396-601 |
2.69e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNdvwFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYlHKQIS 475
Cdd:PRK13540 5 IELD---FDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEP-ILFNCSVEENIAYGFDGEASFTDIENAAKMANAHEFIEaFPdkyntvvgeRGLrLSGGQKQRIAIARALLTNP 554
Cdd:PRK13540 78 FVGHRSgINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLID-YP---------CGL-LSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22327455 555 SVLLLDEATSALDAES-EYLVQDAMDSLMAGRTVLVIAHRLSTVKTAD 601
Cdd:PRK13540 147 KLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
145-344 |
3.29e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 64.42 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 145 SERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLAL 224
Cdd:cd18540 70 EMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 225 VVVPVISVAVKQF-------GRYLREL-SHTTQaaaavaasIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQ 296
Cdd:cd18540 150 AVVPVLAVVSIYFqkkilkaYRKVRKInSRITG--------AFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRA 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 22327455 297 AVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILYSL 344
Cdd:cd18540 222 ARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGTLVAFISYAT 269
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
131-343 |
3.71e-11 |
|
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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 64.46 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 131 SICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQiIKNAATTNLSEALRNVTTALIGVG 210
Cdd:cd18783 56 GILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQIER-IRQFLTGQLFGTLLDATSLLVFLP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 211 FMFTSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETL 290
Cdd:cd18783 135 VLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAI 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22327455 291 KLGLKQAVLvGLFFGGLNAAFT-LSVITVVSYGAYLTIYGSMTVGALTSFILYS 343
Cdd:cd18783 215 RARFAVGRL-SNWPQTLTGPLEkLMTVGVIWVGAYLVFAGSLTVGALIAFNMLA 267
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
398-615 |
3.85e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 398 LNDVWFAYpsRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLhkqISIV 477
Cdd:PRK15056 9 VNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 478 SQE-------PILfncsVEENIAYGFDGEASFTDIENAAKMANAHEFIE--AFPDKYNTVVGErglrLSGGQKQRIAIAR 548
Cdd:PRK15056 84 PQSeevdwsfPVL----VEDVVMMGRYGHMGWLRRAKKRDRQIVTAALArvDMVEFRHRQIGE----LSGGQKKRVFLAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 549 ALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTVKTADCVAVISDGEVAEKG 615
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDeGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
416-623 |
4.71e-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: 65.59 E-value: 4.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 416 GISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLN-----------GVSLMEISHQY---LHKQISIVSQEP 481
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPDGRGRAKRYigiLHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 482 ILFNCSveENIAYGFDGEASFTDIENAAKMAN-----AHEFIEAFPDKyntvvgerglrLSGGQKQRIAIARALLTNPSV 556
Cdd:TIGR03269 382 VLDNLT--EAIGLELPDELARMKAVITLKMVGfdeekAEEILDKYPDE-----------LSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 557 LLLDEATSALDAESEYLVQdamDSLMAGR-----TVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLSL 623
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVT---HSILKAReemeqTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
414-620 |
4.85e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.65 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKG-----KILLNG-----VSLMEISHQYLHK----QISIVSQ 479
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdKMLLRRrsrqvIELSEQSAAQMRHvrgaDMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 480 EPI-----LFncSVEENIA------YGFDGEASFTDienAAKMANAHEFIEAfpdkyNTVVGERGLRLSGGQKQRIAIAR 548
Cdd:PRK10261 112 EPMtslnpVF--TVGEQIAesirlhQGASREEAMVE---AKRMLDQVRIPEA-----QTILSRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 549 ALLTNPSVLLLDEATSALD----AESEYLVQDAMDSLMAGrtVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDEL 620
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMG--VIFITHDMGVVaEIADRVLVMYQGEAVETGSVEQI 256
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
414-601 |
1.66e-10 |
|
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: 61.86 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANliERFYDPLKGKILLNGVSLME----ISHQYLHKQISIvSQEPI------- 482
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN--DTLYPALARRLHLKKEQPGNhdriEGLEHIDKVIVI-DQSPIgrtprsn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 483 -------------LFnCSV-------EENIAYGFDGeASFTDIENAAkMANAHEFIEAFP---DKYNTVV---------G 530
Cdd:cd03271 88 patytgvfdeireLF-CEVckgkrynRETLEVRYKG-KSIADVLDMT-VEEALEFFENIPkiaRKLQTLCdvglgyiklG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 531 ERGLRLSGGQKQRIAIARALL---TNPSVLLLDEATSALDAESEYLVQDAMDSLM-AGRTVLVIAHRLSTVKTAD 601
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKCAD 239
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
388-596 |
3.25e-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: 63.03 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 388 PVGNPDGD--VELNDVWFAYPSRpshMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLnGVSLmei 465
Cdd:TIGR03719 313 PPGPRLGDkvIEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 466 shqylhkQISIVSQ--EPILFNCSVEENIAYGFDgeasftDIENAAKMANAHEFIEAF----PDKyNTVVGErglrLSGG 539
Cdd:TIGR03719 386 -------KLAYVDQsrDALDPNKTVWEEISGGLD------IIKLGKREIPSRAYVGRFnfkgSDQ-QKKVGQ----LSGG 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22327455 540 QKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLmAGrTVLVIAH------RLST 596
Cdd:TIGR03719 448 ERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF-AG-CAVVISHdrwfldRIAT 508
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
414-636 |
4.32e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKIllngvslmeishQYLHKQ-------------ISIVSQE 480
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSI------------LYLGKEvtfngpkssqeagIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 481 -PILFNCSVEENIAYGFDGEASFTDIeNAAKM-ANAHEFIEAFPDKYN--TVVGErglrLSGGQKQRIAIARALLTNPSV 556
Cdd:PRK10762 88 lNLIPQLTIAENIFLGREFVNRFGRI-DWKKMyAEADKLLARLNLRFSsdKLVGE----LSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 557 LLLDEATSAL-DAESEYLVQdAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGE-VAEKGTHDelLSLNGIYTNLVK 632
Cdd:PRK10762 163 IIMDEPTDALtDTETESLFR-VIRELKSqGRGIVYISHRLKEIfEICDDVTVFRDGQfIAEREVAD--LTEDSLIEMMVG 239
|
....
