|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
89-678 |
5.16e-157 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 481.97 E-value: 5.16e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 89 ISYFALYRYATklewIIIVVSSICAIAAGAVLPLMTvvfgslsgtfQGMFQGTMSNGEFnDELVKFVLYFVYLFIGEFFT 168
Cdd:COG1132 13 LRYLRPYRGLL----ILALLLLLLSALLELLLPLLL----------GRIIDALLAGGDL-SALLLLLLLLLGLALLRALL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 169 CYIATVGWIYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGF 248
Cdd:COG1132 78 SYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 249 VKYWKLTLILCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEhlVIAEYWG 328
Cdd:COG1132 158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFRE--ANEELRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 329 KKMKTVLAS--MLGAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVLTILLAVMIGAFSLGNIGPWLQAFTTATAAASKMY 406
Cdd:COG1132 236 ANLRAARLSalFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 407 STIDRVSPLDPTsKEGRRLENLQGRVELRQVKHIYPsrPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDP 486
Cdd:COG1132 316 ELLDEPPEIPDP-PGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 487 VGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIKHGLIGTQyehlehekvREMVYNAAKMSNAHDFVSALP 566
Cdd:COG1132 393 TSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDAT---------DEEVEEAAKAAQAHEFIEALP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 567 EGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADK 646
Cdd:COG1132 464 DGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADR 543
|
570 580 590
....*....|....*....|....*....|..
gi 407923078 647 IVVMSQGRIVEQGTHNELLERKQAYYNLVEAQ 678
Cdd:COG1132 544 ILVLDDGRIVEQGTHEELLARGGLYARLYRLQ 575
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
767-1085 |
2.74e-143 |
|
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: 435.73 E-value: 2.74e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 767 ASFNRQEWLLMVQGLFWSIIAGGGNPTQAVFFAKSISALSRPPSEygKLRSEANFWSLMYLMLALTQLISFTGQGLCFAI 846
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDD--ELRSEANFWALMFLVLAIVAGIAYFLQGYLFGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 847 CSEKLIHRVRDTAFRTMLRQDISFFDQEENSAGALTSFLSTETTSLAGLSGATLGTIFTVLTTLIGALVLGIAIGWKLGL 926
Cdd:cd18578 79 AGERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 927 VCASTIPVLLACGFLRFWILARFEQRSKKAYEKSASYACEATSAIRTVASLTREEDVYASYHQQLVDQGAKNLRSILKSS 1006
Cdd:cd18578 159 VGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 1007 TLYALSQSGMFLCTALGFWYGGTLISKGEYSLFQFFVCFSAITFGAQSAGTIFSFAPDMGKAKHAAIQLKTLFDRKPEI 1085
Cdd:cd18578 239 LGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
432-678 |
2.32e-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: 403.84 E-value: 2.32e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQIS 511
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFATTIFDNIKHGLigtqyehleHEKVREMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIA 591
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGK---------PDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 592 RAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAY 671
Cdd:cd03249 152 RALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVY 231
|
....*..
gi 407923078 672 YNLVEAQ 678
Cdd:cd03249 232 AKLVKAQ 238
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
89-1229 |
2.46e-127 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 426.75 E-value: 2.46e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 89 ISYFALYRYATKLEWIIIVVSSICAIAAGAVLPLMTVVFGslsgtfqgMFQGTMSNGE-FNDELVKFVLYFVYLFIGEFF 167
Cdd:PTZ00265 45 IPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSVFG--------VIMKNMNLGEnVNDIIFSLVLIGIFQFILSFI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 168 TCYIATVgwiyVGERISSRIREYYLSAILRQNvGYFDKLGAGeitTRITADANLVQDGISEKVGLVQQSLATFITAFVIG 247
Cdd:PTZ00265 117 SSFCMDV----VTTKILKTLKLEFLKSVFYQD-GQFHDNNPG---SKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 248 FVkyWKL----TLILCST-IFAIVFTMGGGSTFIMKYNKQSLASYALGG-TVVEEVFSSIRNAVAFGTQDKLARQYNEHL 321
Cdd:PTZ00265 189 YI--WSLfknaRLTLCITcVFPLIYICGVICNKKVKINKKTSLLYNNNTmSIIEEALVGIRTVVSYCGEKTILKKFNLSE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 322 VIAEYWGKKMKTVLASMLGAMMTIVYLNYGLAFWMGSRYLVK--------GEMSLSDVLTILLAVMIGAFSLGNIGPWLQ 393
Cdd:PTZ00265 267 KLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNIT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 394 AFTTATAAASKMYSTIDRvSPLDPTSKEGRRLENLQgRVELRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGK 473
Cdd:PTZ00265 347 EYMKSLEATNSLYEIINR-KPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGK 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 474 STIVGLVERFYDPVGGEVLL-DGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIKHGL--------IGTQYEH----- 539
Cdd:PTZ00265 425 STILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdleaLSNYYNEdgnds 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 540 ------------------------------LEHEKVREM-----VYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQ 584
Cdd:PTZ00265 505 qenknkrnscrakcagdlndmsnttdsnelIEMRKNYQTikdseVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQ 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 585 KQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALD--RAAQGRTTIVIAHRLSTIKTADKIVVMSQ---------- 652
Cdd:PTZ00265 585 KQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNrergstvdvd 664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 653 -------------------------------------GRIVEQGTHNELLERKQA-YYNLVEaqriaaaNEKIEEEEEEE 694
Cdd:PTZ00265 665 iigedptkdnkennnknnkddnnnnnnnnnnkinnagSYIIEQGTHDALMKNKNGiYYTMIN-------NQKVSSKKSSN 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 695 EEVDltevDDETIKRTVSPQSEkRSYsvDPDDDVAARLKRTQSGKSESSVALAKKQPASEQK------------------ 756
Cdd:PTZ00265 738 NDND----KDSDMKSSAYKDSE-RGY--DPDEMNGNSKHENESASNKKSCKMSDENASENNAggklpflrnlfkrkpkap 810
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 757 YSLATLIKLIASFNRQewllmVQGLFWSII-AGGGNPTQAVFFAKSISALsrppSEYGKLRSEANFWSLMYLMLALTQLI 835
Cdd:PTZ00265 811 NNLRIVYREIFSYKKD-----VTIIALSILvAGGLYPVFALLYAKYVSTL----FDFANLEANSNKYSLYILVIAIAMFI 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 836 SFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQEENSAGALTSFLSTETTSL-AGLSGATLgtIFTVLTTL-IGA 913
Cdd:PTZ00265 882 SETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLkTGLVNNIV--IFTHFIVLfLVS 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 914 LVLGIAIGWKLGLVCASTIPVLLACGFLRFWILARFEQRSKKAYEKSASYACEATSAI-RTVASLTRE------------ 980
Cdd:PTZ00265 960 MVMSFYFCPIVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVFAYNSDDEIfKDPSFLIQEafynmntviiyg 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 981 -EDVYASYHQQLVDQGAK-NLRSILKSSTLYALSQSGMFLCTALGFWYGGTLISKGEYSLFQFFVCFSAITFGAQSAGTI 1058
Cdd:PTZ00265 1040 lEDYFCNLIEKAIDYSNKgQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKL 1119
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1059 FSFAPDMGKAKHAAIQLKTLFDRKPEIDTWSSDGEKI---NNMEGHIEFRNVHFRYPTRPEQPVLRGLNLSVKPGQYVAL 1135
Cdd:PTZ00265 1120 MSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIknkNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAI 1199
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1136 VGASGCGKSTTIALLERFY-----------NPLT-------------------------------------------GGI 1161
Cdd:PTZ00265 1200 VGETGSGKSTVMSLLMRFYdlkndhhivfkNEHTndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKI 1279
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 1162 YADGKEISSLNINDYRSYIALVSQEPTLYQGTIRDNILLGadRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:PTZ00265 1280 LLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG--KEDATREDVKRACKFAAIDEFIESLP 1345
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
106-393 |
6.99e-118 |
|
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: 367.96 E-value: 6.99e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 106 IVVSSICAIAAGAVLPLMTVVFGSLSGTFQGMFQGTMSNGEFNDELVKFVLYFVYLFIGEFFTCYIATVGWIYVGERISS 185
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 186 RIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLILCSTIFAI 265
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 266 VFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLVIAEYWGKKMKTVLASMLGAMMTI 345
Cdd:cd18577 161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 407923078 346 VYLNYGLAFWMGSRYLVKGEMSLSDVLTILLAVMIGAFSLGNIGPWLQ 393
Cdd:cd18577 241 IFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQ 288
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
143-678 |
1.78e-117 |
|
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: 377.12 E-value: 1.78e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 143 SNGEFNDELVKFVLYFVYLFIGEFFTCYIATvgwiYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLV 222
Cdd:TIGR02204 53 SSGLLNRYFAFLLVVALVLALGTAARFYLVT----WLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 223 QDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLILCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIR 302
Cdd:TIGR02204 129 QSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 303 NAVAFGTQDKLARQYNEHLVIAEYWGKKMKTVLASMLGAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVLTILLAVMIGA 382
Cdd:TIGR02204 209 TVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 383 FSLGNIGP-W--LQAFTTATAAASKMYSTIDRVS-PLDPTSKEGRrlenLQGRVELRQVKHIYPSRPEVTVMNGVDLVVE 458
Cdd:TIGR02204 289 GSIGTLSEvWgeLQRAAGAAERLIELLQAEPDIKaPAHPKTLPVP----LRGEIEFEQVNFAYPARPDQPALDGLNLTVR 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 459 AGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIKHGLIgtqye 538
Cdd:TIGR02204 365 PGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRP----- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 539 hlehEKVREMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVV 618
Cdd:TIGR02204 440 ----DATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLV 515
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 619 QAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAYYNLVEAQ 678
Cdd:TIGR02204 516 QQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
178-678 |
1.27e-114 |
|
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: 374.17 E-value: 1.27e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 178 YVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITaDANLVQDGISEK-VGLVQQSLATFITAFVIGFVkYWKLTL 256
Cdd:COG2274 222 RLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSlLTALLDLLFVLIFLIVLFFY-SPPLAL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 257 ILCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLVIAEYWGKKMKTVLA 336
Cdd:COG2274 300 VVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSN 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 337 SMLGAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVL--TILLAVMIGAF-SLGNIGPWLQafttataaasKMYSTIDRVS 413
Cdd:COG2274 380 LLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIafNILSGRFLAPVaQLIGLLQRFQ----------DAKIALERLD 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 414 PL------DPTSKEGRRLENLQGRVELRQVKHIYPSRpEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPV 487
Cdd:COG2274 450 DIldlppeREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 488 GGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIKHGligtqYEHLEHEKVREmvynAAKMSNAHDFVSALPE 567
Cdd:COG2274 529 SGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLG-----DPDATDEEIIE----AARLAGLHDFIEALPM 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 568 GYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKI 647
Cdd:COG2274 600 GYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRI 679
|
490 500 510
....*....|....*....|....*....|.
gi 407923078 648 VVMSQGRIVEQGTHNELLERKQAYYNLVEAQ 678
Cdd:COG2274 680 IVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
178-675 |
2.24e-114 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 373.29 E-value: 2.24e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 178 YVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLI 257
Cdd:TIGR00958 227 YTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMV 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 258 LCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHL-VIAEYWGKKMKTVLA 336
Cdd:TIGR00958 307 TLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALeETLQLNKRKALAYAG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 337 -----SMLGAMMTIVYLNYGLafwmgsrYLV-KGEMSLSDVLTILLAVM-IG--AFSLGNIGPWLQAFTTATaaaSKMYS 407
Cdd:TIGR00958 387 ylwttSVLGMLIQVLVLYYGG-------QLVlTGKVSSGNLVSFLLYQEqLGeaVRVLSYVYSGMMQAVGAS---EKVFE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 408 TIDRVSPLDPTSkeGRRLENLQGRVELRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPV 487
Cdd:TIGR00958 457 YLDRKPNIPLTG--TLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 488 GGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIKHGLigTQYEhlehekvREMVYNAAKMSNAHDFVSALPE 567
Cdd:TIGR00958 535 GGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGL--TDTP-------DEEIMAAAKAANAHDFIMEFPN 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 568 GYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAalDRAAQGRTTIVIAHRLSTIKTADKI 647
Cdd:TIGR00958 606 GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQI 683
|
490 500
....*....|....*....|....*...
gi 407923078 648 VVMSQGRIVEQGTHNELLERKQAYYNLV 675
Cdd:TIGR00958 684 LVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
90-674 |
2.01e-111 |
|
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: 360.96 E-value: 2.01e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 90 SYFALYRYAtKLEWIIIVVSSICAIAAGAVLPLMTVVFGSL-SGTFqgmfqgtmsnGEFNDELVKFV-LYFVYLF----I 163
Cdd:TIGR02203 1 TFRRLWSYV-RPYKAGLVLAGVAMILVAATESTLAALLKPLlDDGF----------GGRDRSVLWWVpLVVIGLAvlrgI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 164 GEFFTCYIatVGWiyVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITA 243
Cdd:TIGR02203 70 CSFVSTYL--LSW--VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 244 FVIGFVKYWKLTLILCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEhlVI 323
Cdd:TIGR02203 146 FIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDA--VS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 324 AEYWGKKMKTVLASMLGAMMTIVYLNYGLAFWM-------GSRYLVKGEmsLSDVLTILLAVMIGAFSLGNIGPWLQaft 396
Cdd:TIGR02203 224 NRNRRLAMKMTSAGSISSPITQLIASLALAVVLfialfqaQAGSLTAGD--FTAFITAMIALIRPLKSLTNVNAPMQ--- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 397 tataaasKMYSTIDRV-SPLD--PTSKEGRR-LENLQGRVELRQVKHIYPSRpEVTVMNGVDLVVEAGKTTALVGASGSG 472
Cdd:TIGR02203 299 -------RGLAAAESLfTLLDspPEKDTGTRaIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 473 KSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIKHGLIGtqyehlehEKVREMVYNA 552
Cdd:TIGR02203 371 KSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTE--------QADRAEIERA 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 553 AKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTI 632
Cdd:TIGR02203 443 LAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTL 522
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 407923078 633 VIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAYYNL 674
Cdd:TIGR02203 523 VIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
307-685 |
1.12e-104 |
|
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: 343.73 E-value: 1.12e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 307 FGTQDKLARQYNEHLVIAEYWGKKMKTVLASMLGAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVltillaVMIGAF--- 383
Cdd:COG5265 234 FGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDF------VLVNAYliq 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 384 -----------------SLGNIGpwlqafttataaasKMYSTIDRvsPLDPTSKEGRR-LENLQGRVELRQVKHIY-PSR 444
Cdd:COG5265 308 lyiplnflgfvyreirqALADME--------------RMFDLLDQ--PPEVADAPDAPpLVVGGGEVRFENVSFGYdPER 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 445 PevtVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTI 524
Cdd:COG5265 372 P---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTI 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 525 FDNIKHGLIGTQyehlehekvREMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLD 604
Cdd:COG5265 449 AYNIAYGRPDAS---------EEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFD 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 605 EATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAYYNLVEAQRIAAAN 684
Cdd:COG5265 520 EATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEA 599
|
.
gi 407923078 685 E 685
Cdd:COG5265 600 E 600
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
432-674 |
1.26e-103 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 326.88 E-value: 1.26e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEvTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQIS 511
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFATTIFDNIKHGLigtqyehleHEKVREMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIA 591
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR---------PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 592 RAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAY 671
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
...
gi 407923078 672 YNL 674
Cdd:cd03251 231 AKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
432-678 |
5.83e-97 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 309.16 E-value: 5.83e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPsrPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQIS 511
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFATTIFDNIKHGLIGTQyehlehekvREMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIA 591
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDAT---------DEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 592 RAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAY 671
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLY 229
|
....*..
gi 407923078 672 YNLVEAQ 678
Cdd:cd03253 230 AEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
430-668 |
5.46e-90 |
|
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: 289.51 E-value: 5.46e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 430 GRVELRQVKHIYpsRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQ 509
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEPVLFATTIFDNIKHGLIGTQyehlehekvREMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIA 589
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNAT---------DEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERK 668
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
94-668 |
1.28e-89 |
|
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: 300.91 E-value: 1.28e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 94 LYRYAtKLEWIIIVVSSICAIAAGAVLPLMTVVFGSLsgtFQGMFQGTMSNgefnDELVKFVLYFVYLFIGEFFTCYIAT 173
Cdd:COG4988 8 LKRLA-RGARRWLALAVLLGLLSGLLIIAQAWLLASL---LAGLIIGGAPL----SALLPLLGLLLAVLLLRALLAWLRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 174 VGWIYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITadanlvqDGIsEKVG------LVQQSLATFITAFVIG 247
Cdd:COG4988 80 RAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLT-------EGV-EALDgyfaryLPQLFLAALVPLLILV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 248 FVKY--WKLTLILCSTIFAIVFTMgggstfIM------KYNKQSLASYA-LGGTVVEevfsSIRNA---VAFGTQDKLAR 315
Cdd:COG4988 152 AVFPldWLSGLILLVTAPLIPLFM------ILvgkgaaKASRRQWRALArLSGHFLD----RLRGLttlKLFGRAKAEAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 316 QYNEhlvIAEYWGKK-MKT---------VL--ASMLGAMMTIVYLnyglafwmGSRYLvKGEMSLSDVLTILLAV----- 378
Cdd:COG4988 222 RIAE---ASEDFRKRtMKVlrvaflssaVLefFASLSIALVAVYI--------GFRLL-GGSLTLFAALFVLLLApeffl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 379 ---MIGAF---SLGNIGpwlqafttataAASKMYSTIDRVSPLDPTSKEGRRLENlQGRVELRQVKHIYPSRPevTVMNG 452
Cdd:COG4988 290 plrDLGSFyhaRANGIA-----------AAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGR--PALDG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 453 VDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIkhgL 532
Cdd:COG4988 356 LSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL---R 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 533 IGTqyehleHEKVREMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDT 612
Cdd:COG4988 433 LGR------PDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDA 506
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 613 KSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERK 668
Cdd:COG4988 507 ETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
148-678 |
6.59e-89 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 299.63 E-value: 6.59e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 148 NDELVKFVLYFVYLFIGEFFTCYIATVGWIYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGIS 227
Cdd:PRK11176 61 RSVLKWMPLVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 228 EKVGLVQQSLATFITAFVIGFVKYWKLTLILCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAF 307
Cdd:PRK11176 141 GALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 308 GTQDKLARQYNEhlVIAEYWGKKMKTVLASMLGAMMTIVYLNYGLAF--WMGSRYLVKGEMSlSDVLTILLAVMIGAF-- 383
Cdd:PRK11176 221 GGQEVETKRFDK--VSNRMRQQGMKMVSASSISDPIIQLIASLALAFvlYAASFPSVMDTLT-AGTITVVFSSMIALMrp 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 384 --SLGNIGPWLQAFTTATAAaskMYSTIDrvspLDPTSKEGRR-LENLQGRVELRQVKHIYPSRpEVTVMNGVDLVVEAG 460
Cdd:PRK11176 298 lkSLTNVNAQFQRGMAACQT---LFAILD----LEQEKDEGKRvIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAG 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 461 KTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIKHGLiGTQYEhl 540
Cdd:PRK11176 370 KTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYAR-TEQYS-- 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 541 ehekvREMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQA 620
Cdd:PRK11176 447 -----REQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQA 521
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 621 ALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAYYNLVEAQ 678
Cdd:PRK11176 522 ALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
756-1229 |
4.42e-88 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 297.08 E-value: 4.42e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 756 KYSLATLIKLIASFNRQEWLLMVQGLFWSIIAGGGNPTQAVFFAKSISALSRPPSeygklRSEANFWSLMYLMLALTQLI 835
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGD-----LSALLLLLLLLLGLALLRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 836 SFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTETTSLAGLSGATLGTIFTVLTTLIGALV 915
Cdd:COG1132 77 LSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 916 LGIAIGWKLGLVCASTIPVLLACGFLRFWILARFEQRSKKAYEKSASYACEATSAIRTVASLTREEDVYASYHQQLVDQG 995
Cdd:COG1132 155 VLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 996 AKNLRSILKSSTLYALSQSGMFLCTALGFWYGGTLISKGEYSLFQFFVCFSAITFGAQSAGTIFSFAPDMGKAKHAAIQL 1075
Cdd:COG1132 235 RANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1076 KTLFDRKPEIDTwSSDGEKINNMEGHIEFRNVHFRYPtrPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYN 1155
Cdd:COG1132 315 FELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 1156 PLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGTIRDNILLGadRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:COG1132 392 PTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYG--RPDATDEEVEEAAKAAQAHEFIEALP 463
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
432-678 |
7.45e-81 |
|
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: 264.73 E-value: 7.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIY-PSRPEVtvMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQI 510
Cdd:cd03252 1 ITFEHVRFRYkPDGPVI--LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 511 SLVQQEPVLFATTIFDNIKHGLIGTQyehlehekvREMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAI 590
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMS---------MERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 591 ARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQA 670
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
....*...
gi 407923078 671 YYNLVEAQ 678
Cdd:cd03252 230 YAYLYQLQ 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
231-686 |
8.52e-80 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 274.15 E-value: 8.52e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 231 GLVQQSLATFITAFV---IGFVKYWKLTLILcsTIFAIVFTMGGgsTFIMKYNKQ-------------SLASYALGGTVV 294
Cdd:PRK13657 132 EFMREHLATLVALVVllpLALFMNWRLSLVL--VVLGIVYTLIT--TLVMRKTKDgqaaveehyhdlfAHVSDAIGNVSV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 295 EEVFSSIRNAVafgtqdKLARQYNEHLVIAEY-----WGkkmktvLASMLGAMMTIVYLnygLAFWMGSRYLV-KGEMSL 368
Cdd:PRK13657 208 VQSYNRIEAET------QALRDIADNLLAAQMpvlswWA------LASVLNRAASTITM---LAILVLGAALVqKGQLRV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 369 SDVLT-ILLA-VMIGafSLGNIGPWLQAFTTATAAASKMYSTIDRVspldPTSKE---GRRLENLQGRVELRQVKHIYP- 442
Cdd:PRK13657 273 GEVVAfVGFAtLLIG--RLDQVVAFINQVFMAAPKLEEFFEVEDAV----PDVRDppgAIDLGRVKGAVEFDDVSFSYDn 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 443 SRPEVTvmnGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFAT 522
Cdd:PRK13657 347 SRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNR 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 523 TIFDNIKHGligtqYEHLEHEKVREmvynAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILL 602
Cdd:PRK13657 424 SIEDNIRVG-----RPDATDEEMRA----AAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILI 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 603 LDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAYYNLVEAQRIAA 682
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGMLQ 574
|
....