gi 22327455 633 RQLQ 636
Cdd:PRK10762 240 RKLE 243
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
414-621 |
4.79e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.26 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTT----IANLIErfydPLKGKILLNGVSLMEISHQYLhKQISIV----SQepILFN 485
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILV----PTSGEVRVLGYVPFKRRKEFA-RRIGVVfgqrSQ--LWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 486 CSVEEniaygfdgeaSFT------DIENAAKMANAHEFIEAF--PDKYNTVVgeRglRLSGGQKQRIAIARALLTNPSVL 557
Cdd:COG4586 111 LPAID----------SFRllkaiyRIPDAEYKKRLDELVELLdlGELLDTPV--R--QLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 558 LLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELL 621
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNRerGTTILLTSHDMDDIeALCDRVIVIDHGRIIYDGSLEELK 243
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
412-597 |
5.10e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 412 MILKGISLRLTPGSKVALVGPSGGGKTTIAN-LIERFYDPL--KGKILLNGVSLMEiSHQylhKQISIVSQEPI-LFNCS 487
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERVTTGVitGGDRLVNGRPLDS-SFQ---RSIGYVQQQDLhLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 488 VEENIAYgfdgeASFTDIENAAKMANAHEFIEAFPD-----KY-NTVVGERGLRLSGGQKQRIAIARALLTNPSVLL-LD 560
Cdd:TIGR00956 853 VRESLRF-----SAYLRQPKSVSKSEKMEYVEEVIKllemeSYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190
....*....|....*....|....*....|....*...
gi 22327455 561 EATSALDAESEYLVQDAMDSLM-AGRTVLVIAHRLSTV 597
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLAdHGQAILCTIHQPSAI 965
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
390-620 |
6.44e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.89 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 390 GNPDGDV-ELNDVWFAypsrpshmilkgislrLTPGSKVALVGPSGGGKTTIANLIERFYDP---LKGKILLNGVSLMEI 465
Cdd:PRK09473 23 STPDGDVtAVNDLNFS----------------LRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 466 SHQYLHK----QISIVSQEPIL-FN--CSVEENIA------YGFDGEASFTD---IENAAKMANAHEFIEAFPDKYntvv 529
Cdd:PRK09473 87 PEKELNKlraeQISMIFQDPMTsLNpyMRVGEQLMevlmlhKGMSKAEAFEEsvrMLDAVKMPEARKRMKMYPHEF---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 530 gerglrlSGGQKQRIAIARALLTNPSVLLLDEATSALDAEseylVQDAMDSLMA------GRTVLVIAHRLSTVK-TADC 602
Cdd:PRK09473 163 -------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVT----VQAQIMTLLNelkrefNTAIIMITHDLGVVAgICDK 231
|
250
....*....|....*...
gi 22327455 603 VAVISDGEVAEKGTHDEL 620
Cdd:PRK09473 232 VLVMYAGRTMEYGNARDV 249
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
396-626 |
7.56e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.91 E-value: 7.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPSHmiLKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS 475
Cdd:PRK10522 323 LELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILFNCSVeeniayGFDGEASftdieNAAKMANAHEFIEaFPDKYnTVVGER--GLRLSGGQKQRIAIARALLTN 553
Cdd:PRK10522 401 AVFTDFHLFDQLL------GPEGKPA-----NPALVEKWLERLK-MAHKL-ELEDGRisNLKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 554 PSVLLLDEAtsALDAESEY---LVQDAMDSLMA-GRTVLVIAHRLSTVKTADCVAVISDGEVAE-KGTHDELLSLNGI 626
Cdd:PRK10522 468 RDILLLDEW--AADQDPHFrreFYQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASRDAV 543
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
407-570 |
8.43e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.05 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 407 SRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNC 486
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 SVEENIAY--GFDGEASFTDIENAAKMANAHEFiEAFPDKYntvvgerglrLSGGQKQRIAIARALLTNPSVLLLDEATS 564
Cdd:PRK13538 90 TALENLRFyqRLHGPGDDEALWEALAQVGLAGF-EDVPVRQ----------LSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
....*.
gi 22327455 565 ALDAES 570
Cdd:PRK13538 159 AIDKQG 164
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
392-611 |
1.04e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.20 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 392 PDGDV--ELNDVWfaYPSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLI--ERfyDPLKGKILLNGVslmEISH 467
Cdd:COG3845 252 EPGEVvlEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGE---DITG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 468 ----QYLHKQISIVSQEP-----ILfNCSVEENIAYGFDGEASFTD--IENAAKM-ANAHEFIEAF---PDKYNTVVGer 532
Cdd:COG3845 325 lsprERRRLGVAYIPEDRlgrglVP-DMSVAENLILGRYRRPPFSRggFLDRKAIrAFAEELIEEFdvrTPGPDTPAR-- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 533 glRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLM-AGRTVLVIAHRLSTV-KTADCVAVISDGE 610
Cdd:COG3845 402 --SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEIlALSDRIAVMYEGR 479
|
.
gi 22327455 611 V 611
Cdd:COG3845 480 I 480
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
413-592 |
1.14e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.02 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISH----QYLHKQISIVSQEPILF-NCS 487
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearaKLRAKHVGFVFQSFMLIpTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 488 VEENIAYG--FDGEASFTDIENAAkmanahEFIEAFPdkyntvVGER----GLRLSGGQKQRIAIARALLTNPSVLLLDE 561
Cdd:PRK10584 105 ALENVELPalLRGESSRQSRNGAK------ALLEQLG------LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190
....*....|....*....|....*....|...