gi 407923078 683 ANEK 686
Cdd:PRK13657 575 EDER 578
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
427-655 |
2.10e-79 |
|
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: 260.48 E-value: 2.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 427 NLQGRVELRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWL 506
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 507 RQQISLVQQEPVLFATTIFDNIKHGLIGTQYEhlehekvreMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQ 586
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLQSCSFE---------CVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 587 RIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRI 655
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
182-676 |
1.77e-76 |
|
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: 264.32 E-value: 1.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 182 RISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQD----GISEKVGLVqqsLATFITAFVIGFVkYWKLTLI 257
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNlylrVLLPLLVAL---LVILAAVAFLAFF-SPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 258 LCSTIFAIVFTMGGGSTFIMKYNKQSLAsyALGGTVVEEVFSSIRNA---VAFGTQDKLARQYNE---HLVIAEywgKKM 331
Cdd:COG4987 161 LALGLLLAGLLLPLLAARLGRRAGRRLA--AARAALRARLTDLLQGAaelAAYGALDRALARLDAaeaRLAAAQ---RRL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 332 KTVLASMLGAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVLTILLAVMiGAF-SLGNIGPWLQAFTtataaasKMYSTID 410
Cdd:COG4987 236 ARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAAL-ALFeALAPLPAAAQHLG-------RVRAAAR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 411 RVSPLDPTSK-----EGRRLENLQGRVELRQVKHIYPSRPEvTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYD 485
Cdd:COG4987 308 RLNELLDAPPavtepAEPAPAPGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 486 PVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIkhgLIGtqYEHLEHEKVREmvynAAKMSNAHDFVSAL 565
Cdd:COG4987 387 PQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENL---RLA--RPDATDEELWA----ALERVGLGDWLAAL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 566 PEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTAD 645
Cdd:COG4987 458 PDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMD 537
|
490 500 510
....*....|....*....|....*....|.
gi 407923078 646 KIVVMSQGRIVEQGTHNELLERKQAYYNLVE 676
Cdd:COG4987 538 RILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
200-678 |
3.66e-76 |
|
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: 266.99 E-value: 3.66e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 200 VGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLatFITAFVIGFVKYW-KLT-LILCSTIFAIVFTMGGGStFIM 277
Cdd:TIGR01846 227 LGYFESRRVGDTVARVRELEQIRNFLTGSALTVVLDLL--FVVVFLAVMFFYSpTLTgVVIGSLVCYALLSVFVGP-ILR 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 278 KYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLviAEYWGKKMKTVLASMLG--AMMTIVYLNYGLAFW 355
Cdd:TIGR01846 304 KRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQL--AAYVAASFRVTNLGNIAgqAIELIQKLTFAILLW 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 356 MGSRYLVKGEMSLSDVLTI-LLAVMIGAFSLGNIGPWlQAFTTATAAASKMYSTIDrvSPLDPTSKEGRRLENLQGRVEL 434
Cdd:TIGR01846 382 FGAHLVIGGALSPGQLVAFnMLAGRVTQPVLRLAQLW-QDFQQTGIALERLGDILN--SPTEPRSAGLAALPELRGAITF 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 435 RQVKHIY-PSRPEVtvMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLV 513
Cdd:TIGR01846 459 ENIRFRYaPDSPEV--LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVV 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 514 QQEPVLFATTIFDNIKHGLIGTQYEHLEHekvremvynAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARA 593
Cdd:TIGR01846 537 LQENVLFSRSIRDNIALCNPGAPFEHVIH---------AAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARA 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 594 IVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAYYN 673
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYAR 687
|
....*
gi 407923078 674 LVEAQ 678
Cdd:TIGR01846 688 LWQQQ 692
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
432-654 |
1.50e-73 |
|
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: 241.52 E-value: 1.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEvTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQIS 511
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFATTIFDNIkhgligtqyehlehekvremvynaakmsnahdfvsalpegyetnvgergflLSGGQKQRIAIA 591
Cdd:cd03228 80 YVPQDPFLFSGTIRENI---------------------------------------------------LSGGQRQRIAIA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407923078 592 RAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGR 654
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
182-676 |
1.82e-70 |
|
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: 251.02 E-value: 1.82e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 182 RISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANlVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLIlcst 261
Cdd:TIGR03796 224 KLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLNDQ-VAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLI---- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 262 ifAIVFTMGGGSTFIMKYNKQSLASYAL-------GGTVVEEVfSSIRNAVAFGTQDKLARQYnehlviAEYWGKKMKT- 333
Cdd:TIGR03796 299 --GIAFAAINVLALQLVSRRRVDANRRLqqdagklTGVAISGL-QSIETLKASGLESDFFSRW------AGYQAKLLNAq 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 334 ----VLASMLGAMMTIVY-LNYGLAFWMGSRYLVKGEMSLSDVL---TILLAVMIGAFSLGNIGPWLQafttataaasKM 405
Cdd:TIGR03796 370 qelgVLTQILGVLPTLLTsLNSALILVVGGLRVMEGQLTIGMLVafqSLMSSFLEPVNNLVGFGGTLQ----------EL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 406 YSTIDRVS-----PLDPTSKEGR-------RLENLQGRVELRQVKHIYpSRPEVTVMNGVDLVVEAGKTTALVGASGSGK 473
Cdd:TIGR03796 440 EGDLNRLDdvlrnPVDPLLEEPEgsaatsePPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGK 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 474 STIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIkhgligTQYEH--LEHEKVRemvyn 551
Cdd:TIGR03796 519 STIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNL------TLWDPtiPDADLVR----- 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 552 AAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRaaQGRTT 631
Cdd:TIGR03796 588 ACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTC 665
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 407923078 632 IVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAYYNLVE 676
Cdd:TIGR03796 666 IIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
711-1229 |
2.20e-70 |
|
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: 250.52 E-value: 2.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 711 VSPQSEKRSYSVDPDDDVAaRLKRTQSGKSESSVAL-----AKKQPASEQKYSLATLIKLIasfnRQEWLLMVQGLFWSI 785
Cdd:COG2274 92 LEGVDGDKVTIADPATGRR-KLSLEEFAESWTGVALlleptPEFDKRGEKPFGLRWFLRLL----RRYRRLLLQVLLASL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 786 IAGG---GNPtqavFFAKSIsalsrppseYGKLRSEANFWSLMYLMLALTQLISFTG-----QGLCFAICSEKLIHRVRD 857
Cdd:COG2274 167 LINLlalATP----LFTQVV---------IDRVLPNQDLSTLWVLAIGLLLALLFEGllrllRSYLLLRLGQRIDLRLSS 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 858 TAFRTMLRQDISFFDQEenSAGALTSFLStETTSLA-GLSGATLGTIFTVLTTLIGALVLGIaIGWKLGLVCASTIPVLL 936
Cdd:COG2274 234 RFFRHLLRLPLSFFESR--SVGDLASRFR-DVESIReFLTGSLLTALLDLLFVLIFLIVLFF-YSPPLALVVLLLIPLYV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 937 acgFLRFWILARFEQRSKKAYEKSA---SYACEATSAIRTVASLTREEDVYASYHQQLVDQGAKNLRSILKSSTLYALSQ 1013
Cdd:COG2274 310 ---LLGLLFQPRLRRLSREESEASAkrqSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSG 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1014 SGMFLCTALGFWYGGTLISKGEYSLFQFFVCFSAITFGAQSAGTIFSFAPDMGKAKHAAIQLKTLFDRKPEIDTwSSDGE 1093
Cdd:COG2274 387 LLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREE-GRSKL 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1094 KINNMEGHIEFRNVHFRYPTRpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNI 1173
Cdd:COG2274 466 SLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDP 544
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 1174 NDYRSYIALVSQEPTLYQGTIRDNILLGadRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:COG2274 545 ASLRRQIGVVLQDVFLFSGTIRENITLG--DPDATDEEIIEAARLAGLHDFIEALP 598
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
75-672 |
9.20e-70 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 257.65 E-value: 9.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 75 REILKRQLDTPP-VSISYFALYRYATKlewIIIVVSSIcaIAAGAVLPLMTVVFGSLSGTfqgMFQgtMSNGEFNDElvK 153
Cdd:PTZ00265 800 RNLFKRKPKAPNnLRIVYREIFSYKKD---VTIIALSI--LVAGGLYPVFALLYAKYVST---LFD--FANLEANSN--K 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 154 FVLYF----VYLFIGEFFTCYIATVgwiyVGERISSRIREYYLSAILRQNVGYFD--KLGAGEITTRITADANLVQDGIS 227
Cdd:PTZ00265 868 YSLYIlviaIAMFISETLKNYYNNV----IGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLV 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 228 EKVGLVQQSLATFITAFVIGFVKYWKLTLILCST------IFAIVFTMGGGSTFIMKYNKQSLASYALGGT--------- 292
Cdd:PTZ00265 944 NNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTyfifmrVFAIRARLTANKDVEKKEINQPGTVFAYNSDdeifkdpsf 1023
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 293 VVEEVFSSIRNAVAFGTQDKLARQYnEHLVIAEYWGKKMKTVLASML-GAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDV 371
Cdd:PTZ00265 1024 LIQEAFYNMNTVIIYGLEDYFCNLI-EKAIDYSNKGQKRKTLVNSMLwGFSQSAQLFINSFAYWFGSFLIRRGTILVDDF 1102
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 372 LTILLAVMIGAFSLGNIGPWLQAFTTATAAASKMYSTIDRVSPLDPTSKEGRRLEN---LQGRVELRQVKHIYPSRPEVT 448
Cdd:PTZ00265 1103 MKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVP 1182
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYD-----------------------------PVG----------- 488
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqNVGmknvnefsltk 1262
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 489 --------------GEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIKHGligtqyehlEHEKVREMVYNAAK 554
Cdd:PTZ00265 1263 eggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG---------KEDATREDVKRACK 1333
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 555 MSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL----DRAaqGRT 630
Cdd:PTZ00265 1334 FAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKT 1411
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 407923078 631 TIVIAHRLSTIKTADKIVVMSQ----GRIVE-QGTHNELLERKQAYY 672
Cdd:PTZ00265 1412 IITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQDGVY 1458
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
747-1229 |
4.13e-65 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 235.39 E-value: 4.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 747 AKKQPASEQKYSLATLIKLIaSFNRQEWLLMVQGLFWSIIA--GG-------GNPTQAVFFAKSISALSRPpseygklrs 817
Cdd:TIGR00958 134 SEKEAEQGQSETADLLFRLL-GLSGRDWPWLISAFVFLTLSslGEmfipfytGRVIDTLGGDKGPPALASA--------- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 818 eanfwslMYLMLALTQLISFTG--QGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDqeENSAGALTSFLSTETTSLAGL 895
Cdd:TIGR00958 204 -------IFFMCLLSIASSVSAglRGGSFNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 896 SGATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIP-VLLACGFLRFWILArFEQRSKKAYEKSASYACEATSAIRTV 974
Cdd:TIGR00958 275 LSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPlVFLAEKVFGKRYQL-LSEELQEAVAKANQVAEEALSGMRTV 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 975 ASLTREEDVYASYHQQLVD--QGAKNlRSILKSSTLYALSQSGMFLCTALgFWYGGTLISKGEYS--------LFQFFVc 1044
Cdd:TIGR00958 354 RSFAAEEGEASRFKEALEEtlQLNKR-KALAYAGYLWTTSVLGMLIQVLV-LYYGGQLVLTGKVSsgnlvsflLYQEQL- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1045 fsaitfgAQSAGTIFSFAPDMGKAKHAAIQLKTLFDRKPEIdtwSSDGE-KINNMEGHIEFRNVHFRYPTRPEQPVLRGL 1123
Cdd:TIGR00958 431 -------GEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNI---PLTGTlAPLNLEGLIEFQDVSFSYPNRPDVPVLKGL 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1124 NLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGTIRDNILLGAD 1203
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLT 580
|
490 500
....*....|....*....|....*.
gi 407923078 1204 RenVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:TIGR00958 581 D--TPDEEIMAAAKAANAHDFIMEFP 604
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
232-677 |
1.78e-64 |
|
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: 230.16 E-value: 1.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 232 LVQQSLATFITAFVI---GFVKYWKLTLILcsTIFAIVFTMGGgsTFIMKYNKQSLASY-ALGGTVVEEVFSSIRNAVAF 307
Cdd:TIGR01192 133 FMRQHLATFVALFLLiptAFAMDWRLSIVL--MVLGILYILIA--KLVMQRTKNGQAAVeHHYHNVFKHVSDSISNVSVV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 308 GTQDKLA------RQYNEHLVIAEY-----WGkkmktvLASMLGAMMTIVYLNYGLAfwMGSRYLVKGEMSLSDVLTIL- 375
Cdd:TIGR01192 209 HSYNRIEaetsalKQFTNNLLSAQYpvldwWA------LASGLNRMASTISMMCILV--IGTVLVIKGELSVGEVIAFIg 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 376 -LAVMIGafSLGNIGPWLQAFTTATAAASKMY----STIDRVSPLDptskeGRRLENLQGRVELRQVKHIYPSRPEvTVM 450
Cdd:TIGR01192 281 fANLLIG--RLDQMSGFITQIFEARAKLEDFFdledSVFQREEPAD-----APELPNVKGAVEFRHITFEFANSSQ-GVF 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 451 NgVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIKH 530
Cdd:TIGR01192 353 D-VSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 531 GLIGTQYEHlehekvremVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSAL 610
Cdd:TIGR01192 432 GREGATDEE---------VYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSAL 502
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 611 DTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAYYNLVEA 677
Cdd:TIGR01192 503 DVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1102-1229 |
1.18e-63 |
|
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: 216.25 E-value: 1.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIA 1181
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 407923078 1182 LVSQEPTLYQGTIRDNILLGadRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYG--KPDATDEEVEEAAKKANIHDFIMSLP 126
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
430-659 |
1.52e-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: 212.45 E-value: 1.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 430 GRVELRQVKHIYPSRPEVTVMNgVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQ 509
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDN-VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEPVLFATTIFDNIKHGligtqyeHLEHEKvrEMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIA 589
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLG-------APLADD--ERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQG 659
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
113-650 |
3.26e-60 |
|
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: 216.38 E-value: 3.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 113 AIAAGAVLPLMTVVF-----GSLSGTFQGMFqgtmSNGEFNDELVKFVLYFVYLFIGEFFTCYIATVGWIYVGERISSRI 187
Cdd:TIGR02857 4 ALALLALLGVLGALLiiaqaWLLARVVDGLI----SAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 188 REYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKvgLVQQSLATFITAFVIGFVKY--WKLTLILCSTIFAI 265
Cdd:TIGR02857 80 RERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARY--LPQLVLAVIVPLAILAAVFPqdWISGLILLLTAPLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 266 -VFTMGGGSTFIMKYNKQSLASYALGGTVVEEVfSSIRNAVAFGTQDKLARQYNEhlVIAEYWGKKMKTV---------- 334
Cdd:TIGR02857 158 pIFMILIGWAAQAAARKQWAALSRLSGHFLDRL-RGLPTLKLFGRAKAQAAAIRR--SSEEYRERTMRVLriaflssavl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 335 -LASMLGAMMTIVYLNYGLAFwmgsrylvkGEMSLSDVLTILLAVMIGAFSLGNIGPWLQAFTTATAAASKMYSTIDRVS 413
Cdd:TIGR02857 235 eLFATLSVALVAVYIGFRLLA---------GDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 414 PLDPTSKEGRRLENLQgrVELRQVKHIYPSRPEVtvMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLL 493
Cdd:TIGR02857 306 RPLAGKAPVTAAPASS--LEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 494 DGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIKHGligtqyehlEHEKVREMVYNAAKMSNAHDFVSALPEGYETNV 573
Cdd:TIGR02857 382 NGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA---------RPDASDAEIREALERAGLDEFVAALPQGLDTPI 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 574 GERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVM 650
Cdd:TIGR02857 453 GEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
777-1075 |
1.66e-59 |
|
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: 206.56 E-value: 1.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 777 MVQGLFWSIIAGGGNPTQAVFFAKSISALSRPPSEYG---KLRSEANFWSLMYLMLALTQLISFTGQGLCFAICSEKLIH 853
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESspdEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 854 RVRDTAFRTMLRQDISFFDqeENSAGALTSFLSTETTSL-AGLSGAtLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTI 932
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIqDGIGEK-LGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 933 PVLLACGFLRFWILARFEQRSKKAYEKSASYACEATSAIRTVASLTREEDVYASYHQQLvdqgAKNLRSILKSSTLYALS 1012
Cdd:cd18577 158 PLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKAL----EKARKAGIKKGLVSGLG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 1013 QSGMFLCT----ALGFWYGGTLISKGEYSLFQFFVCFSAITFGAQSAGTIFSFAPDMGKAKHAAIQL 1075
Cdd:cd18577 234 LGLLFFIIfamyALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
430-660 |
1.25e-58 |
|
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: 201.18 E-value: 1.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 430 GRVELRQVKHIYpsRPE-VTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQ 508
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 QISLVQQEPVLFATTIFDNIKhgligtqyehLEHEKVREMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRI 588
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD----------PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 589 AIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGT 660
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
196-678 |
2.43e-58 |
|
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: 214.44 E-value: 2.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 196 LRQNVGYFDKLGAGEITTRItadanlvqDGISE--KV--GLVQQSLATFITAF---VIGFVKYWKLTLILCSTIFAIVFT 268
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASRA--------MGISQirRIlsGSTLTTLLSGIFALlnlGLMFYYSWKLALVAVALALVAIAV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 269 MGGGSTFIMKYNKQSLA-SYALGGTVVEEV--FSSIRNAvafGTQDKL----ARQYNEHLVIaEYWGKKMKTVLASmLGA 341
Cdd:TIGR03797 292 TLVLGLLQVRKERRLLElSGKISGLTVQLIngISKLRVA---GAENRAfarwAKLFSRQRKL-ELSAQRIENLLTV-FNA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 342 MMTIVYLnyGLAFWMGSRYLVKGEMSLSDVL---TILLAVMIGAFSLGNIgpwlqafttataaASKMYSTI---DRVSPL 415
Cdd:TIGR03797 367 VLPVLTS--AALFAAAISLLGGAGLSLGSFLafnTAFGSFSGAVTQLSNT-------------LISILAVIplwERAKPI 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 416 DPTSKE--------GRrlenLQGRVELRQVKHIY-PSRPevTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDP 486
Cdd:TIGR03797 432 LEALPEvdeaktdpGK----LSGAIEVDRVTFRYrPDGP--LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETP 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 487 VGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIkhgLIGTQYEHlehekvrEMVYNAAKMSNAHDFVSALP 566
Cdd:TIGR03797 506 ESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI---AGGAPLTL-------DEAWEAARMAGLAEDIRAMP 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 567 EGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRaaQGRTTIVIAHRLSTIKTADK 646
Cdd:TIGR03797 576 MGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLER--LKVTRIVIAHRLSTIRNADR 653
|
490 500 510
....*....|....*....|....*....|..
gi 407923078 647 IVVMSQGRIVEQGTHNELLERKQAYYNLVEAQ 678
Cdd:TIGR03797 654 IYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
186-680 |
7.03e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 211.12 E-value: 7.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 186 RIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLIlCSTIFAI 265
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALV-AIMIFPA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 266 VFTMGG----GSTFIMKYNKQSLASY------ALGGTVVEEVFssiRNAVAFGtqDKLARQYNEHlviaeyWGKKMKTV- 334
Cdd:PRK10790 178 VLVVMViyqrYSTPIVRRVRAYLADIndgfneVINGMSVIQQF---RQQARFG--ERMGEASRSH------YMARMQTLr 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 335 --------LASMLGAMMTIvylnyGLAFWMGsrylvkgemsLSDVLTILLAVMIgAF--SLGNIGPWLQAFTTATAAASK 404
Cdd:PRK10790 247 ldgfllrpLLSLFSALILC-----GLLMLFG----------FSASGTIEVGVLY-AFisYLGRLNEPLIELTTQQSMLQQ 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 405 MYSTIDRV-----SPLDPTSKEGRRLEnlQGRVELRQVKHIYpsRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGL 479
Cdd:PRK10790 311 AVVAGERVfelmdGPRQQYGNDDRPLQ--SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 480 VERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIKHGligtqyEHLEHEKVremvYNAAKMSNAH 559
Cdd:PRK10790 387 LMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG------RDISEEQV----WQALETVQLA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 560 DFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALdRAAQGRTT-IVIAHRL 638
Cdd:PRK10790 457 ELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTlVVIAHRL 535
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 407923078 639 STIKTADKIVVMSQGRIVEQGTHNELLERKQAYYNLVEAQRI 680
Cdd:PRK10790 536 STIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLA 577
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
182-683 |
7.15e-57 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 207.64 E-value: 7.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 182 RISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKY-WKLTLI--L 258
Cdd:PRK10789 66 QLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTQIsWQLTLLalL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 259 CSTIFAIVFTMGGgsTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEhlvIAEYWGKKMKTVlASM 338
Cdd:PRK10789 146 PMPVMAIMIKRYG--DQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAA---DAEDTGKKNMRV-ARI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 339 LGAMMTIVYLNYG----LAFWMGSRYLVKGEMSLSDVLTIL--LAVMIgafslgnigpW----LQAFTTATAAASKMYST 408
Cdd:PRK10789 220 DARFDPTIYIAIGmanlLAIGGGSWMVVNGSLTLGQLTSFVmyLGLMI----------WpmlaLAWMFNIVERGSAAYSR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 409 IDRVSPLDPTSKEGRR-LENLQGRVELRQVKHIYPSRpEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPV 487
Cdd:PRK10789 290 IRAMLAEAPVVKDGSEpVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 488 GGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIKHGLIGTQYEHLEHekvremvynAAKMSNAHDFVSALPE 567
Cdd:PRK10789 369 EGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEH---------VARLASVHDDILRLPQ 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 568 GYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKI 647
Cdd:PRK10789 440 GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEI 519
|
490 500 510
....*....|....*....|....*....|....*.
gi 407923078 648 VVMSQGRIVEQGTHNELLERKQAYYNLVEAQRIAAA 683
Cdd:PRK10789 520 LVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAA 555
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
151-677 |
9.40e-57 |
|
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: 210.37 E-value: 9.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 151 LVKFVLYFVYLF--IGEFFTCYIATVgwiyVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITaDANLVQDGISe 228
Cdd:TIGR01193 197 IISIGLIIAYIIqqILSYIQIFLLNV----LGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALA- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 229 kvglvqqslATFITAF-------VIGFV-KYWKLTLILCS-------TIFAIVFTmgggSTFiMKYNKQSLASYALGGTV 293
Cdd:TIGR01193 271 ---------STILSLFldmwilvIVGLFlVRQNMLLFLLSllsipvyAVIIILFK----RTF-NKLNHDAMQANAVLNSS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 294 VEEVFSSIRNAVAFGTQD----KLARQYNEHL------VIAEYWGKKMKTVLASMLgammTIVYLnyglafWMGSRYLVK 363
Cdd:TIGR01193 337 IIEDLNGIETIKSLTSEAerysKIDSEFGDYLnksfkyQKADQGQQAIKAVTKLIL----NVVIL------WTGAYLVMR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 364 GEMSLSDVLTilLAVMIGAF-----SLGNIGPWLQAFTTATAAASKMYstidRVSPLDPTSKEGRRLENLQGRVELRQVK 438
Cdd:TIGR01193 407 GKLTLGQLIT--FNALLSYFltpleNIINLQPKLQAARVANNRLNEVY----LVDSEFINKKKRTELNNLNGDIVINDVS 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 439 HIYPSRPEVtvMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPV 518
Cdd:TIGR01193 481 YSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPY 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 519 LFATTIFDNIkhgLIGTQyEHLEHEKVREmvynAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDP 598
Cdd:TIGR01193 559 IFSGSILENL---LLGAK-ENVSQDEIWA----ACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDS 630
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 599 KILLLDEATSALDTKSEGVVQAALdRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAYYNLVEA 677
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
417-670 |
1.05e-55 |
|
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: 203.83 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 417 PTSKEGRRLENLQGRVELRQVKHIYPSRPEVTVmNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVL 492
Cdd:COG4618 316 PAEPERMPLPRPKGRLSVENLTVVPPGSKRPIL-RGVSFSLEPGEVLGVIGPSGSGKSTlarlLVGVWP----PTAGSVR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 493 LDGVNVQelnlHWLRQQ----ISLVQQEPVLFATTIFDNIkhgligtqyehlehekVR------EMVYNAAKMSNAHDFV 562
Cdd:COG4618 391 LDGADLS----QWDREElgrhIGYLPQDVELFDGTIAENI----------------ARfgdadpEKVVAAAKLAGVHEMI 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 563 SALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRA-AQGRTTIVIAHRLSTI 641
Cdd:COG4618 451 LRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLL 530
|
250 260
....*....|....*....|....*....
gi 407923078 642 KTADKIVVMSQGRIVEQGTHNELLERKQA 670
Cdd:COG4618 531 AAVDKLLVLRDGRVQAFGPRDEVLARLAR 559
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
99-388 |
6.75e-55 |
|
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: 194.21 E-value: 6.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 99 TKLEWIIIVVSSICAIAAGAVLPLMTVVFGSLSGTFQgmfqgTMSNGEFNDELVKFVLYFVYLFIGEFFTCYIATVGWIY 178
Cdd:cd18578 4 NKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFS-----LPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 179 VGERISSRIREYYLSAILRQNVGYFDKLG--AGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTL 256
Cdd:cd18578 79 AGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 257 ILCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLVIAEYWGKKMKTVLA 336
Cdd:cd18578 159 VGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 407923078 337 SMLGAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVLTILLAVMIGAFSLGNI 388
Cdd:cd18578 239 LGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQA 290
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
106-390 |
5.63e-53 |
|
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: 188.64 E-value: 5.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 106 IVVSSICAIAAGAVLPLMTVVFGSLSGTFQ--GMFQGTMSNGEFND----------ELVKFVLYFVYLFIGEFFTCYIAT 173
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTngGMTNITGNSSGLNSsagpfekleeEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 174 VGWIYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWK 253
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 254 LTLILCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLVIAEYWGKKMKT 333
Cdd:cd18558 161 LTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 334 VLASMLGAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVLTILLAVMIGAFSLGNIGP 390
Cdd:cd18558 241 TFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVP 297
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
432-670 |
3.75e-52 |
|
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: 182.92 E-value: 3.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPsrPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQELNLHWLR 507
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTllrlLNGLLK----PTSGEVLVDGKDITKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 508 QQISLVQQEPV--LFATTIFDNIKHGL--IGtqyehLEHEKVREMVYNAAKMSNAHDFVSALPegyetnvgergFLLSGG 583
Cdd:COG1122 75 RKVGLVFQNPDdqLFAPTVEEDVAFGPenLG-----LPREEIRERVEEALELVGLEHLADRPP-----------HELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 584 QKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTH 661
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTP 218
|
....*....
gi 407923078 662 NELLERKQA 670
Cdd:COG1122 219 REVFSDYEL 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
453-682 |
9.36e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 190.06 E-value: 9.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 453 VDLVVEAGKTTALVGASGSGKSTIVGLVERFYdPVGGEVLLDGVNVQELNL-HWlRQQISLVQQEPVLFATTIFDNIkhg 531
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPeSW-RKHLSWVGQNPQLPHGTLRDNV--- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 532 LIGtqyehlEHEKVREMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALD 611
Cdd:PRK11174 444 LLG------NPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 612 TKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAYYNLVeAQRIAA 682
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLL-AHRQEE 587
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
432-672 |
2.57e-50 |
|
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: 186.65 E-value: 2.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRP--EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN---LHWL 506
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 507 RQQISLVQQEPV--LFAT-TIFDNIKHGLIgtQYEHLEHEKVREMVYNAAKMsnahdfVsALPEGYEtnvGERGFLLSGG 583
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAEPLR--LHGLLSRAERRERVAELLER------V-GLPPDLA---DRYPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 584 QKQRIAIARAIVSDPKILLLDEATSALDTksegVVQAA-LD-----RAAQGRTTIVIAHRLSTIKT-ADKIVVMSQGRIV 656
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDV----SVQAQiLNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
250
....*....|....*.
gi 407923078 657 EQGTHNELLERKQAYY 672
Cdd:COG1123 485 EDGPTEEVFANPQHPY 500
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
182-638 |
4.60e-48 |
|
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: 180.63 E-value: 4.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 182 RISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDgisekvgLVQQSLATFITAFVIG-------FVKYWKL 254
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQD-------LYVRVIVPAGVALVVGaaavaaiAVLSVPA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 255 TLILCSTIFAIVFTMGGGSTFIMKYNKQSLAsyALGGTVVEEVFSSIRNA---VAFGTQDKLARQY---NEHLVIAEywg 328
Cdd:TIGR02868 156 ALILAAGLLLAGFVAPLVSLRAARAAEQALA--RLRGELAAQLTDALDGAaelVASGALPAALAQVeeaDRELTRAE--- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 329 KKMKTVLASMLGAMMTIVYLNYGLAFWMGSRYLVKGEMSlSDVLTILLAVMIGAF-SLGNIGPWLQAFTTATAAASKMYS 407
Cdd:TIGR02868 231 RRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVLVLLPLAAFeAFAALPAAAQQLTRVRAAAERIVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 408 TIDRVSPLDPTSKEGRRLENLQG-RVELRQVKHIYPSRPEVtvMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDP 486
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 487 VGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIkhgLIGTQyehlehEKVREMVYNAAKMSNAHDFVSALP 566
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENL---RLARP------DATDEELWAALERVGLADWLRALP 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 567 EGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRL 638
Cdd:TIGR02868 459 DGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
362-665 |
2.27e-47 |
|
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: 178.70 E-value: 2.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 362 VKGEMSLSDVL--TILLAVMIGAFSlGNIGPWLQAFTTAtaaasKMYSTIDRVSPLDPTSKEGRRLENLQGRVELRQVkH 439
Cdd:TIGR01842 251 IDGEITPGMMIagSILVGRALAPID-GAIGGWKQFSGAR-----QAYKRLNELLANYPSRDPAMPLPEPEGHLSVENV-T 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 440 IYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVL 519
Cdd:TIGR01842 324 IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVEL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 520 FATTIFDNI-KHGligtqyEHLEHEKVREmvynAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDP 598
Cdd:TIGR01842 404 FPGTVAENIaRFG------ENADPEKIIE----AAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDP 473
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 599 KILLLDEATSALDTKSEGVVQAALDRA-AQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
429-680 |
4.88e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 178.48 E-value: 4.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 429 QGRVELRQVKHIYPSRPEvTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQ 508
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 QISLVQQEPVLFATTIFDNIKHGLIGTQYEHLEH--EKVRemvynaakmsnahdfVSAL---PEGYETNVGERGFLLSGG 583
Cdd:PRK11160 415 AISVVSQRVHLFSATLRDNLLLAAPNASDEALIEvlQQVG---------------LEKLledDKGLNAWLGEGGRQLSGG 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 584 QKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNE 663
Cdd:PRK11160 480 EQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQE 559
|
250
....*....|....*..
gi 407923078 664 LLERKQAYYNLVeaQRI 680
Cdd:PRK11160 560 LLAQQGRYYQLK--QRL 574
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
433-655 |
9.23e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.53 E-value: 9.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 433 ELRQVKHIYPSRPevtVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISL 512
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 513 VQQEPVLFATTIFDNIKHGLigtqyehleheKVREMVYNaakMSNAHDFVSA--LPEGY-ETNVGErgflLSGGQKQRIA 589
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPF-----------QLRERKFD---RERALELLERlgLPPDIlDKPVER----LSGGERQRLA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAH------RLstiktADKIVVMSQGRI 655
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
780-1052 |
9.76e-47 |
|
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: 168.98 E-value: 9.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 780 GLFWSIIAGGGNPTQAVFFAKSISALSrppsEYGKLRSEA-NFWSLMYLMLALTQLISFTGQGLCFAICSEKLIHRVRDT 858
Cdd:pfam00664 4 AILLAILSGAISPAFPLVLGRILDVLL----PDGDPETQAlNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 859 AFRTMLRQDISFFDQeeNSAGALTSFLSTETTSLAGLSGATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLLAC 938
Cdd:pfam00664 80 LFKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 939 GFLRFWILARFEQRSKKAYEKSASYACEATSAIRTVASLTREEDVYASYHQQLVDQGAKNLRSILKSSTLYALSQSGMFL 1018
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 407923078 1019 CTALGFWYGGTLISKGEYSL--FQFFVCFSAITFGA 1052
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVgdLVAFLSLFAQLFGP 273
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
106-383 |
1.50e-46 |
|
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: 168.59 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 106 IVVSSICAIAAGAVLPLMTVVFGSLSGTFqgmfqgTMSNGEFNDELVKFVLYFVYLFIGEFFTCYIATVGWIYVGERISS 185
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL------LPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 186 RIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLILCSTIFAI 265
Cdd:pfam00664 75 RLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 266 VFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLVIAEYWGKKMKTVLASMLGAMMTI 345
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 407923078 346 VYLNYGLAFWMGSRYLVKGEMSLSDVLTI--LLAVMIGAF 383
Cdd:pfam00664 235 GYLSYALALWFGAYLVISGELSVGDLVAFlsLFAQLFGPL 274
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
777-1072 |
2.11e-46 |
|
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: 169.38 E-value: 2.11e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 777 MVQGLFWSIIAGGGNPTQAVFFAK---------------SISALSRPPSEYGKLRSEANFWSLMYLMLALTQLISFTGQG 841
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDmtdsftnggmtnitgNSSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 842 LCFAICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTETTSLAGLSGATLGTIFTVLTTLIGALVLGIAIG 921
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDV--NDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 922 WKLGLVCASTIPVLLACGFLRFWILARFEQRSKKAYEKSASYACEATSAIRTVASLTREEDVYASYHQQLVDQGAKNLRS 1001
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 1002 ILKSSTLYALSQSGMFLCTALGFWYGGTLISKGEYSLFQ-FFVCFSAITFGAQSAGTIFSFAPdMGKAKHAA 1072
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEvLTVFFSVLIGAFSAGQQVPSIEA-FANARGAA 309
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
436-664 |
2.24e-45 |
|
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: 163.83 E-value: 2.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQELN---LHWLRQ 508
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTllrlIVGLLR----PDSGEVLIDGEDISGLSeaeLYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 QISLVQQEPVLF-ATTIFDNIKHGLigtqYEH--LEHEKVREMVYNAAKMSNAHDFVSALPegyetnvGErgflLSGGQK 585
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFPL----REHtrLSEEEIREIVLEKLEAVGLRGAEDLYP-------AE----LSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 586 QRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHN 662
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPE 222
|
..
gi 407923078 663 EL 664
Cdd:cd03261 223 EL 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
433-654 |
4.71e-45 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 161.87 E-value: 4.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 433 ELRQVKHIYPSRPEVtVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISL 512
Cdd:cd03225 1 ELKNLSFSYPDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 513 VQQEP--VLFATTIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPegyetnvgergFLLSGGQKQRIAI 590
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGL---ENLGLPEEEIEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 591 ARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTIKT-ADKIVVMSQGR 654
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
432-658 |
4.77e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 162.52 E-value: 4.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPS-RPEVTVMNGVDLVVEAGKTTALVGASGSGKST---IVGLVERfydPVGGEVLLDGVNVQELN---LH 504
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 505 WLR-QQISLVQQEPVLFAT-TIFDNIkhgLIGTQYEHLEHEKVREMVYNAAKMSNAHDFVSALPegyetnvGErgflLSG 582
Cdd:COG1136 82 RLRrRHIGFVFQFFNLLPElTALENV---ALPLLLAGVSRKERRERARELLERVGLGDRLDHRP-------SQ----LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 583 GQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTIKTADKIVVMSQGRIVEQ 658
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
849-1229 |
6.93e-45 |
|
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: 171.87 E-value: 6.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 849 EKLI-HrvrDTAFRTM--LRqdISFFDQ-EENSAGALTSFLSTET-TSLAG----LSGATLGTIFTVLTTLIGALVLGIA 919
Cdd:COG4987 75 ERLVsH---DATLRLLadLR--VRLYRRlEPLAPAGLARLRSGDLlNRLVAdvdaLDNLYLRVLLPLLVALLVILAAVAF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 920 IGW---KLGLVCAstiPVLLACGFLRFWILARFEQRSKKAYEKS-ASYACEATSAIRTVASLTreedVY---ASYHQQLV 992
Cdd:COG4987 150 LAFfspALALVLA---LGLLLAGLLLPLLAARLGRRAGRRLAAArAALRARLTDLLQGAAELA----AYgalDRALARLD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 993 DQGAKNLRSILKSSTLYALSQSGMFLCTALG----FWYGGTLISKGEYSlfqfFVCFSAITFGAQSAGTIFSFAPD---- 1064
Cdd:COG4987 223 AAEARLAAAQRRLARLSALAQALLQLAAGLAvvavLWLAAPLVAAGALS----GPLLALLVLAALALFEALAPLPAaaqh 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1065 MGKAKHAAIQLKTLFDRKPEIDtwSSDGEKINNMEGHIEFRNVHFRYPTRPeQPVLRGLNLSVKPGQYVALVGASGCGKS 1144
Cdd:COG4987 299 LGRVRAAARRLNELLDAPPAVT--EPAEPAPAPGGPSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1145 TTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGTIRDNILLGadRENVPEEAIIKACKDANIYDF 1224
Cdd:COG4987 376 TLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLA--RPDATDEELWAALERVGLGDW 453
|
....*
gi 407923078 1225 IMSLP 1229
Cdd:COG4987 454 LAALP 458
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
824-1229 |
8.13e-45 |
|
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: 171.82 E-value: 8.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 824 LMYLMLALTQLISFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDqEENSAGALTSFLSTETTSLAGLSGAtlgti 903
Cdd:TIGR02203 58 LVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFD-RQPTGTLLSRITFDSEQVASAATDA----- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 904 FTVLT----TLIGALVLGIAIGWKLGLVCASTIPVLLacgflrfWILARFEQRSKKAYEKSASYACEATSAIRTVASLTR 979
Cdd:TIGR02203 132 FIVLVretlTVIGLFIVLLYYSWQLTLIVVVMLPVLS-------ILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 980 EEDVYA--SYHQQLVDQGA-KNLRSILKSSTLYALSQSGMFLCTALGFwyggtliskgeySLFQFFVCFSAITfGAQSAG 1056
Cdd:TIGR02203 205 VVKLFGgqAYETRRFDAVSnRNRRLAMKMTSAGSISSPITQLIASLAL------------AVVLFIALFQAQA-GSLTAG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1057 TIFSFAPDMGKA----KH-------------AAIQLKTLFDRKPEIDTwssDGEKINNMEGHIEFRNVHFRYPTRpEQPV 1119
Cdd:TIGR02203 272 DFTAFITAMIALirplKSltnvnapmqrglaAAESLFTLLDSPPEKDT---GTRAIERARGDVEFRNVTFRYPGR-DRPA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1120 LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGTIRDNIL 1199
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIA 427
|
410 420 430
....*....|....*....|....*....|
gi 407923078 1200 LGAdRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:TIGR02203 428 YGR-TEQADRAEIERALAAAYAQDFVDKLP 456
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
432-664 |
1.19e-44 |
|
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: 161.19 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRpevTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYD-----PVGGEVLLDGVNVQELNLH-- 504
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 505 WLRQQISLVQQEPVLFATTIFDNIKHGLigTQYEHLEHEKVREMVYNAAKMSnahdfvsALPEgyetNVGER--GFLLSG 582
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGL--RLHGIKLKEELDERVEEALRKA-------ALWD----EVKDRlhALGLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 583 GQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIK-TADKIVVMSQGRIVEQGTH 661
Cdd:cd03260 145 GQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPT 224
|
...
gi 407923078 662 NEL 664
Cdd:cd03260 225 EQI 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
432-669 |
1.62e-44 |
|
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: 161.21 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRP-EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN---LHWLR 507
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 508 QQISLVQQEPVLFAT-TIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQ 586
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPL---EIAGVPKAEIEERVLELLELVGLEDKADAYPAQ-----------LSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 587 RIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALDRAAQGRTTIV-IAHRLSTIKT-ADKIVVMSQGRIVEQGTHNE 663
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETtQSILALLRDINRELGLTIVlITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
....*.
gi 407923078 664 LLERKQ 669
Cdd:cd03258 228 VFANPQ 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
432-659 |
3.08e-44 |
|
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: 159.61 E-value: 3.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSrpeVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHwlRQQIS 511
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFAT-TIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQRIAI 590
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGL---KLRGVPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 591 ARAIVSDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQG 659
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
436-666 |
5.70e-44 |
|
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: 159.76 E-value: 5.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQELN---LHWLRQ 508
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVllklIIGLLR----PDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 QISLVQQEPVLF-ATTIFDNIKHGLIgtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPegyetnvGErgflLSGGQKQR 587
Cdd:COG1127 83 RIGMLFQGGALFdSLTVFENVAFPLR--EHTDLSEAEIRELVLEKLELVGLPGAADKMP-------SE----LSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 588 IAIARAIVSDPKILLLDEATSALDTKSEGVVQAALD--RAAQGRTTIVIAHRLSTIKT-ADKIVVMSQGRIVEQGTHNEL 664
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRelRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 407923078 665 LE 666
Cdd:COG1127 230 LA 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
432-659 |
8.60e-44 |
|
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: 158.82 E-value: 8.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRP-EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWL---R 507
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 508 QQISLVQQEPvlFAT-----TIFDNIKHGLIGTQYEHLEHEKVREMVYNAAKMSNAHDFVSALPegYEtnvgergflLSG 582
Cdd:cd03257 82 KEIQMVFQDP--MSSlnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYP--HE---------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 583 GQKQRIAIARAIVSDPKILLLDEATSALDTksegVVQAA-LD-----RAAQGRTTIVIAHRLSTIK-TADKIVVMSQGRI 655
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDV----SVQAQiLDllkklQEELGLTLLFITHDLGVVAkIADRVAVMYAGKI 224
|
....