gi 22327455 562 ATSALDAESEYLVQDAMDSLMA--GRTVLVIAH 592
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLNRehGTTLILVTH 205
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
413-609 |
1.26e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTT----IANLIERFYDPLKGKILLNGVSLMEISHQYLHKQISIVSQEPILFNCSV 488
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYGFDGEASFTDIEN------AAKMANAHEFIEAFPDKYNTVVGERGLR-LSGGQKQRIAIARALLTNPSVLLLDE 561
Cdd:TIGR00956 156 GETLDFAARCKTPQNRPDGvsreeyAKHIADVYMATYGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 22327455 562 ATSALDAESEYLVQDAMDSL--MAGRTVLVIAHRLS--TVKTADCVAVISDG 609
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKTSanILDTTPLVAIYQCSqdAYELFDKVIVLYEG 287
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
396-612 |
1.47e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.03 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYlHKQIS 475
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQH-HVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVSQEPILFncsveenIAYGFDGEASftdienaaKMANAHefIEAFpdkynTVVGERGLR----LSGGQKQRIAIARALL 551
Cdd:PLN03073 586 DLSSNPLLY-------MMRCFPGVPE--------QKLRAH--LGSF-----GVTGNLALQpmytLSGGQKSRVAFAKITF 643
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 552 TNPSVLLLDEATSALDAeseylvqDAMDSLMAGRT-----VLVIAHRLSTVK-TADCVAVISDGEVA 612
Cdd:PLN03073 644 KKPHILLLDEPSNHLDL-------DAVEALIQGLVlfqggVLMVSHDEHLISgSVDELWVVSEGKVT 703
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
414-612 |
3.00e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLmEISH--QYLHKQISIVS----QEPILFNCS 487
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIRSprDAIRAGIAYVPedrkGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 488 VEENIAYG-FDGEASFTDIENAAKMANAHEFIEAF----PDKYNTVVgerglRLSGGQKQRIAIARALLTNPSVLLLDEA 562
Cdd:COG1129 347 IRENITLAsLDRLSRGGLLDRRRERALAEEYIKRLriktPSPEQPVG-----NLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 563 TSALDAESEYLVQDAMDSLMA-GRTVLVI----------AHRlstvktadcVAVISDGEVA 612
Cdd:COG1129 422 TRGIDVGAKAEIYRLIRELAAeGKAVIVIsselpellglSDR---------ILVMREGRIV 473
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
131-346 |
5.39e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 57.92 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 131 SICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTaLIG-- 208
Cdd:cd18605 56 SLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFG-LLGyl 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 209 VGFMFTSSWkLTLLALVVVPVISVAVKQF---GRYLRELSHTTQAAAAVAASiaeESFGAVRTVRSFAKESYMVSQYSKK 285
Cdd:cd18605 135 VVICYQLPW-LLLLLLPLAFIYYRIQRYYratSRELKRLNSVNLSPLYTHFS---ETLKGLVTIRAFRKQERFLKEYLEK 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 286 VDETLKLGLKQAVL-----VGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTsfilYSLTV 346
Cdd:cd18605 211 LENNQRAQLASQAAsqwlsIRLQLLGVLIVTFVALTAVVQHFFGLSIDAGLIGLALS----YALPI 272
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
135-336 |
5.63e-09 |
|
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: 57.98 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 135 ALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQiIKNAATTNLSEALRNVTTALIGVGFMFT 214
Cdd:cd18566 60 LLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNSLEQ-IREFLTGQALLALLDLPFVLIFLGLIWY 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 215 SSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMV----SQYSKKVDETL 290
Cdd:cd18566 139 LGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLrryeRLQANAAYAGF 218
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22327455 291 KLGLKQAVLVglffgGLNAAFT-LSVITVVSYGAYLTIYGSMTVGAL 336
Cdd:cd18566 219 KVAKINAVAQ-----TLGQLFSqVSMVAVVAFGALLVINGDLTVGAL 260
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
412-611 |
6.15e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.03 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 412 MILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKI-LLNGVSLMEIS-HQ--YLHKQISIVSQEPILFNCS 487
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAqHQleFLRADESPLQHLARLAPQE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 488 VEENI-----AYGFDGeasftdienaakmanahefieafpDKyntvVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEA 562
Cdd:PRK10636 406 LEQKLrdylgGFGFQG------------------------DK----VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22327455 563 TSALDAESEYLVQDAMDSLmAGRTVLVIAHRLSTVKTADCVAVISDGEV 611
Cdd:PRK10636 458 TNHLDLDMRQALTEALIDF-EGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
514-603 |
1.46e-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: 58.10 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 514 AHEFIEAFPD---KYNTVV---------GERGLRLSGGQKQRIAIARALL---TNPSVLLLDEATSALDAESEYLVQDAM 578
Cdd:TIGR00630 796 AYEFFEAVPSisrKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVL 875
|
90 100
....*....|....*....|....*.
gi 22327455 579 DSLM-AGRTVLVIAHRLSTVKTADCV 603
Cdd:TIGR00630 876 QRLVdKGNTVVVIEHNLDVIKTADYI 901
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
535-620 |
1.90e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.14 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 535 RLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEVA 612
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQeGVAIIVVSSELAEVlGLSDRVLVIGEGKLK 482
|
....*...
gi 22327455 613 EKGTHDEL 620
Cdd:TIGR02633 483 GDFVNHAL 490
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
397-622 |
3.19e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.44 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNG-VSLMEISHQyLHKQIS 475
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGsAALIAISSG-LNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVsqepilfncsveENIA-----YGFDGEASFTDIENAAKMANAHEFIEAFPDKYntvvgerglrlSGGQKQRIAIARAL 550
Cdd:PRK13545 102 GI------------ENIElkglmMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 551 LTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTVKTADCVAV-ISDGEVAEKGTHDELLS 622
Cdd:PRK13545 159 HINPDILVIDEALSVGDQTFTKKCLDKMNEFKEqGKTIFFISHSLSQVKSFCTKALwLHYGQVKEYGDIKEVVD 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
416-621 |
4.14e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.93 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 416 GISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKI--------LLNGVSLMEISHQYLHK-QISIVSQEP---IL 483
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqLRDLYALSEAERRRLLRtEWGFVHQHPrdgLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 484 FNCSVEENIA----------YGfdgeasftDIENAAkmANAHEFIEAFPDKyntvVGERGLRLSGGQKQRIAIARALLTN 553
Cdd:PRK11701 104 MQVSAGGNIGerlmavgarhYG--------DIRATA--GDWLERVEIDAAR----IDDLPTTFSGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22327455 554 PSVLLLDEATSALDAEseylVQ----DAMDSLMA--GRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDELL 621
Cdd:PRK11701 170 PRLVFMDEPTGGLDVS----VQarllDLLRGLVRelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVL 240
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
413-595 |
4.52e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLI--ERFYDPLKGKILLNGVSlmeiSHQYLHKQISIVSQEPILFN--CSV 488
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFP----KKQETFARISGYCEQNDIHSpqVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYgfdgeASF----TDIENAAKMANAHEFIE--AFPDKYNTVVGERGLR-LSGGQKQRIAIARALLTNPSVLLLDE 561
Cdd:PLN03140 971 RESLIY-----SAFlrlpKEVSKEEKMMFVDEVMElvELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190
....*....|....*....|....*....|....*
gi 22327455 562 ATSALDAESEYLVQDAM-DSLMAGRTVLVIAHRLS 595
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
452-611 |
6.01e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 452 KGKILLNGVSLmEISH--QYLHKQISIVSQE-------PILfncSVEENIAYG-FDGEASFTDIENAAKMANAHEFIEAF 521
Cdd:PRK13549 317 EGEIFIDGKPV-KIRNpqQAIAQGIAMVPEDrkrdgivPVM---GVGKNITLAaLDRFTGGSRIDDAAELKTILESIQRL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 522 PDKYNTVVGERGlRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTV-KT 599
Cdd:PRK13549 393 KVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQqGVAIIVISSELPEVlGL 471
|
170
....*....|..