gi 407923078 656 VEQG 659
Cdd:cd03257 225 VEEG 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
433-655 |
3.81e-43 |
|
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: 155.07 E-value: 3.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 433 ELRQVKHIYPSRPEvTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISL 512
Cdd:cd03246 2 EVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 513 VQQEPVLFATTIFDNIkhgligtqyehlehekvremvynaakmsnahdfvsalpegyetnvgergflLSGGQKQRIAIAR 592
Cdd:cd03246 81 LPQDDELFSGSIAENI---------------------------------------------------LSGGQRQRLGLAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 593 AIVSDPKILLLDEATSALDTKSEGVVQAALDRA-AQGRTTIVIAHRLSTIKTADKIVVMSQGRI 655
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1100-1229 |
7.86e-43 |
|
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: 156.23 E-value: 7.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1100 GHIEFRNVHFRYptRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSY 1179
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 407923078 1180 IALVSQEPTLYQGTIRDNILLGadRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG--RPNATDEEVIEAAKEAGAHDFIMKLP 126
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
432-680 |
8.86e-43 |
|
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: 156.89 E-value: 8.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPE-VTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVerfyDPVGGEVLLDGVNVQELNLHWL 506
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTllraLAGLE----RPWSGEVTFDGRPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 507 RQQISLVQQEPvlfaTTIFdNIKHGLIGTQYEHLEHEKVREMVYNAAKMSNAhdfvsalpegyetnVG-ERGFL------ 579
Cdd:COG1124 78 RRRVQMVFQDP----YASL-HPRHTVDRILAEPLRIHGLPDREERIAELLEQ--------------VGlPPSFLdryphq 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTksegVVQAA-LD-----RAAQGRTTIVIAHRLSTIKT-ADKIVVMSQ 652
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDV----SVQAEiLNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQN 214
|
250 260 270
....*....|....*....|....*....|
gi 407923078 653 GRIVEQGTHNELLERKQAYY--NLVEAQRI 680
Cdd:COG1124 215 GRIVEELTVADLLAGPKHPYtrELLAASLA 244
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
771-1229 |
4.38e-42 |
|
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: 163.39 E-value: 4.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 771 RQEWLLMVQGLFWSIIAGGGNPTQAVFFAKSISALsrppseygkLRSEANFWSLMYLMLALtqLISFTGQGLCF------ 844
Cdd:COG4988 13 RGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGL---------IIGGAPLSALLPLLGLL--LAVLLLRALLAwlrera 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 845 -AICSEKLIHRVRDTAFRTMLRQDISFFDQEenSAGALTSFLSTETTSLAGLSGATLGTIF-TVLTTLIgaLVLGIA-IG 921
Cdd:COG4988 82 aFRAAARVKRRLRRRLLEKLLALGPAWLRGK--STGELATLLTEGVEALDGYFARYLPQLFlAALVPLL--ILVAVFpLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 922 WKLGLVCASTIPVLLAcgflrFWIL--ARFEQRSKKAYEK----SASYAcEATSAIRTVASLTREEDvyasyHQQLVDQG 995
Cdd:COG4988 158 WLSGLILLVTAPLIPL-----FMILvgKGAAKASRRQWRAlarlSGHFL-DRLRGLTTLKLFGRAKA-----EAERIAEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 996 AKNLR----SILKsstlYALSQSG-----MFLCTALGFWYGGTLISKGEYSLFQ-FFVCFSAITFgaqsagtifsFAP-- 1063
Cdd:COG4988 227 SEDFRkrtmKVLR----VAFLSSAvleffASLSIALVAVYIGFRLLGGSLTLFAaLFVLLLAPEF----------FLPlr 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1064 DMGKAKH-------AAIQLKTLFDRKPEIDTWSSDGEKINNmEGHIEFRNVHFRYPtrPEQPVLRGLNLSVKPGQYVALV 1136
Cdd:COG4988 293 DLGSFYHarangiaAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1137 GASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGTIRDNILLGadRENVPEEAIIKAC 1216
Cdd:COG4988 370 GPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLG--RPDASDEELEAAL 447
|
490
....*....|...
gi 407923078 1217 KDANIYDFIMSLP 1229
Cdd:COG4988 448 EAAGLDEFVAALP 460
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
432-670 |
5.15e-42 |
|
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: 162.38 E-value: 5.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEVTVmNGVDLVVEAGKTTALVGASGSGKST----IVGLVERFYDpVGGEVLLDGVNVQELNLHWLR 507
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTlalaLMGLLPHGGR-ISGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 508 QQISLVQQEP--VLFATTIFDNIKHGLIGTQyehLEHEKVREMVYNAAKMSNAHDFVSALPegyetnvgergFLLSGGQK 585
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEALENLG---LSRAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 586 QRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHN 662
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPE 228
|
....*...
gi 407923078 663 ELLERKQA 670
Cdd:COG1123 229 EILAAPQA 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
432-660 |
8.18e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 156.78 E-value: 8.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRP-EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLV---ERfydPVGGEVLLDGVNVQELN---LH 504
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInllER---PTSGSVLVDGVDLTALSereLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 505 WLRQQISLVQQEPVLFAT-TIFDNIKHGLIGTQYEHLE-HEKVREMVynaakmsnahDFV------SALPEGyetnvger 576
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVALPLEIAGVPKAEiRKRVAELL----------ELVglsdkaDAYPSQ-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 577 gflLSGGQKQRIAIARAIVSDPKILLLDEATSALD---TKSegvVQAALDRAAQ--GRTTIVIAHRLSTIKT-ADKIVVM 650
Cdd:COG1135 141 ---LSGGQKQRVGIARALANNPKVLLCDEATSALDpetTRS---ILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVL 214
|
250
....*....|
gi 407923078 651 SQGRIVEQGT 660
Cdd:COG1135 215 ENGRIVEQGP 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
436-654 |
1.92e-41 |
|
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: 150.42 E-value: 1.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQELNLHW--LRQQ 509
Cdd:cd03229 2 ELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTllrcIAGLEE----PDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEPVLFAT-TIFDNIkhgligtqyehlehekvremvynaakmsnahdfvsalpegyetnvgerGFLLSGGQKQRI 588
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENI------------------------------------------------ALGLSGGQQQRV 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 589 AIARAIVSDPKILLLDEATSALDTKSEGVVQAALD--RAAQGRTTIVIAHRLSTIKT-ADKIVVMSQGR 654
Cdd:cd03229 110 ALARALAMDPDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
438-667 |
1.01e-40 |
|
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: 153.29 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 438 KHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVERFYDpVGGEVLLDGVNVQELN---LHWLR-QQ 509
Cdd:COG0444 9 VYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTlaraILGLLPPPGI-TSGEILFDGEDLLKLSekeLRKIRgRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQE------PVLfatTIFDNIKHGLIgtQYEHLEHEKVREMVYNAAKM---SNAHDFVSALPegyetnvgergFLL 580
Cdd:COG0444 88 IQMIFQDpmtslnPVM---TVGDQIAEPLR--IHGGLSKAEARERAIELLERvglPDPERRLDRYP-----------HEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 581 SGGQKQRIAIARAIVSDPKILLLDEATSALDTksegVVQAA-LD-----RAAQGRTTIVIAHRLSTIK-TADKIVVMSQG 653
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQiLNllkdlQRELGLAILFITHDLGVVAeIADRVAVMYAG 227
|
250
....*....|....
gi 407923078 654 RIVEQGTHNELLER 667
Cdd:COG0444 228 RIVEEGPVEELFEN 241
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
431-657 |
1.02e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 151.01 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 431 RVELRQVKHIYPSRP-EVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQELnlhw 505
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTllrlIAGLEK----PTSGEVLVDGKPVTGP---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 506 lRQQISLVQQEPVLFA-TTIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPegYEtnvgergflLSGGQ 584
Cdd:COG1116 79 -GPDRGVVFQEPALLPwLTVLDNVALGL---ELRGVPKAERRERARELLELVGLAGFEDAYP--HQ---------LSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 585 KQRIAIARAIVSDPKILLLDEATSALD--TKSEgvVQAALDR--AAQGRTTIVIAH------RLstiktADKIVVMSQ-- 652
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDalTRER--LQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArp 216
|
....*
gi 407923078 653 GRIVE 657
Cdd:COG1116 217 GRIVE 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
432-659 |
1.66e-40 |
|
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: 147.46 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEvTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNlHWLRQQIS 511
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFATTIFDNIkhgligtqyehlehekvremvynaakmsnahdfvsalpegyetnvGERgflLSGGQKQRIAIA 591
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------------GRR---FSGGERQRLALA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 592 RAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQG 659
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
430-660 |
2.22e-40 |
|
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: 148.33 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 430 GRVELRQVKHIY-PSRPEVtvMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQ 508
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 QISLVQQEPVLFATTIFDNIKhgligtQYEHLEHEKVREmvynaakmsnahdfvsALpegyetNVGERGFLLSGGQKQRI 588
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLD------PFDEYSDEEIYG----------------AL------RVSEGGLNLSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 589 AIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGT 660
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
432-655 |
2.37e-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: 148.79 E-value: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPE-VTVMNGVDLVVEAGKTTALVGASGSGKST---IVGLVERfydPVGGEVLLDGVNVQELNLHWL- 506
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 507 ---RQQISLVQQEPVLFAT-TIFDNIKHGLIGTQYEHLE-HEKVREMVynaAKMsnahdfvsALPEGYETNVGErgflLS 581
Cdd:cd03255 78 afrRRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKErRERAEELL---ERV--------GLGDRLNHYPSE----LS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 582 GGQKQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALDRAAQGRTTIVIA-HRLSTIKTADKIVVMSQGRI 655
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSEtGKEVMELLRELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
432-669 |
5.08e-40 |
|
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: 149.50 E-value: 5.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRpEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVN-VQELNLHWLRQQI 510
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 511 SLVQQEP--VLFATTIFDNIKHGL--IGtqyehLEHEKVREMVYNAAKMSNAHDFVSALPegyetnvgergFLLSGGQKQ 586
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLenLG-----VPREEMRKRVDEALKLVGMEDFRDREP-----------HLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 587 RIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALD-RAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNEL 664
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREI 223
|
....*
gi 407923078 665 LERKQ 669
Cdd:TIGR04520 224 FSQVE 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1102-1229 |
5.12e-40 |
|
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: 148.15 E-value: 5.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPtrPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIA 1181
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 407923078 1182 LVSQEPTLYQGTIRDNILLGadRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYG--RPDATDEEVIEAAKAAQIHDKIMRFP 124
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
415-1229 |
1.48e-39 |
|
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: 160.88 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 415 LDPTSKEGRRLENLQGR-VELRQVKHIYpSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLL 493
Cdd:TIGR00957 619 LEPDSIERRTIKPGEGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 494 DGvnvqelnlhwlrqQISLVQQEPVLFATTIFDNIkhgLIGTQyehLEHEKVREMVYNAAKMSNahdfVSALPEGYETNV 573
Cdd:TIGR00957 698 KG-------------SVAYVPQQAWIQNDSLRENI---LFGKA---LNEKYYQQVLEACALLPD----LEILPSGDRTEI 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 574 GERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKsegVVQAALDRAA------QGRTTIVIAHRLSTIKTADKI 647
Cdd:TIGR00957 755 GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH---VGKHIFEHVIgpegvlKNKTRILVTHGISYLPQVDVI 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 648 VVMSQGRIVEQGTHNELLERKQAYYNLV-----EAQRIAAANEKIEEEEEEEEEVDLTE----VDDETIKRTVSPQSEKR 718
Cdd:TIGR00957 832 IVMSGGKISEMGSYQELLQRDGAFAEFLrtyapDEQQGHLEDSWTALVSGEGKEAKLIEngmlVTDVVGKQLQRQLSASS 911
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 719 SYSVDPDDDVAARLKRTQSGKSESSVALAKKQPASEQKYSLATL---IKLIASFNRqewllmvqglFWSIIAGGGNPTQA 795
Cdd:TIGR00957 912 SDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQTGQVELSVYwdyMKAIGLFIT----------FLSIFLFVCNHVSA 981
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 796 VFFAKSISALSRPPSEYGKlRSEANFWSLMYLMLALTQLISFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQEE 875
Cdd:TIGR00957 982 LASNYWLSLWTDDPMVNGT-QNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTP 1060
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 876 nSAGALTSF---LSTETTSLAGLSGATLGTIFTVLTTLIgALVLGIAIGwklglvcASTIPVLLACGFL--RFWI----- 945
Cdd:TIGR00957 1061 -SGNLVNRFskeLDTVDSMIPPVIKMFMGSLFNVIGALI-VILLATPIA-------AVIIPPLGLLYFFvqRFYVassrq 1131
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 946 LARFEQRSKKAYEKSASYACEATSAIRtvaSLTREEDVyasYHQQ--LVDQGAKNLRSILKSSTLYALSQSGMFLCTALg 1023
Cdd:TIGR00957 1132 LKRLESVSRSPVYSHFNETLLGVSVIR---AFEEQERF---IHQSdlKVDENQKAYYPSIVANRWLAVRLECVGNCIVL- 1204
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1024 fwYGGTLISKGEYSLFQFFVCFSaITFGAQSAGTI---FSFAPDMGKAKHAAIQLKTLFDRKPEIdTWSSDGEKINN--- 1097
Cdd:TIGR00957 1205 --FAALFAVISRHSLSAGLVGLS-VSYSLQVTFYLnwlVRMSSEMETNIVAVERLKEYSETEKEA-PWQIQETAPPSgwp 1280
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1098 MEGHIEFRNVHFRYptRPE-QPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDY 1176
Cdd:TIGR00957 1281 PRGRVEFRNYCLRY--REDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL 1358
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 407923078 1177 RSYIALVSQEPTLYQGTIRDNIllgADRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:TIGR00957 1359 RFKITIIPQDPVLFSGSLRMNL---DPFSQYSDEEVWWALELAHLKTFVSALP 1408
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1102-1199 |
1.69e-39 |
|
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: 144.45 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIA 1181
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90
....*....|....*...
gi 407923078 1182 LVSQEPTLYQGTIRDNIL 1199
Cdd:cd03228 80 YVPQDPFLFSGTIRENIL 97
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
436-667 |
1.78e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 146.68 E-value: 1.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNV--QELNLHWLRQQ 509
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrcINLLEE----PDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEPVLFA-TTIFDNIKHGLIgtqyehleheKVREMVYNAAKmSNAH---------DFVSALPEGyetnvgergfl 579
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLAPI----------KVKKMSKAEAE-ERAMellervglaDKADAYPAQ----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSEgVVQAALDRAAQGRTTIVIAH-----RlstiKTADKIVVMSQ 652
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDpeLVGE-VLDVMRDLAKEGMTMVVVTHemgfaR----EVADRVVFMDG 211
|
250
....*....|....*
gi 407923078 653 GRIVEQGTHNELLER 667
Cdd:COG1126 212 GRIVEEGPPEEFFEN 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
436-665 |
3.23e-39 |
|
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: 146.73 E-value: 3.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQ 515
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 516 EPVL-FATTIFDNIKHGLigtqYEHL-----EHEKVREMVYNAAKMSNAHDFVsalpegyETNVGErgflLSGGQKQRIA 589
Cdd:COG1120 83 EPPApFGLTVRELVALGR----YPHLglfgrPSAEDREAVEEALERTGLEHLA-------DRPVDE----LSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
436-667 |
3.95e-39 |
|
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: 146.16 E-value: 3.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLhWLRQQISLVQQ 515
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 516 EPVLFAT-TIFDNIKhgLIGTQYeHLEHEKVREMVYNAAKMSNahdfvsaLPEGYETNVGErgflLSGGQKQRIAIARAI 594
Cdd:COG4555 82 ERGLYDRlTVRENIR--YFAELY-GLFDEELKKRIEELIELLG-------LEEFLDRRVGE----LSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 595 VSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNELLER 667
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
432-679 |
4.67e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 145.59 E-value: 4.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSrpeVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQElNLHWLRQQIS 511
Cdd:COG1131 1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFAT-TIFDNIKH--GLIGTQYEHLEhEKVREMVynaakmsnahDFVSaLPEGYETNVGErgflLSGGQKQRI 588
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFfaRLYGLPRKEAR-ERIDELL----------ELFG-LTDAADRKVGT----LSGGMKQRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 589 AIARAIVSDPKILLLDEATSALDTKS-EGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNELLE 666
Cdd:COG1131 141 GLALALLHDPELLILDEPTSGLDPEArRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
250
....*....|....*
gi 407923078 667 R--KQAYYNLVEAQR 679
Cdd:COG1131 221 RllEDVFLELTGEEA 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
432-658 |
9.73e-39 |
|
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: 144.15 E-value: 9.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPS-RPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNlhwlrQQI 510
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 511 SLVQQEPVLFA-TTIFDNIKHGLigtqyehleheKVREMVYNAAKmSNAHDFVSAlpegyetnVGERGFL------LSGG 583
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGL-----------ELQGVPKAEAR-ERAEELLEL--------VGLSGFEnayphqLSGG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 584 QKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLS-TIKTADKIVVMSQ--GRIVEQ 658
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
432-665 |
1.40e-38 |
|
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: 144.37 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPevTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQIS 511
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFA-TTIFDNIkhGLIgTQYEHLEHEKVREMVYNAAKMsnahdfVSALPEGYetnvGER-GFLLSGGQKQRIA 589
Cdd:cd03295 79 YVIQQIGLFPhMTVEENI--ALV-PKLLKWPKEKIRERADELLAL------VGLDPAEF----ADRyPHELSGGQQQRVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRL-STIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
142-674 |
1.40e-38 |
|
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: 157.41 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 142 MSNGEFNDELVKFVLYFVyLFIGEFFTCYIATVGWIYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANL 221
Cdd:TIGR00957 996 MVNGTQNNTSLRLSVYGA-LGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDT 1074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 222 VQDGISEKVGLVQQSLATFITAFVIgfvkywkltLILCSTIFAIVF-TMGGGSTFIMK-YNKQSLASYALGGTVVEEVFS 299
Cdd:TIGR00957 1075 VDSMIPPVIKMFMGSLFNVIGALIV---------ILLATPIAAVIIpPLGLLYFFVQRfYVASSRQLKRLESVSRSPVYS 1145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 300 SIRNAV-------AFGTQDKLARQYNEHL----------VIAEYWgkkmktvLASMLGAMMTIVYLNYGLAFWMGSRYLV 362
Cdd:TIGR00957 1146 HFNETLlgvsvirAFEEQERFIHQSDLKVdenqkayypsIVANRW-------LAVRLECVGNCIVLFAALFAVISRHSLS 1218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 363 KGEMSLSDVLTILLAVMIGafslgnigpWLqafttaTAAASKMYSTI---DRVSPLDPTSKEGR-RLENLQ--------G 430
Cdd:TIGR00957 1219 AGLVGLSVSYSLQVTFYLN---------WL------VRMSSEMETNIvavERLKEYSETEKEAPwQIQETAppsgwpprG 1283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 431 RVELRQVKHIYpsRPEVT-VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQ 509
Cdd:TIGR00957 1284 RVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFK 1361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEPVLFATTIFDNIKHGligTQYEHlehekvrEMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIA 589
Cdd:TIGR00957 1362 ITIIPQDPVLFSGSLRMNLDPF---SQYSD-------EEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVC 1431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQ 669
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
....*
gi 407923078 670 AYYNL 674
Cdd:TIGR00957 1512 IFYSM 1516
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1102-1229 |
2.36e-38 |
|
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: 143.53 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPEqPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIA 1181
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 407923078 1182 LVSQEPTLYQGTIRDNILLGadRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG--RPGATREEVEEAARAANAHEFIMELP 125
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
130-1198 |
1.55e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 153.98 E-value: 1.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 130 LSGTFQGMFQGtmsngefNDELVKFVLYFVyLFIGEFFTCYIATVGWIYVGeRISSRIREYYLSAILRQNVGYFDK---- 205
Cdd:PLN03232 324 LSHLLQSMQEG-------DPAWVGYVYAFL-IFFGVTFGVLCESQYFQNVG-RVGFRLRSTLVAAIFHKSLRLTHEarkn 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 206 LGAGEITTRITADANLVQDgISEKV-GLvqqslatfitafvigfvkyWkltlilcSTIFAIVFTMgggstfIMKYNKQSL 284
Cdd:PLN03232 395 FASGKVTNMITTDANALQQ-IAEQLhGL-------------------W-------SAPFRIIVSM------VLLYQQLGV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 285 ASyalggtvveeVFSSIRNAVAFGTQDKLARQYNEHLVIAEYWGKKMKTVLASMLGAMMTIVYLNYGLAF---------- 354
Cdd:PLN03232 442 AS----------LFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFesriqgirne 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 355 ---WMGSRYLVKGEMS--LSDVLTILLAVMIGAFSL--GNIGPW--LQAFTTATAAASKMYSTIDRVSPLDPTSKEGRRL 425
Cdd:PLN03232 512 elsWFRKAQLLSAFNSfiLNSIPVVVTLVSFGVFVLlgGDLTPAraFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRI 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 426 ENL---QGRVeLRQVKHIYPSRPEVTVMNG---------------VDLVVEAGKTTALVGASGSGKSTIVglverfydpv 487
Cdd:PLN03232 592 EELllsEERI-LAQNPPLQPGAPAISIKNGyfswdsktskptlsdINLEIPVGSLVAIVGGTGEGKTSLI---------- 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 488 ggEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIkhgLIGTQYEHLEHEKVREMVynaakmSNAHDfVSALPE 567
Cdd:PLN03232 661 --SAMLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENI---LFGSDFESERYWRAIDVT------ALQHD-LDLLPG 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 568 GYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALDRAAQGRTTIVIAHRLSTIKTADK 646
Cdd:PLN03232 729 RDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDR 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 647 IVVMSQGRIVEQGTHNELLERKQAYYNLVE-AQRIAAANEkieeeeeeeeevdlTEVDDETIKRtVSPQSEKrsysvdpd 725
Cdd:PLN03232 809 IILVSEGMIKEEGTFAELSKSGSLFKKLMEnAGKMDATQE--------------VNTNDENILK-LGPTVTI-------- 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 726 dDVAAR-LKRTQSGKSESSVaLAKKQPASEQKYSLATLIKliasFNRQE---WLLMVqgLFWSIIagggnpTQAVFFAKS 801
Cdd:PLN03232 866 -DVSERnLGSTKQGKRGRSV-LVKQEERETGIISWNVLMR----YNKAVgglWVVMI--LLVCYL------TTEVLRVSS 931
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 802 ISALSRPPSEYGKLRSEANFWSLMYLMLALTQL-ISFTGQglcFAICSEKL--IHRVRDTAFRTMLRQDISFFdqEENSA 878
Cdd:PLN03232 932 STWLSIWTDQSTPKSYSPGFYIVVYALLGFGQVaVTFTNS---FWLISSSLhaAKRLHDAMLNSILRAPMLFF--HTNPT 1006
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 879 GALTSFLSTET----TSLAGLSGATLGTIFTVLTT--LIGaLVLGIAIgWKLglvcaSTIPVLLACGFLRFWILARfEQR 952
Cdd:PLN03232 1007 GRVINRFSKDIgdidRNVANLMNMFMNQLWQLLSTfaLIG-TVSTISL-WAI-----MPLLILFYAAYLYYQSTSR-EVR 1078
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 953 SKKAYEKSASYAC--EATSAIRTVASltreedvYASYHQQLVDQGA---KNLRSILKSS------TLYALSQSGMFLcta 1021
Cdd:PLN03232 1079 RLDSVTRSPIYAQfgEALNGLSSIRA-------YKAYDRMAKINGKsmdNNIRFTLANTssnrwlTIRLETLGGVMI--- 1148
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1022 lgfWYGGTliskgeYSLFQFFVCFSAITFgAQSAGTIFSFAPD--------MGKAKHAAIQLKTLFDRKPEIDTWSSDGE 1093
Cdd:PLN03232 1149 ---WLTAT------FAVLRNGNAENQAGF-ASTMGLLLSYTLNittllsgvLRQASKAENSLNSVERVGNYIDLPSEATA 1218
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1094 KINN--------MEGHIEFRNVHFRYptRPE-QPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYAD 1164
Cdd:PLN03232 1219 IIENnrpvsgwpSRGSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMID 1296
|
1130 1140 1150
....*....|....*....|....*....|....