gi 22327455 600 ADCVAVISDGEV 611
Cdd:PRK13549 472 SDRVLVMHEGKL 483
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
134-340 |
7.49e-08 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of 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: 350052 [Multi-domain] Cd Length: 294 Bit Score: 54.48 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 134 TALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTqIIKNAATTNLSEALRNVTTALIGVGFMF 213
Cdd:cd18779 59 GLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNA-TIRELLTSQTLSALLDGTLVLGYLALLF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 214 TSSWKLTLLALVVVPVISVAVKQFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLG 293
Cdd:cd18779 138 AQSPLLGLVVLGLAALQVALLLATRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNAS 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22327455 294 LKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGALTSFI 340
Cdd:cd18779 218 LRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
414-567 |
1.41e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEIS-HQYLHKQISIVSQEP----ILFNCSV 488
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRkrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYGFDGEASFT--DIENAAKMANAHEFIEAFPDKYNTVVGERGLrLSGGQKQRIAIARALLTNPSVLLLDEATSAL 566
Cdd:PRK10762 348 KENMSLTALRYFSRAggSLKHADEQQAVSDFIRLFNIKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
.
gi 22327455 567 D 567
Cdd:PRK10762 427 D 427
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
413-617 |
1.53e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.87 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTI-ANLIERF-YDPLKGKILLNGVSLMEIS-HQYLHKQISIVSQEPI------- 482
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVeipgvsn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 483 LFNCSVEENIAYGFDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVgerGLRLSGGQKQRIAIARALLTNPSVLLLDEA 562
Cdd:PRK09580 96 QFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSV---NVGFSGGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 563 TSALDAESEYLVQDAMDSLMAG-RTVLVIAH--RLSTVKTADCVAVISDGEVAEKGTH 617
Cdd:PRK09580 173 DSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
414-616 |
1.69e-07 |
|
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: 52.80 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGS-----KVALVGPSGGGKTTIANLIERFYDPLKGKIllnGVSLMEISH--QYLH-KQISIVSQepILFN 485
Cdd:cd03237 10 LGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYkpQYIKaDYEGTVRD--LLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 486 csveenIAYGFDGEASF-TDIENaakmanahefieafPDKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATS 564
Cdd:cd03237 85 ------ITKDFYTHPYFkTEIAK--------------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 565 ALDAESEYLVQDAMD--SLMAGRTVLVIAHrlsTVKTADCVA---VISDGEVAEKGT 616
Cdd:cd03237 145 YLDVEQRLMASKVIRrfAENNEKTAFVVEH---DIIMIDYLAdrlIVFEGEPSVNGV 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
414-635 |
1.85e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSL-MEISHQYLHKQISIVSQE-PILFNCSVEEN 491
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 492 IAYG-FDGEASFTDienAAKMANAHEFIEAFPDkYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSAL-DAE 569
Cdd:PRK10982 94 MWLGrYPTKGMFVD---QDKMYRDTKAIFDELD-IDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtEKE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 570 SEYLVQDAMDSLMAGRTVLVIAHRLSTV-KTADCVAVISDGE-VAEKGTHDelLSLNGIYTNLVKRQL 635
Cdd:PRK10982 170 VNHLFTIIRKLKERGCGIVYISHKMEEIfQLCDEITILRDGQwIATQPLAG--LTMDKIIAMMVGRSL 235
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
504-620 |
1.88e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.59 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 504 DIENAAKMANAHEFIEAFpdKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA 583
Cdd:NF000106 115 DLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR 192
|
90 100 110
....*....|....*....|....*....|....*....
gi 22327455 584 -GRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDEL 620
Cdd:NF000106 193 dGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
415-613 |
1.91e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 415 KGISLRLTPGSKVALVGPSGGGKTTIANLIerF-YDPLK-GKILLNGVSlMEISHQY--LHKQISIVSQ---EPILF-NC 486
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCL--FgVDKRAgGEIRLNGKD-ISPRSPLdaVKKGMAYITEsrrDNGFFpNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 SVEENIAY-------GFDGEASFTDIENAAKMA-NAHEFIEAFPDKYNTVVGErglrLSGGQKQRIAIARALLTNPSVLL 558
Cdd:PRK09700 357 SIAQNMAIsrslkdgGYKGAMGLFHEVDEQRTAeNQRELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 559 LDEATSALDAESEYLVQDAMDSLM-AGRTVLVIAHRLSTVKTA-DCVAVISDGEVAE 613
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
396-573 |
2.13e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIAnlierfydplkgKILLNGVSLMEISHQYlhKQIS 475
Cdd:PRK11147 4 ISIHGAWLSFSDAP---LLDNAELHIEDNERVCLVGRNGAGKSTLM------------KILNGEVLLDDGRIIY--EQDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 476 IVS---QEPIL-FNCSVEENIAYGFDGEA----SFTDI----------ENAAKMANAHEFIE-----AFPDKYNTVVGER 532
Cdd:PRK11147 67 IVArlqQDPPRnVEGTVYDFVAEGIEEQAeylkRYHDIshlvetdpseKNLNELAKLQEQLDhhnlwQLENRINEVLAQL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22327455 533 GL-------RLSGGQKQRIAIARALLTNPSVLLLDEATSALDAES-EYL 573
Cdd:PRK11147 147 GLdpdaalsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWL 195
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
414-621 |
2.48e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.51 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNG-VSLMEISHQyLHKQISIVsqEPILFNCsveenI 492
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAISAG-LSGQLTGI--ENIEFKM-----L 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 493 AYGFDGEASFTDIENAAKMANAHEFIEAFPDKYntvvgerglrlSGGQKQRIAIARALLTNPSVLLLDEATSALDaesEY 572
Cdd:PRK13546 112 CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD---QT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 22327455 573 LVQDAMDSLM----AGRTVLVIAHRLSTVKT-ADCVAVISDGEVAEKGTHDELL 621
Cdd:PRK13546 178 FAQKCLDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
396-601 |
3.73e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIE----RFYD---PLKGKILLNGVSLMEIShq 468
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGYSndlTLFGRRRGSGETIWDIK-- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 469 ylhKQISIVSQEPIL---FNCSVEENIAYGFdgeasFTDIEnaakmanaheFIEAFPDKYNTVVGE----RGL------- 534
Cdd:PRK10938 336 ---KHIGYVSSSLHLdyrVSTSVRNVILSGF-----FDSIG----------IYQAVSDRQQKLAQQwldiLGIdkrtada 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 535 ---RLSGGQkQRIA-IARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLV------------IAHRLSTV 597
Cdd:PRK10938 398 pfhSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISeGETQLLfvshhaedapacITHRLEFV 476
|
....
gi 22327455 598 KTAD 601
Cdd:PRK10938 477 PDGD 480
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
417-622 |
3.81e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.44 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 417 ISLRLTPGSKVALVGPSGGGKT----TIANLIERFYDPLKGKILLNGVSLMEIS----HQYLHKQISIVSQEPIlfnCSV 488
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISekerRNLVGAEVAMIFQDPM---TSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYGFDGEASFTDIENAAKMANAHEFIEAFpdkynTVVG----ERGL-----RLSGGQKQRIAIARALLTNPSVLLL 559
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLL-----NQVGipdpASRLdvyphQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 560 DEATSALDAESEYLVQDAMDSL-----MAgrtVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELqqkenMA---LVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
414-635 |
5.31e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYdP---LKGKILLNGvSLMEIS--HQYLHKQISIVSQE----PILf 484
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDG-EVCRFKdiRDSEALGIVIIHQElaliPYL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 485 ncSVEENIaygFDG--EASFTDIENAAKMANAHEFIE--AFPDKYNTVVGERGLrlsgGQKQRIAIARALLTNPSVLLLD 560
Cdd:NF040905 94 --SIAENI---FLGneRAKRGVIDWNETNRRARELLAkvGLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 561 EATSAL-DAESEYLVqDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEVAEK-GTHDELLSLNGIYTNLVKRQL 635
Cdd:NF040905 165 EPTAALnEEDSAALL-DLLLELKAqGITSIIISHKLNEIrRVADSITVLRDGRTIETlDCRADEVTEDRIIRGMVGRDL 242
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
414-592 |
7.83e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGSK-----VALVGPSGGGKTTIANLIERFYDPLKGKILLNgvslMEISH--QYlhkqisIVSQEPIlfnc 486
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKISYkpQY------IKPDYDG---- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 SVEE---NIAYGFDGeaSFTDIENAAKMAnahefIEAFPDKYntvVGErglrLSGGQKQRIAIARALLTNPSVLLLDEAT 563
Cdd:PRK13409 416 TVEDllrSITDDLGS--SYYKSEIIKPLQ-----LERLLDKN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPS 481
|
170 180 190
....*....|....*....|....*....|.
gi 22327455 564 SALDAESEYLVQDAMDSLMAGR--TVLVIAH 592
Cdd:PRK13409 482 AHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
421-594 |
7.97e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 421 LTPGSKVALVGPSGGGKTTIA---------NL------------IERFydplKGKILLN---GVSLMEI--SH--QYlhk 472
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVkilsgelipNLgdyeeepswdevLKRF----RGTELQNyfkKLYNGEIkvVHkpQY--- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 473 qisiVSQEPILFNCSVEENIaygfdgeasftdiENAAKMANAHEFIEAFpdKYNTVVgERGLR-LSGGQKQRIAIARALL 551
Cdd:PRK13409 169 ----VDLIPKVFKGKVRELL-------------KKVDERGKLDEVVERL--GLENIL-DRDISeLSGGELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 22327455 552 TNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRL 594
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
132-291 |
8.10e-07 |
|
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: 51.35 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 132 ICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGF 211
Cdd:cd18580 54 LLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 212 MFTSSWKLTLLALVVVPVISVAVKQFGRYLREL------------SHTTqaaaavaasiaeESFGAVRTVRSFAKESYMV 279
Cdd:cd18580 134 IAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLrrlesesrsplySHFS------------ETLSGLSTIRAFGWQERFI 201
|
170
....*....|..
gi 22327455 280 SQYSKKVDETLK 291
Cdd:cd18580 202 EENLRLLDASQR 213
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
414-616 |
1.04e-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: 51.71 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 414 LKGISLRLTPGS-----KVALVGPSGGGKTTIANLIERFYDPLKGKILLNgvslMEISH--QYLHKQISIvsqepilfnc 486
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----LKISYkpQYISPDYDG---------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 487 SVEENI--AYGFDGEASFTDIENAAKMAnahefIEAFPDKYntvVGErglrLSGGQKQRIAIARALLTNPSVLLLDEATS 564
Cdd:COG1245 417 TVEEFLrsANTDDFGSSYYKTEIIKPLG-----LEKLLDKN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 565 ALDAESEYLVQDAMDSLMAGR--TVLVIAHRLSTVktaDCVA---VISDGEVAEKGT 616
Cdd:COG1245 485 HLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYISdrlMVFEGEPGVHGH 538
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
397-592 |
1.80e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWFAYPSRpshMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLnGVSLmEISH--QYlhkqi 474
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL-EVAYfdQH----- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 475 sivsQEPILFNCSVEENIAygfDGEasfTDIENAAKMANAHEFIEAF---PDKYNTVVGErglrLSGGQKQRIAIARALL 551
Cdd:PRK11147 391 ----RAELDPEKTVMDNLA---EGK---QEVMVNGRPRHVLGYLQDFlfhPKRAMTPVKA----LSGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 22327455 552 TNPSVLLLDEATSALDAESEYLVQDAMDSLMAgrTVLVIAH 592
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELLDSYQG--TVLLVSH 495
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
385-598 |
1.85e-06 |
|
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: 50.90 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 385 DKCPVGNPDGDVELNDVWFAYPSrpshmilkgislrltpGSKVALVGPSGGGKTTIANLIE--------RFYDPLKGKIL 456
Cdd:TIGR00954 455 ENIPLVTPNGDVLIESLSFEVPS----------------GNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 457 LngvslmeishqylhkqisiVSQEPILFNCSVEENIAYG------FDGEASFTDIENAAKMANAHEFIEAfpdkyntvvg 530
Cdd:TIGR00954 519 Y-------------------VPQRPYMTLGTLRDQIIYPdssedmKRRGLSDKDLEQILDNVQLTHILER---------- 569
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22327455 531 ERGLR--------LSGGQKQRIAIARALLTNPSVLLLDEATSALDAEseylVQDAMDSLM--AGRTVLVIAHRLSTVK 598
Cdd:TIGR00954 570 EGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD----VEGYMYRLCreFGITLFSVSHRKSLWK 643
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
523-594 |
2.37e-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: 48.34 E-value: 2.37e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 523 DKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLM--AGRTVLVIAHRL 594
Cdd:cd03222 59 DGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDL 132
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
396-626 |
3.08e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 396 VELNDVWFAYPSRPshmILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKI------------------LL 457
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyyaqdhaydFE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 458 NGVSLMEISHQYlhkqisivSQEpilfncSVEENIAYGFDGEASFT--DIENAAKManahefieafpdkyntvvgerglr 535
Cdd:PRK15064 397 NDLTLFDWMSQW--------RQE------GDDEQAVRGTLGRLLFSqdDIKKSVKV------------------------ 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 536 LSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDsLMAGrTVLVIAH-R--LSTVKTAdCVAVISDGEVA 612
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE-KYEG-TLIFVSHdRefVSSLATR-IIEITPDGVVD 515
|
250
....*....|....