gi 407923078 1165 GKEISSLNINDYRSYIALVSQEPTLYQGTIRDNI 1198
Cdd:PLN03232 1297 DCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
452-671 |
4.22e-37 |
|
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: 139.78 E-value: 4.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 452 GVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHwlRQQISLVQQEPVLFA-TTIFDNIKH 530
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 531 GLIGTQYEHLE-HEKVREMvynaAKMSNAHDFVSALPEgyetnvgergfLLSGGQKQRIAIARAIVSDPKILLLDEATSA 609
Cdd:cd03299 95 GLKKRKVDKKEiERKVLEI----AEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 610 LDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTIKT-ADKIVVMSQGRIVEQGTHNELLERKQAY 671
Cdd:cd03299 160 LDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNE 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
432-667 |
4.51e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 143.70 E-value: 4.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPsrpEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGlverFYDPVGGEVLLDGVNVQELNLHwlR 507
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTllrmIAG----FETPDSGRILLDGRDVTGLPPE--K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 508 QQISLVQQEPVLFA-TTIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMsnahdfvsalpegyetnVGERGFL------L 580
Cdd:COG3842 77 RNVGMVFQDYALFPhLTVAENVAFGL---RMRGVPKAEIRARVAELLEL-----------------VGLEGLAdryphqL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 581 SGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAHRLS---TIktADKIVVMSQGRI 655
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRI 214
|
250
....*....|..
gi 407923078 656 VEQGTHNELLER 667
Cdd:COG3842 215 EQVGTPEEIYER 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1097-1229 |
5.41e-37 |
|
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: 139.14 E-value: 5.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1097 NMEGHIEFRNVHFRYPTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDY 1176
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 407923078 1177 RSYIALVSQEPTLYQGTIRDNILLGAdrENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGL--QSCSFECVKEAAQKAHAHSFISELA 137
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
443-1198 |
7.74e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 151.81 E-value: 7.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 443 SRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVErfydpvgGEV--LLDGVNVqelnlhwLRQQISLVQQEPVLF 520
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAML-------GELppRSDASVV-------IRGTVAYVPQVSWIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 521 ATTIFDNIkhgLIGTQYEHLEHEKVREMVynaakmSNAHDfVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKI 600
Cdd:PLN03130 692 NATVRDNI---LFGSPFDPERYERAIDVT------ALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 601 LLLDEATSALDTK-SEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAYYNLVEAqr 679
Cdd:PLN03130 762 YIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMEN-- 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 680 iAAANEkieeeeeeeeevdltEVDDETIKRTVSPQSEKRSysvdpDDDVAARLKRTQSGKSES----SVaLAKKQPASEQ 755
Cdd:PLN03130 840 -AGKME---------------EYVEENGEEEDDQTSSKPV-----ANGNANNLKKDSSSKKKSkegkSV-LIKQEERETG 897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 756 KYSLATLIKLIASFNrQEWLLMVqgLFWSIIAgggnpTQaVFFAKSISALSRPPSEYGKLRSEANFWSLMYLMLALTQLI 835
Cdd:PLN03130 898 VVSWKVLERYKNALG-GAWVVMI--LFLCYVL-----TE-VFRVSSSTWLSEWTDQGTPKTHGPLFYNLIYALLSFGQVL 968
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 836 SFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFdqEENSAGALTSFLSTET----TSLAGLSGATLGTIFTVLTT-- 909
Cdd:PLN03130 969 VTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFF--HTNPLGRIINRFAKDLgdidRNVAVFVNMFLGQIFQLLSTfv 1046
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 910 LIGaLVLGIAIgWklglvcaSTIPVLLA--CGFLRFWILARfEQRSKKAYEKSASYA--CEATSAIRTVASLtREEDVYA 985
Cdd:PLN03130 1047 LIG-IVSTISL-W-------AIMPLLVLfyGAYLYYQSTAR-EVKRLDSITRSPVYAqfGEALNGLSTIRAY-KAYDRMA 1115
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 986 SYHQQLVDQgakNLRsilksSTLYALSqSGMFLCTALGFwYGGTLIskgeyslfqfFVCFSAITFGAQSAGTIFSFAPDM 1065
Cdd:PLN03130 1116 EINGRSMDN---NIR-----FTLVNMS-SNRWLAIRLET-LGGLMI----------WLTASFAVMQNGRAENQAAFASTM 1175
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1066 GKAKHAAIQLKTLF----------------------------DRKPEIDT------WSSDGEkinnmeghIEFRNVHFRY 1111
Cdd:PLN03130 1176 GLLLSYALNITSLLtavlrlaslaenslnavervgtyidlpsEAPLVIENnrpppgWPSSGS--------IKFEDVVLRY 1247
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1112 ptRPE-QPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLY 1190
Cdd:PLN03130 1248 --RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLF 1325
|
....*...
gi 407923078 1191 QGTIRDNI 1198
Cdd:PLN03130 1326 SGTVRFNL 1333
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
433-654 |
9.86e-37 |
|
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: 135.84 E-value: 9.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 433 ELRQVKHIYPSRPevtVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISL 512
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 513 VQQepvlfattifdnikhgligtqyehlehekvremvynaakmsnahdfvsalpegyetnvgergflLSGGQKQRIAIAR 592
Cdd:cd00267 78 VPQ----------------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 593 AIVSDPKILLLDEATSALDTKS-EGVVQAALDRAAQGRTTIVIAHRLSTIKTA-DKIVVMSQGR 654
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASrERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
432-667 |
1.20e-36 |
|
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: 138.52 E-value: 1.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSrpeVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHwlRQQIS 511
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFA-TTIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQRIAI 590
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGL---RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 591 ARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTIKT-ADKIVVMSQGRIVEQGTHNELLER 667
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
451-608 |
1.64e-36 |
|
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: 135.08 E-value: 1.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 451 NGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLF-ATTIFDNIK 529
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 530 HGLIGtqYEHLEHEKvremvynAAKMSNAHDFVSaLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATS 608
Cdd:pfam00005 82 LGLLL--KGLSKREK-------DARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
432-683 |
2.63e-36 |
|
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: 145.60 E-value: 2.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSR--------PEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVerfydPVGGEVLLDGVNVQ 499
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 500 ELN---LHWLRQQISLVQQEPvlFAT-----TIFDNIKHGLiGTQYEHLEHEKVREMVynaakmsnahdfVSALPEgyet 571
Cdd:COG4172 351 GLSrraLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGL-RVHGPGLSAAERRARV------------AEALEE---- 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 572 nVG-ERGFL------LSGGQKQRIAIARAIVSDPKILLLDEATSALDtKSegvVQA---ALDRAAQGR---TTIVIAHRL 638
Cdd:COG4172 412 -VGlDPAARhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VS---VQAqilDLLRDLQREhglAYLFISHDL 486
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 407923078 639 STIKT-ADKIVVMSQGRIVEQGTHNELLER-KQAYynlveAQR-IAAA 683
Cdd:COG4172 487 AVVRAlAHRVMVMKDGKVVEQGPTEQVFDApQHPY-----TRAlLAAA 529
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
436-667 |
4.82e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 140.28 E-value: 4.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLvERfydPVGGEVLLDGVNVQeLNLHWLRQQIS 511
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTllriIAGL-ET---PDSGRIVLNGRDLF-TNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFA-TTIFDNIKHGL-IGTQYEHLEHEKVREMVynaaKMSNAHDFVSALPEGyetnvgergflLSGGQKQRIA 589
Cdd:COG1118 79 FVFQHYALFPhMTVAENIAFGLrVRPPSKAEIRARVEELL----ELVQLEGLADRYPSQ-----------LSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKsegvVQAALDR------AAQGRTTIVIAH------RLstiktADKIVVMSQGRIVE 657
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDAK----VRKELRRwlrrlhDELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQ 214
|
250
....*....|
gi 407923078 658 QGTHNELLER 667
Cdd:COG1118 215 VGTPDEVYDR 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
432-660 |
1.08e-35 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 139.17 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYP-SRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN---LHWLR 507
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 508 QQISLVQQEPVLFAT-TIFDNIKHGL--IGTQYEHLEhEKVRE---MVYNAAKmsnaHDFvsalpegYETNvgergflLS 581
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALPLelAGTPKAEIK-ARVTElleLVGLSDK----ADR-------YPAQ-------LS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 582 GGQKQRIAIARAIVSDPKILLLDEATSALDTKSegvVQAALDRAAQ-----GRTTIVIAHRLSTIK-TADKIVVMSQGRI 655
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPAT---TRSILELLKDinrelGLTIVLITHEMDVVKrICDRVAVIDAGRL 219
|
....*
gi 407923078 656 VEQGT 660
Cdd:PRK11153 220 VEQGT 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
432-667 |
1.36e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 138.71 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYP------SRPEVTV--MNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN- 502
Cdd:COG4608 8 LEVRDLKKHFPvrgglfGRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 503 --LHWLRQQISLVQQEPvlFAT-----TIFDNIKHGL----IGTQYEHLEheKVREMVynaakmsnahDFVSALPEGYET 571
Cdd:COG4608 88 reLRPLRRRMQMVFQDP--YASlnprmTVGDIIAEPLrihgLASKAERRE--RVAELL----------ELVGLRPEHADR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 572 NVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALDtKSegvVQAA-----LD-RAAQGRTTIVIAHRLSTIK-TA 644
Cdd:COG4608 154 YPHE----FSGGQRQRIGIARALALNPKLIVCDEPVSALD-VS---IQAQvlnllEDlQDELGLTYLFISHDLSVVRhIS 225
|
250 260
....*....|....*....|...
gi 407923078 645 DKIVVMSQGRIVEQGTHNELLER 667
Cdd:COG4608 226 DRVAVMYLGKIVEIAPRDELYAR 248
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
430-667 |
1.40e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 139.05 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 430 GRVELRQVKHIYPsrpEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLverfYDPVGGEVLLDGVNVQEL---- 501
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrmIAGL----EDPTSGEILIGGRDVTDLppkd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 502 -NlhwlrqqISLVQQEPVLF-ATTIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergfl 579
Cdd:COG3839 75 rN-------IAMVFQSYALYpHMTVYENIAFPL---KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQ----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAHRLS---TIktADKIVVMSQGR 654
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRlhRRLGTTTIYVTHDQVeamTL--ADRIAVMNDGR 211
|
250
....*....|...
gi 407923078 655 IVEQGTHNELLER 667
Cdd:COG3839 212 IQQVGTPEELYDR 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
432-664 |
1.93e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.57 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRpeVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN---LHWLRQ 508
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 QISLVQQEPVLFA-TTIFDNIKHGLIGTqyehleHEKVREMV--YNAAKMSNAHDfvsALPEgyetnVGERGFL------ 579
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVLAGRLGR------TSTWRSLLglFPPEDRERALE---ALER-----VGLADKAyqradq 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTIKT-ADKIVVMSQGRIV 656
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
....*...
gi 407923078 657 EQGTHNEL 664
Cdd:COG3638 227 FDGPPAEL 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
75-677 |
3.35e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 146.66 E-value: 3.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 75 REILKRQLDTPPVSISYFALYRYATKLE--WIIIVVssicaiaagAVLPLMTVVFGSLSGTFQGMFQGTMSNGEFNDELv 152
Cdd:PLN03232 882 RSVLVKQEERETGIISWNVLMRYNKAVGglWVVMIL---------LVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSPGF- 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 153 kFVLYFVYLFIGEFFTCYIATVGWIYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEK--- 229
Cdd:PLN03232 952 -YIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLmnm 1030
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 230 -VGLVQQSLATFITAFVIGFVKYWKLT--LILcstIFAIVFTMGGGSTFIMKYNKQSLAS-YALGGTVVEEVfSSIRNAV 305
Cdd:PLN03232 1031 fMNQLWQLLSTFALIGTVSTISLWAIMplLIL---FYAAYLYYQSTSREVRRLDSVTRSPiYAQFGEALNGL-SSIRAYK 1106
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 306 AFGTQDKLARQY---NEHLVIAEYWGKKMKTVLASMLGAMM-----TIVYLNYGLAfwmgsrylvKGEMSLSDVLTILLA 377
Cdd:PLN03232 1107 AYDRMAKINGKSmdnNIRFTLANTSSNRWLTIRLETLGGVMiwltaTFAVLRNGNA---------ENQAGFASTMGLLLS 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 378 VMIgafslgNIGPWLQAFTTATAAASKMYSTIDRVSP-LDPTSKEGRRLEN--------LQGRVELRQVKHIYpsRPEVT 448
Cdd:PLN03232 1178 YTL------NITTLLSGVLRQASKAENSLNSVERVGNyIDLPSEATAIIENnrpvsgwpSRGSIKFEDVHLRY--RPGLP 1249
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 -VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDN 527
Cdd:PLN03232 1250 pVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFN 1329
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 528 IKhgligtqyEHLEHEKVRemVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEAT 607
Cdd:PLN03232 1330 ID--------PFSEHNDAD--LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 608 SALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERK-QAYYNLVEA 677
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDtSAFFRMVHS 1470
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
432-669 |
3.67e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 135.50 E-value: 3.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRpEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQIS 511
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEP--VLFATTIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQRIA 589
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGL---ENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKS-EGVVQAALDRAAQG-RTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLER 667
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGkREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
..
gi 407923078 668 KQ 669
Cdd:PRK13632 233 KE 234
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
436-655 |
4.74e-35 |
|
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: 133.04 E-value: 4.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNV--QELNLHWLRQQISLV 513
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 514 QQEPVLFA-TTIFDNIKHGLIgtqyehleheKVREMVYNAAKmsnahdfvsALPEGYETNVGERGFL------LSGGQKQ 586
Cdd:cd03262 82 FQQFNLFPhLTVLENITLAPI----------KVKGMSKAEAE---------ERALELLEKVGLADKAdaypaqLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 587 RIAIARAIVSDPKILLLDEATSALDTKSEG-VVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRI 655
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGeVLDVMKDLAEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
432-654 |
1.19e-34 |
|
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: 131.82 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEVT--VMNGVDLVVEAGKTTALVGASGSGKST----IVGLVERfydpVGGEVLLDGvnvqelnlhw 505
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSllsaLLGELEK----LSGSVSVPG---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 506 lrqQISLVQQEPVLFATTIFDNIkhgLIGTQYEHLEHEKVREmvynAAKMSNahDFvSALPEGYETNVGERGFLLSGGQK 585
Cdd:cd03250 67 ---SIAYVSQEPWIQNGTIRENI---LFGKPFDEERYEKVIK----ACALEP--DL-EILPDGDLTEIGEKGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 586 QRIAIARAIVSDPKILLLDEATSALDTKS-----EGVVQAALdraAQGRTTIVIAHRLSTIKTADKIVVMSQGR 654
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
432-655 |
7.28e-34 |
|
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: 128.28 E-value: 7.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPevtVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQElNLHWLR 507
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTlikiILGLLK----PDSGEIKVLGKDIKK-EPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 508 QQISLVQQEPVLfattifdnikhgligtqYEHLeheKVREMVYnaakmsnahdfvsalpegyetnvgergflLSGGQKQR 587
Cdd:cd03230 73 RRIGYLPEEPSL-----------------YENL---TVRENLK-----------------------------LSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 588 IAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRI 655
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESrREFWELLRELKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
449-672 |
8.61e-34 |
|
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: 131.18 E-value: 8.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNI 528
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 529 KHgligtqyehlEHEKVREMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATS 608
Cdd:cd03288 116 DP----------ECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 609 ALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAYY 672
Cdd:cd03288 186 SIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVF 249
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
451-666 |
1.06e-33 |
|
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: 131.23 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 451 NGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQ----QISLVQQEPVLFA-TTIF 525
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPhRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 526 DNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPegyetnvGErgflLSGGQKQRIAIARAIVSDPKILLLDE 605
Cdd:cd03294 121 ENVAFGL---EVQGVPRAEREERAAEALELVGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 606 ATSALDTKSEGVVQAALDR--AAQGRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQGTHNELLE 666
Cdd:cd03294 187 AFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
436-659 |
1.08e-33 |
|
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: 127.94 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQ 515
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 516 epVLFATTIfdnikhgligtqyEHLEHEKVREmvynaakmsnahdfvsalpegyetnvgergflLSGGQKQRIAIARAIV 595
Cdd:cd03214 81 --ALELLGL-------------AHLADRPFNE--------------------------------LSGGERQRVLLARALA 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 596 SDPKILLLDEATSALDTKSEgvvQAALDRAAQ-----GRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQG 659
Cdd:cd03214 114 QEPPILLLDEPTSHLDIAHQ---IELLELLRRlarerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
449-659 |
2.16e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 129.77 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYD--P---VGGEVLLDGVNV--QELNLHWLRQQISLVQQEPVLFA 521
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 522 TTIFDNIKHGLigTQYEHLEHEKVREMVYNAAKMSnahdfvsALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKIL 601
Cdd:COG1117 106 KSIYDNVAYGL--RLHGIKSKSELDEIVEESLRKA-------ALWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 602 LLDEATSALDTKSEGVVQAALDRAAQgRTTIVI-------AHRLStiktaDKIVVMSQGRIVEQG 659
Cdd:COG1117 177 LMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFG 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
432-655 |
5.17e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 128.28 E-value: 5.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPevtVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQELnlhwlR 507
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTllkaILGLLP----PTSGTVRLFGKPPRRA-----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 508 QQISLV-QQEPV--LFATTIFDNIKHGLIGTQ-----YEHLEHEKVREmvynAAKMSNAHDFVSalpegyeTNVGErgfl 579
Cdd:COG1121 75 RRIGYVpQRAEVdwDFPITVRDVVLMGRYGRRglfrrPSRADREAVDE----ALERVGLEDLAD-------RPIGE---- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTIKT-ADKIVVMSQGRI 655
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
433-664 |
1.15e-32 |
|
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: 127.30 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 433 ELRQVKHIYPSrpEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQEL---NLHWLRQQ 509
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEPVLFA-TTIFDNIKHGLIGTqyehleHEKVREMvynaAKMSNAHDFVSALpEGYETnVGERGFL------LSG 582
Cdd:cd03256 80 IGMIFQQFNLIErLSVLENVLSGRLGR------RSTWRSL----FGLFPKEEKQRAL-AALER-VGLLDKAyqradqLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 583 GQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTIKT-ADKIVVMSQGRIVEQG 659
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREyADRIVGLKDGRIVFDG 227
|
....*
gi 407923078 660 THNEL 664
Cdd:cd03256 228 PPAEL 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
432-684 |
1.96e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 130.45 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRpevTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQelNLHWLRQQIS 511
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFA-TTIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQRIAI 590
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGL---RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQ-----------LSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 591 ARAIVSDPKILLLDEATSALDTKSEGVVQAALdRAAQ---GRTTIVIAH-RLSTIKTADKIVVMSQGRIVEQGTHNELLE 666
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMQNEL-KALQrklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
250
....*....|....*...
gi 407923078 667 RKQayyNLVEAQRIAAAN 684
Cdd:PRK09452 235 EPK---NLFVARFIGEIN 249
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
433-667 |
2.81e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.02 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 433 ELRQVKHIYPSRPevtvMNgVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHwlRQQISL 512
Cdd:COG3840 3 RLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 513 VQQEPVLFA-TTIFDNIKHGL-IGTQYEHLEHEKVREMvynAAKMsNAHDFVSALPEGyetnvgergflLSGGQKQRIAI 590
Cdd:COG3840 76 LFQENNLFPhLTVAQNIGLGLrPGLKLTAEQRAQVEQA---LERV-GLAGLLDRLPGQ-----------LSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 591 ARAIVSDPKILLLDEATSALDT--KSEG---VVQAALDRaaqGRTTIVIAHRLSTIKT-ADKIVVMSQGRIVEQGTHNEL 664
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPalRQEMldlVDELCRER---GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
...
gi 407923078 665 LER 667
Cdd:COG3840 218 LDG 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
436-659 |
4.88e-32 |
|
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: 124.67 E-value: 4.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHwlRQQISLVQQ 515
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 516 EPVLFA-TTIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQRIAIARAI 594
Cdd:cd03301 80 NYALYPhMTVYDNIAFGL---KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 595 VSDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAH-RLSTIKTADKIVVMSQGRIVEQG 659
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
432-663 |
1.02e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.93 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIY-PSRP-EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNV--QELNLHWLR 507
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 508 QQISLVQQEP--VLFATTIFDNIKHGLIGTQyehLEHEKVREMVYNAAKMSnahdfvsALPegYETNVGERGFLLSGGQK 585
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLG---LSEEEIENRVKRAMNIV-------GLD--YEDYKDKSPFELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 586 QRIAIARAIVSDPKILLLDEATSALDTKS--EGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHN 662
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGrdEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPR 230
|
.