gi 22327455 613 EKGTHDELLSLNGI 626
Cdd:PRK15064 516 FSGTYEEYLRSQGI 529
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
536-627 |
5.78e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 536 LSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEY-LVQDAMDSLMAGRTVLVIAHRL-STVKTADCVAVISDGEVA- 612
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFeIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLVAg 471
|
90
....*....|....*....
gi 22327455 613 ----EKGTHDELLSLNGIY 627
Cdd:PRK10982 472 ivdtKTTTQNEILRLASLH 490
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
417-612 |
8.73e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 8.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 417 ISLRLTPGSKVALVGPSGGGKTTIAnliERFY---DPLKGKILLNGVslmEISH----QYLHKQISIVSQE--------- 480
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELA---ETLYglrPARGGRIMLNGK---EINAlstaQRLARGLVYLPEDrqssglyld 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 481 -PILFN-CSVEENiaygfdgEASFTdIENAAKMANAHEFIEAFPDKYNTVvgERGLR-LSGGQKQRIAIARALLTNPSVL 557
Cdd:PRK15439 356 aPLAWNvCALTHN-------RRGFW-IKPARENAVLERYRRALNIKFNHA--EQAARtLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 558 LLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTV-KTADCVAVISDGEVA 612
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIAAqNVAVLFISSDLEEIeQMADRVLVMHQGEIS 482
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
536-601 |
1.02e-05 |
|
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: 46.55 E-value: 1.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22327455 536 LSGGQKQRIAIARALLTNP--SVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLSTVKTAD 601
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDlGNTVILIEHNLDVLSSAD 156
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
388-592 |
2.54e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 388 PVGNPDGD--VELNDVWFAYPSRpshMILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLnGVSLmei 465
Cdd:PRK11819 315 PPGPRLGDkvIEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 466 shqylhkQISIVSQ--EPILFNCSVEENIAYGFDgeasftDIENAAKMANAHEFIEAF----PDKyNTVVGErglrLSGG 539
Cdd:PRK11819 388 -------KLAYVDQsrDALDPNKTVWEEISGGLD------IIKVGNREIPSRAYVGRFnfkgGDQ-QKKVGV----LSGG 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 22327455 540 QKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLmAGrTVLVIAH 592
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEF-PG-CAVVISH 500
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
423-596 |
3.95e-05 |
|
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: 46.70 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 423 PGSKVALVGPSGGGKTTIANL---------------------IERFydplKGKILlngvslmeisHQYLHK----QISiV 477
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKIlsgelkpnlgdydeepswdevLKRF----RGTEL----------QDYFKKlangEIK-V 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 478 SQEP--IlfncsveENIAYGFDGEASftDI-ENAAKMANAHEFIEAFpdKYNTVVgERGLR-LSGGQKQRIAIARALLTN 553
Cdd:COG1245 163 AHKPqyV-------DLIPKVFKGTVR--ELlEKVDERGKLDELAEKL--GLENIL-DRDISeLSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 22327455 554 PSVLLLDEATSALD----AESEYLVQDAMDSlmaGRTVLVIAHRLST 596
Cdd:COG1245 231 ADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAI 274
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
537-618 |
5.30e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 537 SGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMdsLMAGRTVLVIAHR---LSTVKTaDCVAVISDGEVAE 613
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSHArefLNTVVT-DILHLHGQKLVTY 422
|
....*
gi 22327455 614 KGTHD 618
Cdd:PLN03073 423 KGDYD 427
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
417-622 |
7.34e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.18 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 417 ISLRLTPGSKVALVGPSGGGKTTIANLI------------ERFYdplkgkilLNGVSLMEISHQYLHK----QISIVSQE 480
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtaDRMR--------FDDIDLLRLSPRERRKlvghNVSMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 481 PIlfNC-----SVEENIAYGFDG---EASFTDIENAAKMaNAHEFIEAFPDK-YNTVVGERGLRLSGGQKQRIAIARALL 551
Cdd:PRK15093 98 PQ--SCldpseRVGRQLMQNIPGwtyKGRWWQRFGWRKR-RAIELLHRVGIKdHKDAMRSFPYELTEGECQKVMIAIALA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22327455 552 TNPSVLLLDEATSALDAESEYLVQDAMDSLMA--GRTVLVIAHRLSTV-KTADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKELVT 248
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
418-622 |
8.43e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 418 SLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLHKQIS---------IVSQEPILFNCSV 488
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSdewqrnntdMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 489 EENIAYGFDgeasftdiENAAKMANAHEF-IEAFPDKyntvvgeRGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALD 567
Cdd:PRK10938 103 AEIIQDEVK--------DPARCEQLAQQFgITALLDR-------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 22327455 568 AESEYLVQDAMDSLMAGRTVLV-IAHRLSTVKT-ADCVAVISDGEVAEKGTHDELLS 622
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ 224
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
536-603 |
9.71e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 9.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327455 536 LSGGQKQRIAIARALLT---NPSVLLLDEATSALDAESEYLVQDAMDSLM-AGRTVLVIAHRLSTVKTADCV 603
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYV 881
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
390-616 |
1.17e-04 |
|
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: 45.39 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 390 GNPDGDVELNDVWFAYPSRPSHMILKgISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSlmeishqy 469
Cdd:TIGR01257 1932 GNKTDILRLNELTKVYSGTSSPAVDR-LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKS-------- 2002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 470 lhkqisivsqepILFNCS-VEENIAY--GFDgeaSFTDIENAAKMANAHEFIEAFPDK-----YNTVVGERGLRL----- 536
Cdd:TIGR01257 2003 ------------ILTNISdVHQNMGYcpQFD---AIDDLLTGREHLYLYARLRGVPAEeiekvANWSIQSLGLSLyadrl 2067
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 537 ----SGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLM-AGRTVLVIAHRLStvktaDCVAVISDGEV 611
Cdd:TIGR01257 2068 agtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIrEGRAVVLTSHSME-----ECEALCTRLAI 2142
|
....*
gi 22327455 612 AEKGT 616
Cdd:TIGR01257 2143 MVKGA 2147
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
397-623 |
1.21e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 397 ELNDVWfAYPSRP---SHMILKG---------ISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGvslme 464
Cdd:PRK11288 241 EIGDIY-GYRPRPlgeVRLRLDGlkgpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG----- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 465 ishqylhKQISIVS-----------------QEPILFNCSVEENI---AYGFDGEASFTdIENAAKMANAHEFIEAFPDK 524
Cdd:PRK11288 315 -------KPIDIRSprdairagimlcpedrkAEGIIPVHSVADNInisARRHHLRAGCL-INNRWEAENADRFIRSLNIK 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 525 ynTVVGERGLR-LSGGQKQRIAIARALLTNPSVLLLDEATSALD--AESEylVQDAMDSLMA-GRTVLVIAHRLSTV-KT 599
Cdd:PRK11288 387 --TPSREQLIMnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDvgAKHE--IYNVIYELAAqGVAVLFVSSDLPEVlGV 462
|
250 260
....*....|....*....|....*....