gi 407923078 663 E 663
Cdd:PRK13637 231 E 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
432-657 |
1.27e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 123.62 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPsrPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN---LHWLRQ 508
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 QISLVQQE-PVLFATTIFDNIKHGL--IGTqyehlEHEKVREMVYNAAKMSNAHDFVSALPEgyEtnvgergflLSGGQK 585
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALPLrvTGK-----SRKEIRRRVREVLDLVGLSDKAKALPH--E---------LSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 586 QRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQaALDRAAQGRTTIVIA-HRLSTIKTADK-IVVMSQGRIVE 657
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPEtSWEIME-LLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
446-666 |
1.81e-31 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 123.31 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 446 EVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVerfyDPVGGEVLLDGVNVQELNLHW-LRQQISLVQQEPVLF 520
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTllktIMGLL----PPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 521 AT-TIFDNIKHGliGTQYEHLEHEKVREMVYnaakmsnahDFVSALPEgyetNVGERGFLLSGGQKQRIAIARAIVSDPK 599
Cdd:cd03224 88 PElTVEENLLLG--AYARRRAKRKARLERVY---------ELFPRLKE----RRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 600 ILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVI----AHRLSTIktADKIVVMSQGRIVEQGTHNELLE 666
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLA 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
845-1229 |
1.86e-31 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 131.62 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 845 AICSEKLIHRVRDT----AFRTMLRQDISFfDQEENSAGALTSFLSTeTTSLAGLsgaTLGTIFTVLTTLIGALVL---G 917
Cdd:PRK13657 77 ARHADRLAHRRRLAvlteYFERIIQLPLAW-HSQRGSGRALHTLLRG-TDALFGL---WLEFMREHLATLVALVVLlplA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 918 IAIGWKLGLVcastipvLLACGFLrFWILARFEQRSKKA--------YEKSASYACEATSAIRTVASLTR-EEDVYA--S 986
Cdd:PRK13657 152 LFMNWRLSLV-------LVVLGIV-YTLITTLVMRKTKDgqaaveehYHDLFAHVSDAIGNVSVVQSYNRiEAETQAlrD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 987 YHQQLVDqgAKN-------LRSILK--SSTLyalSQSGMFLctaLGFWyggtLISKGEYSLFQF--FVCFSAITFG---- 1051
Cdd:PRK13657 224 IADNLLA--AQMpvlswwaLASVLNraASTI---TMLAILV---LGAA----LVQKGQLRVGEVvaFVGFATLLIGrldq 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1052 -AQSAGTIFSFAPDMGkakhaaiQLKTLFDRKPEIDTwSSDGEKINNMEGHIEFRNVHFRYPTRPeqPVLRGLNLSVKPG 1130
Cdd:PRK13657 292 vVAFINQVFMAAPKLE-------EFFEVEDAVPDVRD-PPGAIDLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1131 QYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGTIRDNILLGadRENVPEE 1210
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG--RPDATDE 439
|
410
....*....|....*....
gi 407923078 1211 AIIKACKDANIYDFIMSLP 1229
Cdd:PRK13657 440 EMRAAAERAQAHDFIERKP 458
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1078-1229 |
2.25e-31 |
|
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: 131.48 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1078 LFDRKPEI-DTWSSDGEKINnmEGHIEFRNVHFRYptRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNP 1156
Cdd:COG5265 335 LLDQPPEVaDAPDAPPLVVG--GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV 410
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407923078 1157 LTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGTIRDNILLGadRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:COG5265 411 TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG--RPDASEEEVEAAARAAQIHDFIESLP 481
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
812-1229 |
3.29e-31 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 130.52 E-value: 3.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 812 YGKlrSEANFWSLMYLML-ALTQLISFTG--QGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTE 888
Cdd:PRK11176 56 FGK--ADRSVLKWMPLVViGLMILRGITSfiSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDK--QSTGTLLSRITYD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 889 TTSLAGLSGATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLlacGFLRFWILARFEQRSKKAYEKSAsyacEAT 968
Cdd:PRK11176 132 SEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIV---SIAIRVVSKRFRNISKNMQNTMG----QVT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 969 SairTVASLTREEDVYASYHQQLV-----DQGAKNLRsilksstlyalsQSGMFLCTALGfwyggtlISKGEY----SLF 1039
Cdd:PRK11176 205 T---SAEQMLKGHKEVLIFGGQEVetkrfDKVSNRMR------------QQGMKMVSASS-------ISDPIIqliaSLA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1040 QFFVCFSAiTF----GAQSAGTI---FS------------------FAPDMgkakhAAIQ-LKTLFDRKPEIDTWSSDGE 1093
Cdd:PRK11176 263 LAFVLYAA-SFpsvmDTLTAGTItvvFSsmialmrplksltnvnaqFQRGM-----AACQtLFAILDLEQEKDEGKRVIE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1094 KINnmeGHIEFRNVHFRYPTRpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGkeissLNI 1173
Cdd:PRK11176 337 RAK---GDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG-----HDL 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 1174 NDY-----RSYIALVSQEPTLYQGTIRDNILLgADRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:PRK11176 408 RDYtlaslRNQVALVSQNVHLFNDTIANNIAY-ARTEQYSREQIEEAARMAYAMDFINKMD 467
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
437-670 |
3.73e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.97 E-value: 3.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 437 VKHI---YP--SRPEVTvmnGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQIS 511
Cdd:PRK13635 8 VEHIsfrYPdaATYALK---DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEP--VLFATTIFDNIKHGL--IGtqyehLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQR 587
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLenIG-----VPREEMVERVDQALRQVGMEDFLNREPHR-----------LSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 588 IAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALDRAAQGRTTIV-IAHRLSTIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGrREVLETVRQLKEQKGITVLsITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
....*
gi 407923078 666 ERKQA 670
Cdd:PRK13635 229 KSGHM 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
432-656 |
3.73e-31 |
|
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: 120.23 E-value: 3.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSrpeVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGvnvqelnlhwlrqqis 511
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 lvqqEPVLFATTIfDNIKHGLigtqyehlehekvrEMVYNaakmsnahdfvsalpegyetnvgergflLSGGQKQRIAIA 591
Cdd:cd03216 62 ----KEVSFASPR-DARRAGI--------------AMVYQ----------------------------LSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 592 RAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIV 656
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRlRAQGVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
432-667 |
3.86e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 124.07 E-value: 3.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQIS 511
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEP--VLFATTIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEgyetnvgergfLLSGGQKQRIA 589
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGL---ENKGIPHEEMKERVNEALELVGMQDFKEREPA-----------RLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKSE----GVVQAAldRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRleliKTIKGI--RDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELF 228
|
..
gi 407923078 666 ER 667
Cdd:PRK13650 229 SR 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
436-666 |
5.63e-31 |
|
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: 122.45 E-value: 5.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHwlRQQISLVQQ 515
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 516 EPVLFA-TTIFDNIKHGL-IGTQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQRIAIARA 593
Cdd:cd03296 82 HYALFRhMTVFDNVAFGLrVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQ-----------LSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 594 IVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQGTHNELLE 666
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1100-1229 |
1.13e-30 |
|
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: 121.06 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1100 GHIEFRNVHFRYptRPE-QPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRS 1178
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 407923078 1179 YIALVSQEPTLYQGTIRDNIllgaDRENV-PEEAIIKACKDANIYDFIMSLP 1229
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL----DPFGEySDEELWQALERVGLKEFVESLP 126
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
122-389 |
1.25e-30 |
|
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: 123.05 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 122 LMTVVFGSLSGTFQGMFQG----TMSNGEFNDELVKFVLYFVYLFIGEFftcyIATVGWIY----VGERISSRIREYYLS 193
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGrlidTIIKGGDLDVLNELALILLAIYLLQS----VFTFVRYYlfniAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 194 AILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLILCSTI--FAIVFTMGG 271
Cdd:cd18557 78 SLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIplLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 272 gsTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLVIAEYWGKKMKTVLASMLGAMMTIVYLNYG 351
Cdd:cd18557 158 --RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLL 235
|
250 260 270
....*....|....*....|....*....|....*...
gi 407923078 352 LAFWMGSRYLVKGEMSLSDVLTILLAVMIGAFSLGNIG 389
Cdd:cd18557 236 LVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLS 273
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
906-1206 |
1.88e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 128.40 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 906 VLTTLIGALV--LGIAIG-----WKLGLVCASTIPVLLACGFLRFWILARfeQRSKKAYEKSASYACEATSAIRTVASLT 978
Cdd:PRK11160 137 LISPLVAALVviLVLTIGlsffdLTLALTLGGILLLLLLLLPLLFYRLGK--KPGQDLTHLRAQYRVQLTEWLQGQAELT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 979 reedVYAS---YHQQLVDQGAKNLRSILKSSTLYALSQSGMFLCTALG----FWYGGTLISKGEYS-----LFQFFV--C 1044
Cdd:PRK11160 215 ----LFGAedrYRQQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTvvlmLWLAAGGVGGNAQPgaliaLFVFAAlaA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1045 FSAItfgaQSAGTIFSFapdMGKAKHAAIQLKTLFDRKPEIdTWSSDGEKINNmEGHIEFRNVHFRYPTRPeQPVLRGLN 1124
Cdd:PRK11160 291 FEAL----MPVAGAFQH---LGQVIASARRINEITEQKPEV-TFPTTSTAAAD-QVSLTLNNVSFTYPDQP-QPVLKGLS 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1125 LSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGTIRDNILLGADR 1204
Cdd:PRK11160 361 LQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPN 440
|
..
gi 407923078 1205 EN 1206
Cdd:PRK11160 441 AS 442
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
432-667 |
3.50e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 122.77 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSR-----PEVTV--MNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN-- 502
Cdd:PRK11308 6 LQAIDLKKHYPVKrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 503 -LHWLRQQISLVQQEPvlFAT-----TIFDNIKHGL-IGTQYEHLEH-EKVREMVynaAKmsnahdfVSALPEGYetnvG 574
Cdd:PRK11308 86 aQKLLRQKIQIVFQNP--YGSlnprkKVGQILEEPLlINTSLSAAERrEKALAMM---AK-------VGLRPEHY----D 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 575 ERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKsegvVQAA-----LDRAAQGRTTIV-IAHRLSTIK-TADKI 647
Cdd:PRK11308 150 RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS----VQAQvlnlmMDLQQELGLSYVfISHDLSVVEhIADEV 225
|
250 260
....*....|....*....|
gi 407923078 648 VVMSQGRIVEQGTHNELLER 667
Cdd:PRK11308 226 MVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
448-669 |
4.55e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 120.24 E-value: 4.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 448 TVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGG-----EVLLDG---VNVQELNLHWLRQQISLVQQEPVL 519
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTarsLSQQKGLIRQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 520 FA-TTIFDNIKHGLIGTQYEHLEH--EKVREMVynaAKMSNAhdfvsalpeGYETNVGERgflLSGGQKQRIAIARAIVS 596
Cdd:PRK11264 97 FPhRTVLENIIEGPVIVKGEPKEEatARARELL---AKVGLA---------GKETSYPRR---LSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 597 DPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVI-AHRLSTIK-TADKIVVMSQGRIVEQGTHNELLERKQ 669
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIvTHEMSFARdVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
454-659 |
8.02e-30 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 117.98 E-value: 8.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 454 DLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHwlRQQISLVQQEPVLFA-TTIFDNIKHGL 532
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 533 IGTQyeHLEHEKvREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQRIAIARAIVSDPKILLLDEATSALD- 611
Cdd:cd03298 96 SPGL--KLTAED-RQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDp 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 407923078 612 TKSEGVVQAALD-RAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQG 659
Cdd:cd03298 162 ALRAEMLDLVLDlHAETKMTVLMVTHQPEDAkRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
432-655 |
9.23e-30 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 117.89 E-value: 9.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPsrPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN---LHWLRQ 508
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 QISLVQQEPVLFAT-TIFDNIKHGLIGTQYEHLEHEKVREMVYNAAKMSNAHDfvsALPEGyetnvgergflLSGGQKQR 587
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHR---ALPAE-----------LSGGEQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 588 IAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTI--KTADKIVVMSQGRI 655
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvdTTRHRVIALERGKL 214
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
813-1050 |
1.47e-29 |
|
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: 119.96 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 813 GKLRSEANFWSLMYLMLALTQLISFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDqeENSAGALTSFLSTETTSL 892
Cdd:cd07346 32 AGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 893 AGLSGATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLlacgflrFWILARFEQRSKKAYEKS-------ASYAC 965
Cdd:cd07346 110 QNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLY-------VLILRYFRRRIRKASREVreslaelSAFLQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 966 EATSAIRTVASLTREEDVYASYHQQLVDQGAKNLRSILKSSTLYALSQSGMFLCTALGFWYGGTLISKGEYSLFQFFVCF 1045
Cdd:cd07346 183 ESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFL 262
|
....*
gi 407923078 1046 SAITF 1050
Cdd:cd07346 263 AYLGM 267
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
433-659 |
1.50e-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: 116.88 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 433 ELRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLV--ERFYDPVGGEVLLDGVNvqeLNLHWLRQQI 510
Cdd:cd03213 8 NLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRP---LDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 511 SLVQQEPVLFAT-TifdnikhgligtqyehlehekVREMVYNAAKMsnahdfvsalpegyetnvgeRGflLSGGQKQRIA 589
Cdd:cd03213 85 GYVPQDDILHPTlT---------------------VRETLMFAAKL--------------------RG--LSGGERKRVS 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ-GRTTIVIAHRLST--IKTADKIVVMSQGRIVEQG 659
Cdd:cd03213 122 IALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
432-667 |
2.33e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.89 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQV-KHIYPSrpevTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDG--VNVQELNLHWLRQ 508
Cdd:PRK09493 2 IEFKNVsKHFGPT----QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 QISLVQQEPVLFA-TTIFDNIKHGLI---GTQYEHLEhEKVREMVYNAAKMSNAHDFVSALpegyetnvgergfllSGGQ 584
Cdd:PRK09493 78 EAGMVFQQFYLFPhLTALENVMFGPLrvrGASKEEAE-KQARELLAKVGLAERAHHYPSEL---------------SGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 585 KQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALDRAAQGRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQGTHN 662
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQ 221
|
....*
gi 407923078 663 ELLER 667
Cdd:PRK09493 222 VLIKN 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
450-669 |
7.49e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.14 E-value: 7.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 450 MNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEP--VLFATTIFDN 527
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 528 IKhglIGTQYEHLEHEKVREMVYNAAKMSNAHDFVSALPegyetnvgergFLLSGGQKQRIAIARAIVSDPKILLLDEAT 607
Cdd:PRK13647 101 VA---FGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 608 SALDTKSEGVVQAALDR-AAQGRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQGThNELLERKQ 669
Cdd:PRK13647 167 AYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDED 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
447-660 |
7.77e-29 |
|
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: 116.00 E-value: 7.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 447 VTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWL-RQQISLVQQEPVLFAT-TI 524
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 525 FDNI--------KHGLIGTQYEHLEH---EKVREMVynaakmsnahDFVsALPEGYETNVGErgflLSGGQKQRIAIARA 593
Cdd:cd03219 93 LENVmvaaqartGSGLLLARARREERearERAEELL----------ERV-GLADLADRPAGE----LSYGQQRRLEIARA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 594 IVSDPKILLLDEATSAL-DTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKT-ADKIVVMSQGRIVEQGT 660
Cdd:cd03219 158 LATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
430-665 |
8.33e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 125.62 E-value: 8.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 430 GRVELRQVKHIYpsRPEVT-VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQ 508
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 QISLVQQEPVLFATTIFDNIKhgligtqyEHLEHEKVRemVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRI 588
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLD--------PFNEHNDAD--LWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLL 1383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 589 AIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1102-1229 |
9.90e-29 |
|
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: 115.66 E-value: 9.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYptRPEQP-VLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYI 1180
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 407923078 1181 ALVSQEPTLYQGTIRDNILLGadRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALA--DPGMSMERVIEAAKLAGAHDFISELP 125
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
780-1068 |
1.27e-28 |
|
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: 116.89 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 780 GLFWSIIAGGGNPTQAVFFAKSISALSRppseyGKLRSEANFWSLMYLMLALTQLISFTGQGLCFAICSEKLIHRVRDTA 859
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIK-----GGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 860 FRTMLRQDISFFDQeeNSAGALTSFLSTETTSLAGLSGATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLLACG 939
Cdd:cd18557 76 FSSLLRQEIAFFDK--HKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 940 flrfWILARF-EQRSKKAYE---KSASYACEATSAIRTVASLTREEDVYASYHQQLvdqgAKNLRSILKSSTLYALSQSG 1015
Cdd:cd18557 154 ----KIYGRYiRKLSKEVQDalaKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEAL----DRSYRLARKKALANALFQGI 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1016 M----FLCTALGFWYGGTLISKGEYS---LFQFFVCFSAITFgaqSAGTIFSFAPDMGKA 1068
Cdd:cd18557 226 TslliYLSLLLVLWYGGYLVLSGQLTvgeLTSFILYTIMVAS---SVGGLSSLLADIMKA 282
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
449-684 |
1.49e-28 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 124.89 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNI 528
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 529 KHGLIGTQYEhlehekvremVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVS-DPKILLLDEAT 607
Cdd:PTZ00243 1405 DPFLEASSAE----------VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEAT 1474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 608 SALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQA-YYNLVEA-QRIAAAN 684
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSiFHSMVEAlGRSEAKR 1553
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
433-659 |
1.67e-28 |
|
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: 114.55 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 433 ELRQVKHIYPSRPevtVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQELnlhwlRQ 508
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTllkaILGLLK----PTSGSIRVFGKPLEKE-----RK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 QISLV-QQEPVL--FATTIFDNIKHGLIGT-----QYEHLEHEKVREmvynaakmsnAHDFVSAlpegyeTNVGERGF-L 579
Cdd:cd03235 69 RIGYVpQRRSIDrdFPISVRDVVLMGLYGHkglfrRLSKADKAKVDE----------ALERVGL------SELADRQIgE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTIKT-ADKIVVMSqGRIVE 657
Cdd:cd03235 133 LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLN-RTVVA 211
|
..
gi 407923078 658 QG 659
Cdd:cd03235 212 SG 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
446-671 |
1.93e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 115.08 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 446 EVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVerfyDPVGGEVLLDGVNVQELNLHWL-RQQISLVQQEPVLF 520
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTllkaISGLL----PPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 521 AT-TIFDNIKHGLIgTQYEHLEHEKVREMVYNA----AKMSNAhdfvsalpegyetnvgeRGFLLSGGQKQRIAIARAIV 595
Cdd:COG0410 91 PSlTVEENLLLGAY-ARRDRAEVRADLERVYELfprlKERRRQ-----------------RAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 596 SDPKILLLDEAtsaldtkSEG----VVQ---AALDRAAQGRTTIVI----AHRLSTIktADKIVVMSQGRIVEQGTHNEL 664
Cdd:COG0410 153 SRPKLLLLDEP-------SLGlaplIVEeifEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAEL 223
|
250
....*....|
gi 407923078 665 L---ERKQAY 671
Cdd:COG0410 224 LadpEVREAY 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1100-1229 |
2.45e-28 |
|
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: 114.22 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1100 GHIEFRNVHFRYPTRpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSY 1179
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 407923078 1180 IALVSQEPTLYQGTIRDNILLGAdrENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHP 127
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
824-1229 |
4.05e-28 |
|
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: 120.54 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 824 LMYLMLALTQLISFtGQGLCFAICSEKLI-HrvrDTAFRTMLRQDISFFDQEENSAGALTSFLSTetTSLAGLSGATLGT 902
Cdd:TIGR02868 49 VLYLSVAAVAVRAF-GIGRAVFRYLERLVgH---DAALRSLGALRVRVYERLARQALAGRRRLRR--GDLLGRLGADVDA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 903 ----IFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLLACGFLRFWILARFEQRSKKAYEKS-----ASYACEATSAIRT 973
Cdd:TIGR02868 123 lqdlYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQAlarlrGELAAQLTDALDG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 974 VASLT---REEDVYASYhqqlVDQGAKNLRSILKSSTLYALSQSGMFL----CTALGFWYGGTLISKGEYS--------L 1038
Cdd:TIGR02868 203 AAELVasgALPAALAQV----EEADRELTRAERRAAAATALGAALTLLaaglAVLGALWAGGPAVADGRLApvtlavlvL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1039 FQF--FVCFSAITFGAQSagtifsfapdMGKAKHAAIQLKTLFDRKPEIDTWSSDGEKINNMEG-HIEFRNVHFRYPtrP 1115
Cdd:TIGR02868 279 LPLaaFEAFAALPAAAQQ----------LTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYP--G 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1116 EQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGTIR 1195
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVR 426
|
410 420 430
....*....|....*....|....*....|....
gi 407923078 1196 DNILLGadRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:TIGR02868 427 ENLRLA--RPDATDEELWAALERVGLADWLRALP 458
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
432-664 |
1.60e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.20 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSrpeVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN-LHWLRQQI 510
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 511 SLVQQEPVLFAT-TIFDNIkhgLIGtqyehleHEKVREMVYNAAKM-SNAHDFVSALpeGYETNVGERGFLLSGGQKQRI 588
Cdd:COG1129 82 AIIHQELNLVPNlSVAENI---FLG-------REPRRGGLIDWRAMrRRARELLARL--GLDIDPDTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 589 AIARAIVSDPKILLLDEATSALdTKSEgvVQAALDR----AAQGRTTIVIAHRLSTIKT-ADKIVVMSQGRIVEQGTHNE 663
Cdd:COG1129 150 EIARALSRDARVLILDEPTASL-TERE--VERLFRIirrlKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAE 226
|
.
gi 407923078 664 L 664
Cdd:COG1129 227 L 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
443-678 |
1.98e-27 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 113.01 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 443 SRPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPv 518
Cdd:COG4167 22 RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTlakmLAGIIE----PTSGEILINGHKLEYGDYKYRCKHIRMIFQDP- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 519 lfATTIFDNIKhglIGTQYE-------HLEHEKVREMVYNAAKMsnahdfVSALPEGYETNVgergFLLSGGQKQRIAIA 591
Cdd:COG4167 97 --NTSLNPRLN---IGQILEeplrlntDLTAEEREERIFATLRL------VGLLPEHANFYP----HMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 592 RAIVSDPKILLLDEATSALD--TKSEgVVQAALD-RAAQGRTTIVIAHRLSTIK-TADKIVVMSQGRIVEQGTHNELLER 667
Cdd:COG4167 162 RALILQPKIIIADEALAALDmsVRSQ-IINLMLElQEKLGISYIYVSQHLGIVKhISDKVLVMHQGEVVEYGKTAEVFAN 240
|
250
....*....|...