gi 22327455 600 ADCVAVISDGEVA-----EKGTHDELLSL 623
Cdd:PRK11288 463 ADRIVVMREGRIAgelarEQATERQALSL 491
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
402-590 |
1.22e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 402 WFAY-PSRPSHMILKGISLRLTPGSKVALVGPSGGGKTTIA-NLIERFYDP-LKGKILLNG--VSLMEISHQYLH----- 471
Cdd:NF040905 263 WTVYhPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGkeVDVSTVSDAIDAglayv 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 472 ----KQISIVSQEPILFNCSveeniAYGFDGEASFTDIENAAKMANAHEFIEAFPDKYNTVVGERGlRLSGGQKQRIAIA 547
Cdd:NF040905 343 tedrKGYGLNLIDDIKRNIT-----LANLGKVSRRGVIDENEEIKVAEEYRKKMNIKTPSVFQKVG-NLSGGNQQKVVLS 416
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 22327455 548 RALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVI 590
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAeGKGVIVI 460
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
134-288 |
1.31e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 44.48 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 134 TALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGVGF-M 212
Cdd:cd18599 75 SLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIiA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 213 FTSSWklTLLALVVVPVI-SVAVKQFGRYLREL------------SHTTqaaaavaasiaeESFGAVRTVRSFAKESYMV 279
Cdd:cd18599 155 IVFPW--FLIALIPLAIIfVFLSKIFRRAIRELkrlenisrsplfSHLT------------ATIQGLSTIHAFNKEKEFL 220
|
....*....
gi 22327455 280 SQYSKKVDE 288
Cdd:cd18599 221 SKFKKLLDQ 229
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
417-600 |
1.44e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 417 ISLRLTPGSKVALVGPSGGGKTTIANLIERFYDPLKGKILLNGVSLMEISHQYLhkqISIVSQEPILFNCSVEENIAYgf 496
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC---TYIGHNLGLKLEMTVFENLKF-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 497 dgeasFTDIENAAKMANA--HEFieafpdKYNTVVGERGLRLSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLV 574
Cdd:PRK13541 94 -----WSEIYNSAETLYAaiHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170 180
....*....|....*....|....*...
gi 22327455 575 QD--AMDSlMAGRTVLVIAHRLSTVKTA 600
Cdd:PRK13541 163 NNliVMKA-NSGGIVLLSSHLESSIKSA 189
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
413-621 |
1.76e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 413 ILKGISLRLTPGSKVALVGPSGGGKTTIANLIERFYDP---LKGKILLNGVSLME---------ISHQYLHKQISIVsQE 480
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPslkVSGEITYNGYRLNEfvprktsayISQNDVHVGVMTV-KE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 481 PILFNCSVEeNIAYGFDGEASFTDIENAAKM-----------ANAHEFIEA--FPDkY-----------NTVVGERGLR- 535
Cdd:PLN03140 259 TLDFSARCQ-GVGTRYDLLSELARREKDAGIfpeaevdlfmkATAMEGVKSslITD-YtlkilgldickDTIVGDEMIRg 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 536 LSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMAGRTVLVIAHRLS----TVKTADCVAVISDGEV 611
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapeTFDLFDDIILLSEGQI 416
|
250
....*....|
gi 22327455 612 AEKGTHDELL 621
Cdd:PLN03140 417 VYQGPRDHIL 426
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
536-595 |
2.04e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 43.51 E-value: 2.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 536 LSGGQKQRIAIARALLTNPSVLLLDEATSALDAESEYLVQDAMDSLMA-GRTVLVIAHRLS 595
Cdd:cd03236 140 LSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLA 200
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
156-339 |
2.84e-04 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they 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: 350013 [Multi-domain] Cd Length: 294 Bit Score: 43.23 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 156 LFRHLMHQEIAFYDVTKTGELLSRLSEDTQIiKNAATTNLSEALRNVTTALIGVGFMFTSSWKLTLLALVVVPVISVAVK 235
Cdd:cd18569 81 FFWHVLRLPVEFFSQRYAGDIASRVQSNDRV-ANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 236 QFGRYLRELSHTTQAAAAVAASIAEESFGAVRTVRSFAKESYMVSQ----YSKKVDETLKLGLKQAVLVGL--FFGGLNA 309
Cdd:cd18569 160 LVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESDFFSRwagyQAKVLNAQQELGRTNQLLGALptLLSALTN 239
|
170 180 190
....*....|....*....|....*....|
gi 22327455 310 AFTLSVitvvsyGAYLTIYGSMTVGALTSF 339
Cdd:cd18569 240 AAILGL------GGLLVMDGALTIGMLVAF 263
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
531-592 |
3.42e-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: 42.21 E-value: 3.42e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22327455 531 ERGlRLSGGQKQ------RIAIARALLTNPSVLLLDEATSALDAES--EYLVQ--DAMDSLmAGRTVLVIAH 592
Cdd:cd03240 112 MRG-RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENieESLAEiiEERKSQ-KNFQLIVITH 181
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
421-601 |
4.21e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.19 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 421 LTPGSKVALVGPSGGGKTTIANlierfydplkgKILLngVSLMEISHQYLHKQISIVSQEPilfncsveeniaygfdgea 500
Cdd:cd03227 18 FGEGSLTIITGPNGSGKSTILD-----------AIGL--ALGGAQSATRRRSGVKAGCIVA------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 501 sftdienaakmanaheFIEAFPdkYNTVVGerglrLSGGQKQRIAIARAL---LTNPSVL-LLDEATSALDAESEYLVQD 576
Cdd:cd03227 66 ----------------AVSAEL--IFTRLQ-----LSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQALAE 122
|
170 180
....*....|....*....|....*.