gi 407923078 668 KQAYY--NLVEAQ 678
Cdd:COG4167 241 PQHEVtkRLIESH 253
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1102-1229 |
3.95e-27 |
|
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: 117.39 E-value: 3.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeqPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIA 1181
Cdd:TIGR02857 322 LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIA 399
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 407923078 1182 LVSQEPTLYQGTIRDNILLGadRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLA--RPDASDAEIREALERAGLDEFVAALP 445
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
432-677 |
1.24e-26 |
|
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: 110.67 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPS------RPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN--- 502
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 503 LHWLRQQISLVQQE------PVLFATTIfdnikhglIGTQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGYETNvger 576
Cdd:TIGR02769 83 RRAFRRDVQLVFQDspsavnPRMTVRQI--------IGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 577 gflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALD--RAAQGRTTIVIAHRLSTI-KTADKIVVMSQG 653
Cdd:TIGR02769 151 ---LSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRklQQAFGTAYLFITHDLRLVqSFCQRVAVMDKG 227
|
250 260
....*....|....*....|....*
gi 407923078 654 RIVEQGTHNELLERKQ-AYYNLVEA 677
Cdd:TIGR02769 228 QIVEECDVAQLLSFKHpAGRNLQSA 252
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
432-659 |
1.88e-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: 108.43 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRpevTVMNGVDLVVEAGkTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQElNLHWLRQQIS 511
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPvlfatTIFDNIkhgligTQYEHLEH---------EKVREMVYNAAKMSNAHDFvsalpegYETNVGErgflLSG 582
Cdd:cd03264 76 YLPQEF-----GVYPNF------TVREFLDYiawlkgipsKEVKARVDEVLELVNLGDR-------AKKKIGS----LSG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 583 GQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIK-TADKIVVMSQGRIVEQG 659
Cdd:cd03264 134 GMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
104-388 |
1.92e-26 |
|
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: 110.80 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 104 IIIVVSSICAIAagavLPLMtvvFGSL--SGTFQGMFQGTMSNGEFNDELVKFVLYFVylfIGEFFTcyiATVGWIY--V 179
Cdd:cd18780 3 IALLVSSGTNLA----LPYF---FGQVidAVTNHSGSGGEEALRALNQAVLILLGVVL---IGSIAT---FLRSWLFtlA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 180 GERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLILC 259
Cdd:cd18780 70 GERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVML 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 260 STIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLVIAEYWGKKMKTVLASML 339
Cdd:cd18780 150 SVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFN 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 407923078 340 GAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVLTILLAVMIGAFSLGNI 388
Cdd:cd18780 230 GFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFL 278
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
441-1198 |
2.50e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 117.57 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 441 YPSRPEVTVMNgVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVlldgvnvqelnlhWLRQQISLVQQEPVLF 520
Cdd:PTZ00243 668 FELEPKVLLRD-VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 521 ATTIFDNIkhgLIGTqyehlehEKVREMVYNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKI 600
Cdd:PTZ00243 734 NATVRGNI---LFFD-------EEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDV 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 601 LLLDEATSALDTK-SEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERkqayyNLVEAQR 679
Cdd:PTZ00243 804 YLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT-----SLYATLA 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 680 IAAANEKIEEEEEEEEEVDLTEVDDE--TIKRTVSPQSEKRSYSVDP--DDDVAARLKrTQSGKSESSVALAKKQPASEQ 755
Cdd:PTZ00243 879 AELKENKDSKEGDADAEVAEVDAAPGgaVDHEPPVAKQEGNAEGGDGaaLDAAAGRLM-TREEKASGSVPWSTYVAYLRF 957
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 756 KYSLATLIKLIASFNRQEWLLMVQGLFWSIIAGggnptqavffaksisalsrppseyGKLRSEANFWSLMYLMLALTQLI 835
Cdd:PTZ00243 958 CGGLHAAGFVLATFAVTELVTVSSGVWLSMWST------------------------RSFKLSAATYLYVYLGIVLLGTF 1013
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 836 SFTgqgLCFAICSEKLIHRVRdTAFRTMLRQ----DISFFDQeeNSAGALTSFLSTETTSL-AGLSGATLgTIFTVLTTL 910
Cdd:PTZ00243 1014 SVP---LRFFLSYEAMRRGSR-NMHRDLLRSvsrgTMSFFDT--TPLGRILNRFSRDIDILdNTLPMSYL-YLLQCLFSI 1086
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 911 IGALvlgiaigwklgLVCASTIP-VLLA---CGFLRFWIL-----ARFEQRSKKAYEKSA--SYACEATSAIRTVAS--- 976
Cdd:PTZ00243 1087 CSSI-----------LVTSASQPfVLVAlvpCGYLYYRLMqfynsANREIRRIKSVAKSPvfTLLEEALQGSATITAygk 1155
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 977 --------LTREEDVYASYHQQLVDQGAKNLRSILKSSTLYALsqsgMFLCTALGFWYGGTLISKGEYSLfqffvcfsAI 1048
Cdd:PTZ00243 1156 ahlvmqeaLRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTV----IALIGVIGTMLRATSQEIGLVSL--------SL 1223
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1049 TFGAQSAGT-------IFSFAPDMGKA-----------KHAAIQLKTLFDRKPEIDTWSSDGEKINNME----------- 1099
Cdd:PTZ00243 1224 TMAMQTTATlnwlvrqVATVEADMNSVerllyytdevpHEDMPELDEEVDALERRTGMAADVTGTVVIEpasptsaaphp 1303
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1100 ---GHIEFRNVHFRYptRPEQP-VLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIND 1175
Cdd:PTZ00243 1304 vqaGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE 1381
|
810 820
....*....|....*....|...
gi 407923078 1176 YRSYIALVSQEPTLYQGTIRDNI 1198
Cdd:PTZ00243 1382 LRRQFSMIPQDPVLFDGTVRQNV 1404
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
424-672 |
3.21e-26 |
|
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: 114.78 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 424 RLENLqgRVELRQVKHiypsrpEVTVMNGVDLVVEAGKTTALVGASGSGKS----TIVGLVERFYDPVGGEVLLDGVNVQ 499
Cdd:COG4172 8 SVEDL--SVAFGQGGG------TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 500 ELNLHWLRQ----QISLVQQEPV-----LFAttifdnikhglIGTQ-YEHLE-HEKVREmvyNAAK-----------MSN 557
Cdd:COG4172 80 GLSERELRRirgnRIAMIFQEPMtslnpLHT-----------IGKQiAEVLRlHRGLSG---AAARaralellervgIPD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 558 AHDFVSALPegyetnvgergFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTksegVVQAA-LD-----RAAQGRTT 631
Cdd:COG4172 146 PERRLDAYP-----------HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQAQiLDllkdlQRELGMAL 210
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 407923078 632 IVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNELLERKQAYY 672
Cdd:COG4172 211 LLITHDLGVVrRFADRVAVMRQGEIVEQGPTAELFAAPQHPY 252
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
432-669 |
4.19e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.55 E-value: 4.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEVtvMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDG--VNVQELNLHWLRQQ 509
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEP--VLFATTIFDNIKHGLIGTQyehLEHEKVREMVYNAAKMSnahdfvsalpeGYETNVGERGFLLSGGQKQR 587
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLK---LPEDEVRKRVDNALKRT-----------GIEHLKDKPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 588 IAIARAIVSDPKILLLDEATSALDTK--SEgVVQAALDRAAQGRTTIVIA-HRLSTIKT-ADKIVVMSQGRIVEQGTHNE 663
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMgvSE-IMKLLVEMQKELGLTIIIAtHDIDIVPLyCDNVFVMKEGRVILQGNPKE 228
|
....*.
gi 407923078 664 LLERKQ 669
Cdd:PRK13636 229 VFAEKE 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
446-664 |
4.21e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 110.71 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 446 EVTVMNGVDLVVEAGKTTALVGASGSGKSTIV----GL---------VERFY--DPVGGEVLLDGVNVQEL-NLHWLRQQ 509
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVthfnGLikskygtiqVGDIYigDKKNNHELITNPYSKKIkNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEP--VLFATTIFDNIKHGLIGTQYEHLE-HEKVRemvYNAAKMSNAHDFVSALPegyetnvgergFLLSGGQKQ 586
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEaKKLAK---FYLNKMGLDDSYLERSP-----------FGLSGGQKR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 587 RIAIARAIVSDPKILLLDEATSALDTKSEG-VVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNEL 664
Cdd:PRK13631 184 RVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
436-667 |
7.40e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.94 E-value: 7.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQelnlHWLRQQIS---- 511
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA----DWSPAELArrra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 -LVQQEPVLFATTIFDNIKHGLIGTQyehLEHEKVREMVynAAKMSNAHdfVSALpegyetnvGERGFL-LSGGQKQRIA 589
Cdd:PRK13548 80 vLPQHSSLSFPFTVEEVVAMGRAPHG---LSRAEDDALV--AAALAQVD--LAHL--------AGRDYPqLSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 590 IARAIV------SDPKILLLDEATSALDTK-SEGVVQAALDRA-AQGRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQGT 660
Cdd:PRK13548 145 LARVLAqlwepdGPPRWLLLDEPTSALDLAhQHHVLRLARQLAhERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
250
....*....|..
gi 407923078 661 -----HNELLER 667
Cdd:PRK13548 225 paevlTPETLRR 236
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
436-649 |
9.40e-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: 106.02 E-value: 9.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQELNLHWlRQQIS 511
Cdd:COG4133 4 EAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFAT-TIFDNIK-----HGLIGTQY-----------EHLEHEKVREmvynaakmsnahdfvsalpegyetnvg 574
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGLRADREaidealeavglAGLADLPVRQ--------------------------- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 575 ergflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIA-HRLSTIKTADKIVV 649
Cdd:COG4133 132 -----LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
432-659 |
1.26e-25 |
|
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: 105.76 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRpevTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQelNLHWLRQQIS 511
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFAT-TIFDNIKHGLIGTQYEHLEHEKVREMVynaaKMSN-AHDFVsalpegyetnvgeRGFllSGGQKQRIA 589
Cdd:cd03268 76 ALIEAPGFYPNlTARENLRLLARLLGIRKKRIDEVLDVV----GLKDsAKKKV-------------KGF--SLGMKQRLG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 590 IARAIVSDPKILLLDEATSALDTksEGVV---QAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQG 659
Cdd:cd03268 137 IALALLGNPDLLILDEPTNGLDP--DGIKelrELILSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
436-656 |
1.48e-25 |
|
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: 105.80 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVT-VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNvqeLNLHWLRQQISLVQ 514
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 515 QEP--VLFATTIFDNIkhgLIGTQYEHLEHEKVREMVynaaKMSNAHDFVSALPegyetnvgergFLLSGGQKQRIAIAR 592
Cdd:cd03226 78 QDVdyQLFTDSVREEL---LLGLKELDAGNEQAETVL----KDLDLYALKERHP-----------LSLSGGQKQRLAIAA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 593 AIVSDPKILLLDEATSALDTKS-EGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIV 656
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
429-667 |
2.04e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.54 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 429 QGRVELRQVKHIYPSrpeVTVMNGVDLVVEAGKTTALVGASGSGKSTIVG----LVERFYDP-VGGEVLLDGVNVQELNL 503
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEArVSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 504 HWLRQQISLVQQEPVLFAT-TIFDNIKHGL----IGTQYEHLEhEKVREMVYNAAKMSNAHDFVSAlPEGYetnvgergf 578
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNlSIFENVALGLklnrLVKSKKELQ-ERVRWALEKAQLWDEVKDRLDA-PAGK--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 579 lLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAH-RLSTIKTADKIVVMSQGRIVE 657
Cdd:PRK14247 147 -LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVE 225
|
250
....*....|
gi 407923078 658 QGTHNELLER 667
Cdd:PRK14247 226 WGPTREVFTN 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
432-667 |
2.11e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.58 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEvTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDP---VGGEVLLDGVNVQELNLHWLRQ 508
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 QISLVQQEP--VLFATTIFDNIKHGLIGTQYEHLEHEKVREMVYNAAKMSnahDFVSALPEGyetnvgergflLSGGQKQ 586
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGML---DYIDSEPAN-----------LSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 587 RIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALD-RAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNEL 664
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGkEQILKLIRKlKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
...
gi 407923078 665 LER 667
Cdd:PRK13640 231 FSK 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
432-670 |
3.26e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 106.76 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEVTvMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQIS 511
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEP---VLFATTIFDnIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQRI 588
Cdd:PRK13648 87 IVFQNPdnqFVGSIVKYD-VAFGL---ENHAVPYDEMHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 589 AIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGR--TTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLE 666
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
....
gi 407923078 667 RKQA 670
Cdd:PRK13648 232 HAEE 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
432-665 |
4.56e-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: 105.55 E-value: 4.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRpevTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVL------LDGVNVQElnlhw 505
Cdd:COG1119 4 LELRNVTVRRGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 506 LRQQISLV---QQEPVLFATTIFDNIKHGLIGT-----QYEHLEHEKVREMvynaakmsnAHDF-VSALpegyetnvGER 576
Cdd:COG1119 76 LRKRIGLVspaLQLRFPRDETVLDVVLSGFFDSiglyrEPTDEQRERAREL---------LELLgLAHL--------ADR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 577 GFL-LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIV-IAHRLSTI-KTADKIVVMSQ 652
Cdd:COG1119 139 PFGtLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIpPGITHVLLLKD 218
|
250
....*....|...
gi 407923078 653 GRIVEQGTHNELL 665
Cdd:COG1119 219 GRVVAAGPKEEVL 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
432-657 |
5.40e-25 |
|
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: 104.82 E-value: 5.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRP-EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLV---ERfydPVGGEVLLDGVNVQELN----L 503
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDLFALDedarA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 504 HWLRQQISLVQQEPVLFAT-TIFDNIkhGLigtqyeHLEhekvremvynAAKMSNAHDFVSALPEgyETNVGERgfL--- 579
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTlTALENV--ML------PLE----------LAGRRDARARARALLE--RVGLGHR--Ldhy 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 ---LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALD--RAAQGRTTIVIAHRLSTIKTADKIVVMSQGR 654
Cdd:COG4181 144 paqLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGR 223
|
...
gi 407923078 655 IVE 657
Cdd:COG4181 224 LVE 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
455-665 |
5.75e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 108.97 E-value: 5.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 455 LVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQ----QISLVQQEPVLFA-TTIFDNIK 529
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 530 HGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQRIAIARAIVSDPKILLLDEATSA 609
Cdd:PRK10070 129 FGM---ELAGINAEERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 610 LDTKSEGVVQAALDR--AAQGRTTIVIAHRL-STIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK10070 195 LDPLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
447-660 |
8.03e-25 |
|
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: 105.12 E-value: 8.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 447 VTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWL-RQQISLVQQEPVLFAT-TI 524
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPElTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 525 FDNIK------------HGLIGTQYEHLEHEKVREMVYNAAKMSN----AHDFVSALPegyetnvgergfllsGGQKQRI 588
Cdd:COG0411 97 LENVLvaaharlgrgllAALLRLPRARREEREARERAEELLERVGladrADEPAGNLS---------------YGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 589 AIARAIVSDPKILLLDEATSALDTK-SEGVVQAALD-RAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGT 660
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEeTEELAELIRRlRDERGITILLIEHDMDLVmGLADRIVVLDFGRVIAEGT 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
432-664 |
8.42e-25 |
|
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: 103.74 E-value: 8.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEVTVmNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQElNLHWLRQQIS 511
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQepvlfattiFDNIKHGLigTQYEHLEhekvremVYNAAKMSNAHDfVSALPEGYETNVGERGFL------LSGGQK 585
Cdd:cd03263 79 YCPQ---------FDALFDEL--TVREHLR-------FYARLKGLPKSE-IKEEVELLLRVLGLTDKAnkrartLSGGMK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 586 QRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAH------RLstiktADKIVVMSQGRIVEQG 659
Cdd:cd03263 140 RKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeaeAL-----CDRIAIMSDGKLRCIG 214
|
....*
gi 407923078 660 THNEL 664
Cdd:cd03263 215 SPQEL 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1102-1198 |
8.73e-25 |
|
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: 102.39 E-value: 8.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNiNDYRSYIA 1181
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90
....*....|....*..
gi 407923078 1182 LVSQEPTLYQGTIRDNI 1198
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL 95
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
433-651 |
1.02e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.03 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 433 ELRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISL 512
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 513 VQQEPVLFATTIFDNIKHgligtQYEhLEHEKVREMVYNAAKMSnahdFvsALPEG-YETNVGErgflLSGGQKQRIAIA 591
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIF-----PWQ-IRNQQPDPAIFLDDLER----F--ALPDTiLTKNIAE----LSGGEKQRISLI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 592 RAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVI--AHRLSTIKTADKIVVMS 651
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVITLQ 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
432-664 |
1.35e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.77 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEVtvMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDG--VNVQELNLHWLRQQ 509
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEP--VLFATTIFDNIKHGLIGTQyehLEHEKVREMVYNAAKMsnahdfVSAlpEGYETNVGERgflLSGGQKQR 587
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLG---LSKEEVEKRVKEALKA------VGM--EGFENKPPHH---LSGGQKKR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 588 IAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-DRAAQGRTTIVIAHRLSTIKT-ADKIVVMSQGRIVEQGTHNEL 664
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
453-659 |
1.64e-24 |
|
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: 102.76 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 453 VDLVVEAGkTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGV----NVQELNLHWLRQQISLVQQEPVLFA-TTIFDN 527
Cdd:cd03297 17 IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFPhLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 528 IKHGLIGtqyehlehEKVREMVYNAAKMSNAHDFvsalpegyeTNVGERGFL-LSGGQKQRIAIARAIVSDPKILLLDEA 606
Cdd:cd03297 96 LAFGLKR--------KRNREDRISVDELLDLLGL---------DHLLNRYPAqLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 607 TSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTIKT-ADKIVVMSQGRIVEQG 659
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
816-1037 |
1.75e-24 |
|
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: 104.93 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 816 RSEANFWS--LMYLMLALTQLIsFTG-QGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTETTSL 892
Cdd:cd18572 30 GSREAFYRavLLLLLLSVLSGL-FSGlRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDA--TKTGELTSRLTSDCQKV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 893 AGLSGATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLlacgFLRFWILARFEQR-SKKAYE---KSASYACEAT 968
Cdd:cd18572 107 SDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVI----ALITKVYGRYYRKlSKEIQDalaEANQVAEEAL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 969 SAIRTVASLTREEDVYASYHQQLVDQGAKNLRSILKSSTLYALSQSGMFLCTALGFWYGGTLISKGEYS 1037
Cdd:cd18572 183 SNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMS 251
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
432-669 |
2.79e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.48 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIY-PSRP-EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNV----QELNLHW 505
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 506 LRQQISLVQQ--EPVLFATTIFDNIkhgLIGTQYEHLEHEKVREmvynaakmsNAHDFVSALpeGYETNVGERG-FLLSG 582
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREI---IFGPKNFKMNLDEVKN---------YAHRLLMDL--GFSRDVMSQSpFQMSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 583 GQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQG 659
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQT 228
|
250
....*....|
gi 407923078 660 THNELLERKQ 669
Cdd:PRK13646 229 SPKELFKDKK 238
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
446-664 |
3.35e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.01 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 446 EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHW-LRQQISLVQQEP--VLFAT 522
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNPdnQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 523 TIFDNIKHGLigtqyEHL--EHEKVREMVYNAAKMSNAHDFVSALPEgyetnvgergfLLSGGQKQRIAIARAIVSDPKI 600
Cdd:PRK13633 102 IVEEDVAFGP-----ENLgiPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 601 LLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNEL 664
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
450-664 |
3.49e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.93 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 450 MNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYD-----PVGGEVLLDGVNVQELNLHW--LRQQISLVQQEPVLFAT 522
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 523 TIFDNIKHGL--IGTQYEHLEHEKVREMVYNAAKMSNAHDFVsalpegYETNVGergflLSGGQKQRIAIARAIVSDPKI 600
Cdd:PRK14239 101 SIYENVVYGLrlKGIKDKQVLDEAVEKSLKGASIWDEVKDRL------HDSALG-----LSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 601 LLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNEL 664
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
448-668 |
4.55e-24 |
|
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: 102.22 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 448 TVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVerfyDPVGGEVLLDGVNVQELNLHWL-RQQISLVQQEPVLFAT 522
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTllktLMGLL----PVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 523 -TIFDNIKHGLIGTQYEHlehEKVREMVYnaakmsnahDFVSALPEgyetNVGERGFLLSGGQKQRIAIARAIVSDPKIL 601
Cdd:TIGR03410 90 lTVEENLLTGLAALPRRS---RKIPDEIY---------ELFPVLKE----MLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 602 LLDEATsaldtksEGV-------VQAALDR-AAQGRTTIV-IAHRLS-TIKTADKIVVMSQGRIVEQGTHNELLERK 668
Cdd:TIGR03410 154 LLDEPT-------EGIqpsiikdIGRVIRRlRAEGGMAILlVEQYLDfARELADRYYVMERGRVVASGAGDELDEDK 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1102-1207 |
5.20e-24 |
|
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: 99.98 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIA 1181
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100
....*....|....*....|....*.