gi 22327455 577 A-MDSLMAGRTVLVIAHRLSTVKTAD 601
Cdd:cd03227 123 AiLEHLVKGAQVIVITHLPELAELAD 148
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
536-601 |
4.74e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.48 E-value: 4.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 536 LSGGQKQRIAIARALL---TNPSVLLLDEATSAL---DaeseylVQDAMDSLM----AGRTVLVIAHRLSTVKTAD 601
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLhfhD------IRKLLEVLHrlvdKGNTVVVIEHNLDVIKTAD 896
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
78-336 |
5.46e-04 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 42.49 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 78 LLIGSTTNLLVPKFGGMIIDIVSRDVKTPEQQTESLI----AVRnavviillivVIGSICTALRAWLFNSASERVVARLR 153
Cdd:cd18582 5 LVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLLlaygLAR----------ILSSLFNELRDALFARVSQRAVRRLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 154 KDLFRHLMHQEIAFYDVTKTGELlsrlsedTQIIkNAATTNLSEALRNVT-----TAL--IGVGFMFTS--SWKLTLLAL 224
Cdd:cd18582 75 LRVFRHLHSLSLRFHLSRKTGAL-------SRAI-ERGTRGIEFLLRFLLfnilpTILelLLVCGILWYlyGWSYALITL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 225 VVvpvisvavkqFGRYLRELSHTTQAAAAVAASIAEESFGA----------VRTVRSFAKESYMVSQYSKKVDETLKLGL 294
Cdd:cd18582 147 VT----------VALYVAFTIKVTEWRTKFRREMNEADNEAnakavdsllnYETVKYFNNEEYEAERYDKALAKYEKAAV 216
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 22327455 295 KQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGAL 336
Cdd:cd18582 217 KSQTSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDF 258
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
514-601 |
1.07e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.37 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 514 AHEFIEAFP---DKYNTVVgERGL----------RLSGGQKQRIAIARALL---TNPSVLLLDEATSALDAESeylVQDA 577
Cdd:PRK00349 797 ALEFFEAIPkiaRKLQTLV-DVGLgyiklgqpatTLSGGEAQRVKLAKELSkrsTGKTLYILDEPTTGLHFED---IRKL 872
|
90 100
....*....|....*....|....*...
gi 22327455 578 MDSLM----AGRTVLVIAHRLSTVKTAD 601
Cdd:PRK00349 873 LEVLHrlvdKGNTVVVIEHNLDVIKTAD 900
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
536-627 |
1.10e-03 |
|
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: 42.31 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 536 LSGGQKQRIAIARAL---LTnpSVL-LLDEATSAL-DAESEYLVQDAMDSLMAGRTVLVIAHRLSTVKTADCV------A 604
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgLT--GVLyVLDEPSIGLhQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVidigpgA 566
|
90 100
....*....|....*....|....*..
gi 22327455 605 VISDGEVAEKGTHDELL----SLNGIY 627
Cdd:TIGR00630 567 GEHGGEVVASGTPEEILanpdSLTGQY 593
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
78-342 |
1.33e-03 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 40.97 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 78 LLIGSTTNLLVPKFGGMIIDIVSRDVKT-PEQQTESLIAVRnavviillIVVIGSICTALRAWLFN---SASERVVARLr 153
Cdd:cd18583 5 LLAERVLNVLVPRQLGIIVDSLSGGSGKsPWKEIGLYVLLR--------FLQSGGGLGLLRSWLWIpveQYSYRALSTA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 154 kdLFRHLMHQEIAFYDVTKTGELLSrlsedtQIIKNAATTNLSE--------ALRNVTTALIGVGFMFTSSWKLTLLA-- 223
Cdd:cd18583 76 --AFNHVMNLSMDFHDSKKSGEVLK------AIEQGSSINDLLEqilfqivpMIIDLVIAIVYLYYLFDPYMGLIVAVvm 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 224 ---LVVVPVISVAVKQFGRYLRELSHTTqaaaavaASIAEESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKqaVLV 300
Cdd:cd18583 148 vlyVWSTIKLTSWRTKLRRDMIDADREE-------RSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERK--YLF 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 22327455 301 GLFFGGL--NAAFTLSVITVVSYGAYLTIYGSMTVGALTSFILY 342
Cdd:cd18583 219 SLNLLNAvqSLILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTY 262
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
261-336 |
2.55e-03 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 40.11 E-value: 2.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22327455 261 ESFGAVRTVRSFAKESYMVSQYSKKVDETLKLGLKQAVLVGLFFGGLNAAFTLSVITVVSYGAYLTIYGSMTVGAL 336
Cdd:cd18587 184 ESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGGL 259
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
536-603 |
3.18e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 3.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22327455 536 LSGGQKQRIAIARALLTNPSVLL--LDEATSALDAESEYLVQDAMDSLM-AGRTVLVIAHRLSTVKTADCV 603
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHV 208
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
130-224 |
5.14e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 39.37 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22327455 130 GSICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSEDTQIIKNAATTNLSEALRNVTTALIGV 209
Cdd:cd18604 56 SVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVIL 135
|
90
....*....|....*
gi 22327455 210 GFMFTSSWKLTLLAL 224
Cdd:cd18604 136 IAIVVVSPAFLLPAV 150
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
539-567 |
6.35e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 6.35e-03
10 20
....*....|....*....|....*....
gi 22327455 539 GQKQRIAIARALLTNPSVLLLDEATSALD 567
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
131-182 |
9.13e-03 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 38.54 E-value: 9.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 22327455 131 SICTALRAWLFNSASERVVARLRKDLFRHLMHQEIAFYDVTKTGELLSRLSE 182
Cdd:cd18584 51 ALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTE 102
|
|
| |