gi 407923078 1182 LVSQEPTLYQGTIRDNILLGADRENV 1207
Cdd:cd03246 80 YLPQDDELFSGSIAENILSGGQRQRL 105
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
104-380 |
5.33e-24 |
|
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: 103.78 E-value: 5.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 104 IIIVVSSICAIAAGAVLPLMT---VVFGSLSGTFQGmfqgtmsngefndeLVKFVLYFVYLFIGEFFTCYIATVGWIYVG 180
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTkllIDDVIPAGDLSL--------------LLWIALLLLLLALLRALLSYLRRYLAARLG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 181 ERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLILCS 260
Cdd:cd07346 68 QRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 261 TIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHlvIAEYWGKKMKTVL--ASM 338
Cdd:cd07346 148 LLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREA--NRDLRDANLRAARlsALF 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 407923078 339 LGAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVLTILLAVMI 380
Cdd:cd07346 226 SPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGM 267
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
453-668 |
6.54e-24 |
|
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: 104.81 E-value: 6.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 453 VDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQE------LNLHwlRQQISLVQQEPVLFA-TTIF 525
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPE--KRRIGYVFQEARLFPhLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 526 DNIKHGLIGT--QYEHLEHEKVREMVynaakmsnahdfvsalpeGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLL 603
Cdd:TIGR02142 94 GNLRYGMKRArpSERRISFERVIELL------------------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 604 DEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNELLERK 668
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
451-672 |
7.15e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 104.40 E-value: 7.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 451 NGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQELN---LHWLRQQISLVQQEPVlfAT- 522
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTfaraIIGLVK----ATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDPL--ASl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 523 ----TIFDNIKHGLIgTQYEHLEHEKVREMVynAAKMSNahdfVSALPegyetNVGER---GFllSGGQKQRIAIARAIV 595
Cdd:PRK15079 112 nprmTIGEIIAEPLR-TYHPKLSRQEVKDRV--KAMMLK----VGLLP-----NLINRyphEF--SGGQCQRIGIARALI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 596 SDPKILLLDEATSALDTKsegvVQAA---LDRAAQ---GRTTIVIAHRLSTIK-TADKIVVMSQGRIVEQGTHNELLERK 668
Cdd:PRK15079 178 LEPKLIICDEPVSALDVS----IQAQvvnLLQQLQremGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEVYHNP 253
|
....
gi 407923078 669 QAYY 672
Cdd:PRK15079 254 LHPY 257
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
454-665 |
7.87e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.58 E-value: 7.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 454 DLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNvqelnlHWL----RQQISLVQQEPVLFA-TTIFDNI 528
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtppsRRPVSMLFQENNLFShLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 529 KHGL-IGTQYEHLEHEKVREMvynAAKMSnAHDFVSALPegyetnvGErgflLSGGQKQRIAIARAIVSDPKILLLDEAT 607
Cdd:PRK10771 93 GLGLnPGLKLNAAQREKLHAI---ARQMG-IEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 608 SALDTKSEGVVQAALDRAAQGR--TTIVIAHRLS-TIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
453-667 |
9.80e-24 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 104.41 E-value: 9.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 453 VDLVVEAGKTTALVGASGSGKSTIVGLV---ERfydP------VGGEVLLDGVNVQELNLHwlRQQISLVQQEPVLFAT- 522
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PdsgrirLGGEVLQDSARGIFLPPH--RRRIGYVFQEARLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 523 TIFDNIKHGL--IGTQYEHLEHEKVREMVynaakmsnahdfvsalpeGYETNVGERGFLLSGGQKQRIAIARAIVSDPKI 600
Cdd:COG4148 93 SVRGNLLYGRkrAPRAERRISFDEVVELL------------------GIGHLLDRRPATLSGGERQRVAIGRALLSSPRL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 601 LLLDEATSALD--TKSEgvVQAALDR-AAQGRTTIV-IAH------RLstiktADKIVVMSQGRIVEQGTHNELLER 667
Cdd:COG4148 155 LLMDEPLAALDlaRKAE--ILPYLERlRDELDIPILyVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
432-665 |
1.51e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 101.31 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPevtVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQIS 511
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLfattifdNIKhgligtqyehLeheKVREMV------YN--------AAKMSNAHDFVSaLpegyeTNVGERg 577
Cdd:COG4604 79 ILRQENHI-------NSR----------L---TVRELVafgrfpYSkgrltaedREIIDEAIAYLD-L-----EDLADR- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 578 FL--LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSegVVQ--AALDRAA--QGRTTIVIAHRLS-TIKTADKIVVM 650
Cdd:COG4604 132 YLdeLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKH--SVQmmKLLRRLAdeLGKTVVIVLHDINfASCYADHIVAM 209
|
250
....*....|....*
gi 407923078 651 SQGRIVEQGTHNELL 665
Cdd:COG4604 210 KDGRVVAQGTPEEII 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
427-669 |
1.68e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 102.01 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 427 NLQGRVELRQVKHIYPSRP--EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDG----VNVQE 500
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 501 LN-LHWLRQQISLVQQEP--VLFATTIFDNIKHGLIgtqyeHLEHEKvrEMVYNaaKMSNAHDFVSaLPEGYetnVGERG 577
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPV-----NLGENK--QEAYK--KVPELLKLVQ-LPEDY---VKRSP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 578 FLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAHRLSTI-KTADKIVVMSQGR 654
Cdd:PRK13645 149 FELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGK 228
|
250
....*....|....*
gi 407923078 655 IVEQGTHNELLERKQ 669
Cdd:PRK13645 229 VISIGSPFEIFSNQE 243
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
441-650 |
1.83e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.23 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 441 YPSRPevtVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGvnvqELNLHWLRQQISLVQQEPVlf 520
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 521 atTIFDNIKHGLIGTQYEHLEHEKVREMVYNAAKMSnahdfvsalpegyetnVGERGFL------LSGGQKQRIAIARAI 594
Cdd:NF040873 73 --TVRDLVAMGRWARRGLWRRLTRDDRAAVDDALER----------------VGLADLAgrqlgeLSGGQRQRALLAQGL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 595 VSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTIKTADKIVVM 650
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
436-662 |
1.88e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDG------VNVQELNLHWLRQQ 509
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQepvlfattifdnikhgligtQYEHLEHEKVREMVYNA----AKMSNAH---------------DFVSALPegye 570
Cdd:COG4161 84 VGMVFQ--------------------QYNLWPHLTVMENLIEApckvLGLSKEQarekamkllarlrltDKADRFP---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 571 tnvgergFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIV 648
Cdd:COG4161 140 -------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVV 212
|
250
....*....|....
gi 407923078 649 VMSQGRIVEQGTHN 662
Cdd:COG4161 213 YMEKGRIIEQGDAS 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
432-667 |
2.17e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.42 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYpsRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQIS 511
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEP--VLFATTIFDNIKHGLIGTQyehLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQRIA 589
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLG---LDEETVAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNELLE 666
Cdd:PRK13652 148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFL 227
|
.
gi 407923078 667 R 667
Cdd:PRK13652 228 Q 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1103-1219 |
2.97e-23 |
|
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: 99.08 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1103 EFRNVHFRYPTRpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIAL 1182
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 407923078 1183 VSQEPT--LYQGTIRDNILLGADRENVPEEAIIKACKDA 1219
Cdd:cd03225 80 VFQNPDdqFFGPTVEEEVAFGLENLGLPEEEIEERVEEA 118
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
432-665 |
3.07e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.94 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQIS 511
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEP--VLFATTIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEgyetnvgergfLLSGGQKQRIA 589
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGM---ENQGIPREEMIKRVDEALLAVNMLDFKTREPA-----------RLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGR--TTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
434-666 |
4.52e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 100.25 E-value: 4.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 434 LRQVKHIYPSRpevTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQIS-L 512
Cdd:PRK10575 14 LRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 513 VQQEPVLFATTIFDNIK------HGLIGtQYEHLEHEKVREMVYNAAKMSNAHDFVSALpegyetnvgergfllSGGQKQ 586
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAigrypwHGALG-RFGAADREKVEEAISLVGLKPLAHRLVDSL---------------SGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 587 RIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAhRLSTIKTA----DKIVVMSQGRIVEQGTHN 662
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPA 233
|
....
gi 407923078 663 ELLE 666
Cdd:PRK10575 234 ELMR 237
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
446-656 |
5.08e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.16 E-value: 5.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 446 EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVL---FAT 522
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 523 TIFDNI--------KHGL-IGTQYEHLEHekVREMVynaakmsnahdfvSALPEGYE----TNVGergfLLSGGQKQRIA 589
Cdd:COG1101 98 TIEENLalayrrgkRRGLrRGLTKKRREL--FRELL-------------ATLGLGLEnrldTKVG----LLSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAHRLS-TIKTADKIVVMSQGRIV 656
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
432-667 |
5.69e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.11 E-value: 5.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELrqvKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLhwlrQQ-- 509
Cdd:PRK11432 7 VVL---KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI----QQrd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEPVLFA-TTIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAhdfvsalpEGYETNVGERgflLSGGQKQRI 588
Cdd:PRK11432 80 ICMVFQSYALFPhMSLGENVGYGL---KMLGVPKEERKQRVKEALELVDL--------AGFEDRYVDQ---ISGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 589 AIARAIVSDPKILLLDEATSALDtksegvvqAALDRAAQ----------GRTTIVIAHRLS-TIKTADKIVVMSQGRIVE 657
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLD--------ANLRRSMRekirelqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQ 217
|
250
....*....|
gi 407923078 658 QGTHNELLER 667
Cdd:PRK11432 218 IGSPQELYRQ 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
446-654 |
5.86e-23 |
|
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: 98.66 E-value: 5.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 446 EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLD----GVNVQELN----LHWLRQQISLVQQep 517
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreiLALRRRTIGYVSQ-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 518 vlFATTI-----FDNIKHGLIGTQYEHLE-HEKVREMVynaakmsnahdfvSALpegyetNVGERGFLL-----SGGQKQ 586
Cdd:COG4778 101 --FLRVIprvsaLDVVAEPLLERGVDREEaRARARELL-------------ARL------NLPERLWDLppatfSGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 587 RIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRA-AQGRTTIVIAHRLSTIKT-ADKIVVMSQGR 654
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
449-665 |
7.39e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 99.73 E-value: 7.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYD-----PVGGEVLLDGVNVQE--LNLHWLRQQISLVQQEPVLFA 521
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYErrVNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 522 TTIFDNIKHG--LIGTqyehleHEKVR--EMVYNAAKMSNAHDFVsalpegyETNVGERGFLLSGGQKQRIAIARAIVSD 597
Cdd:PRK14258 102 MSVYDNVAYGvkIVGW------RPKLEidDIVESALKDADLWDEI-------KHKIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 598 PKILLLDEATSALD----TKSEGVVQAALDRAAQgrTTIVIAHRLSTIKTADKIVVMSQG------RIVEQGTHNELL 665
Cdd:PRK14258 169 PKVLLMDEPCFGLDpiasMKVESLIQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFKGnenrigQLVEFGLTKKIF 244
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
405-684 |
9.89e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.84 E-value: 9.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 405 MYSTIDRvspldPTSKEGRRLENLqgrVELRQVKHIYPSRPEVtvmNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFY 484
Cdd:PRK11607 1 MNDAIPR-----PQAKTRKALTPL---LEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 485 DPVGGEVLLDGVNVQELNLHwlRQQISLVQQEPVLFA-TTIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVS 563
Cdd:PRK11607 70 QPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPhMTVEQNIAFGL---KQDKLPKAEIASRVNEMLGLVHMQEFAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 564 ALPEGyetnvgergflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAA----LDRAaqGRTTIVIAHRLS 639
Cdd:PRK11607 145 RKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEvvdiLERV--GVTCVMVTHDQE 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 407923078 640 TIKT-ADKIVVMSQGRIVEQGTHNELLERKQAYYNlveAQRIAAAN 684
Cdd:PRK11607 212 EAMTmAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS---AEFIGSVN 254
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1088-1206 |
1.18e-22 |
|
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: 97.48 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1088 WSSDGEkinnmeghIEFRNVHFRYptRPEQP-VLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGK 1166
Cdd:cd03369 1 WPEHGE--------IEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI 70
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 407923078 1167 EISSLNINDYRSYIALVSQEPTLYQGTIRDNIllgaDREN 1206
Cdd:cd03369 71 DISTIPLEDLRSSLTIIPQDPTLFSGTIRSNL----DPFD 106
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1096-1211 |
1.51e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 98.62 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1096 NNMEGHIEFRNVHFRYPTRP-EQPVLRGLNLSVKPGQYVALVGASGCGKST---TIALLERfynPLTGGIYADGKEISSL 1171
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTllrLIAGLEK---PTSGEVLVDGKPVTGP 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 407923078 1172 NINdyrsyIALVSQEPTLYQ-GTIRDNILLGADRENVPEEA 1211
Cdd:COG1116 79 GPD-----RGVVFQEPALLPwLTVLDNVALGLELRGVPKAE 114
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
432-666 |
1.59e-22 |
|
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: 97.61 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRpevTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQELNLHW-L 506
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGKILLDGQDITKLPMHKrA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 507 RQQISLVQQEPVLFAT-TIFDNIKHGLIGTQYEHLE-HEKVREMVynaakmsnaHDFvsalpeGYETNVGERGFLLSGGQ 584
Cdd:cd03218 74 RLGIGYLPQEASIFRKlTVEENILAVLEIRGLSKKErEEKLEELL---------EEF------HITHLRKSKASSLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 585 KQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIA-HRLS-TIKTADKIVVMSQGRIVEQGTHN 662
Cdd:cd03218 139 RRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPE 218
|
....
gi 407923078 663 ELLE 666
Cdd:cd03218 219 EIAA 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
444-659 |
1.72e-22 |
|
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: 97.34 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 444 RPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVERFYDpVGGEVLLDGvnvQELNLHWLRQQISLVQQepvl 519
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNG---QPRKPDQFQKCVAYVRQ---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 520 fattiFDNIKHGLigTQYEHLEH-----------EKVREMVYNAAKMSNAHDfvsalpegyeTNVGERGFL-LSGGQKQR 587
Cdd:cd03234 89 -----DDILLPGL--TVRETLTYtailrlprkssDAIRKKRVEDVLLRDLAL----------TRIGGNLVKgISGGERRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 588 IAIARAIVSDPKILLLDEATSALDTKSE-GVVQAALDRAAQGRTTIVIAH--RLSTIKTADKIVVMSQGRIVEQG 659
Cdd:cd03234 152 VSIAVQLLWDPKVLILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
449-664 |
1.79e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.54 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELnlHWLRQQISLVQQEPVLFA-TTIFDN 527
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKVGFVFQHYALFRhMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 528 IKHGL-IGTQYEHLEHEKVREMVYNAAKMSNahdfVSALPEGYETNvgergflLSGGQKQRIAIARAIVSDPKILLLDEA 606
Cdd:PRK10851 95 IAFGLtVLPRRERPNAAAIKAKVTQLLEMVQ----LAHLADRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 607 TSALDTKsegvVQAALDRAAQGR------TTIVIAH-RLSTIKTADKIVVMSQGRIVEQGTHNEL 664
Cdd:PRK10851 164 FGALDAQ----VRKELRRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
103-389 |
1.80e-22 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 99.10 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 103 WIIIVVSSicaiAAGAVLPLmtvVFGSLSGTFQGmfqgtmsnGEFNDELVKFVLYFVYLFIGEFFTCYIATVGWIYVGER 182
Cdd:cd18576 2 LILLLLSS----AIGLVFPL---LAGQLIDAALG--------GGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGER 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 183 ISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEK-VGLVQQSLaTFITAFVIGFVKYWKLTLILCST 261
Cdd:cd18576 67 VVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTlAEFLRQIL-TLIGGVVLLFFISWKLTLLMLAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 262 IFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHlvIAEYWGKKMKTVL--ASML 339
Cdd:cd18576 146 VPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKA--LERVVKLALKRARirALFS 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 407923078 340 GAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVLT-ILLAVMIGAfSLGNIG 389
Cdd:cd18576 224 SFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLA 273
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
437-665 |
1.82e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.61 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 437 VKHIYPS------RPEVTVMNGVDLVVEAGKTTALVGASGSGKSTI----VGLvERfydPVGGEVLLDGVNVQELN---L 503
Cdd:PRK10419 9 LSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLarllVGL-ES---PSQGNVSWRGEPLAKLNraqR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 504 HWLRQQISLVQQEPvLFATtifdNIKHGL---IGTQYEHL-------EHEKVREMVyNAAKMSNAHdfVSALPEGyetnv 573
Cdd:PRK10419 85 KAFRRDIQMVFQDS-ISAV----NPRKTVreiIREPLRHLlsldkaeRLARASEML-RAVDLDDSV--LDKRPPQ----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 574 gergflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTksegVVQA---ALDRAAQGRTTIV---IAHRLSTI-KTADK 646
Cdd:PRK10419 152 ------LSGGQLQRVCLARALAVEPKLLILDEAVSNLDL----VLQAgviRLLKKLQQQFGTAclfITHDLRLVeRFCQR 221
|
250
....*....|....*....
gi 407923078 647 IVVMSQGRIVEQGTHNELL 665
Cdd:PRK10419 222 VMVMDNGQIVETQPVGDKL 240
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
829-1062 |
2.15e-22 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 98.71 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 829 LALTQLISFtGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFdqEENSAGALTSFLSTETTSLAGLSGATLGTIFTVLT 908
Cdd:cd18576 46 FLLQAVFSF-FRIYLFARVGERVVADLRKDLYRHLQRLPLSFF--HERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQIL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 909 TLIGALVLGIAIGWKLGLVCASTIPV--LLACGFLRFwilarFEQRSKKAYEKSA---SYACEATSAIRTVASLTREEDV 983
Cdd:cd18576 123 TLIGGVVLLFFISWKLTLLMLATVPVvvLVAVLFGRR-----IRKLSKKVQDELAeanTIVEETLQGIRVVKAFTREDYE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 984 YASYHQQLVDQGAKNLRSILKSSTLYALSQSGMFLCTALGFWYGGTLISKGEYS---LFQFFVcfsaitFGAQSAGTIFS 1060
Cdd:cd18576 198 IERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTagdLVAFLL------YTLFIAGSIGS 271
|
..
gi 407923078 1061 FA 1062
Cdd:cd18576 272 LA 273
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
178-388 |
2.21e-22 |
|
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: 98.77 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 178 YVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLI 257
Cdd:cd18572 62 YAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 258 LCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLviAEYWGKKMKTVLAS 337
Cdd:cd18572 142 AFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERAL--DKALKLSVRQALAY 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 338 MLGAMMTIVYLN--YGLAFWMGSRYLVKGEMSLSDVLTILL--AVMIGAF-SLGNI 388
Cdd:cd18572 220 AGYVAVNTLLQNgtQVLVLFYGGHLVLSGRMSAGQLVTFMLyqQQLGEAFqSLGDV 275
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1022-1229 |
3.19e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 102.62 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1022 LGFWYGGTLiSKGEY----SLFQ-FFVCFSAITFgaqsagtifsFAP--DMG---KAKHAAI----QLKTLFDRkpEIDT 1087
Cdd:PRK11174 268 FGFSYLGEL-NFGHYgtgvTLFAgFFVLILAPEF----------YQPlrDLGtfyHAKAQAVgaaeSLVTFLET--PLAH 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1088 WSSDGEKINNMEG-HIEFRNVHFrypTRPEQPVLRG-LNLSVKPGQYVALVGASGCGKSTTIALLERFYnPLTGGIYADG 1165
Cdd:PRK11174 335 PQQGEKELASNDPvTIEAEDLEI---LSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKING 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 1166 KEISSLNINDYRSYIALVSQEPTLYQGTIRDNILLGadRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:PRK11174 411 IELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG--NPDASDEQLQQALENAWVSEFLPLLP 472
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
425-667 |
4.60e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 96.67 E-value: 4.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 425 LENLQGRVElrqvkhiypsrpEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfYDPVGGEVLLDGVNVQE 500
Cdd:COG0396 3 IKNLHVSVE------------GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakvLMGHPK--YEVTSGSILLDGEDILE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 501 LNLHwLRQQ--ISLVQQEPVLFA-TTIFDNIKHGLIGTQYEHLEHEKVREMVYNAAKMSNahdfvsaLPEGY---ETNVG 574
Cdd:COG0396 69 LSPD-ERARagIFLAFQYPVEIPgVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELG-------LDEDFldrYVNEG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 575 ergflLSGGQKQRIAIARAIVSDPKILLLDEATSALD-----TKSEGVvqAALdrAAQGRTTIVIAH--RLSTIKTADKI 647
Cdd:COG0396 141 -----FSGGEKKRNEILQMLLLEPKLAILDETDSGLDidalrIVAEGV--NKL--RSPDRGILIITHyqRILDYIKPDFV 211
|
250 260
....*....|....*....|
gi 407923078 648 VVMSQGRIVEQGTHnELLER 667
Cdd:COG0396 212 HVLVDGRIVKSGGK-ELALE 230
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
826-1229 |
5.73e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 102.10 E-value: 5.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 826 YLMLALTQLISFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQEenSAGALTSFLSTETTSLAGLSGATLGTIFT 905
Cdd:PRK10790 71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQ--PVGQLISRVTNDTEVIRDLYVTVVATVLR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 906 VlTTLIGA-LVLGIAIGWKLGLVCASTIPVLLacgfLRFWILARFeqrSKKAYEKSASYACEATSAIRTVASltreedvY 984
Cdd:PRK10790 149 S-AALIGAmLVAMFSLDWRMALVAIMIFPAVL----VVMVIYQRY---STPIVRRVRAYLADINDGFNEVIN-------G 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 985 ASYHQQLVDQGAKNLRSILKSSTLY-----ALSQSGMFLCTALgfwyggtliskgeySLFQFFV-CFSAITFGAQSAGTI 1058
Cdd:PRK10790 214 MSVIQQFRQQARFGERMGEASRSHYmarmqTLRLDGFLLRPLL--------------SLFSALIlCGLLMLFGFSASGTI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1059 -----FSFAPDMGKAKHAAIQLKT-----------------LFDRKPEidTWSSDGEKINNmeGHIEFRNVHFRYptRPE 1116
Cdd:PRK10790 280 evgvlYAFISYLGRLNEPLIELTTqqsmlqqavvagervfeLMDGPRQ--QYGNDDRPLQS--GRIDIDNVSFAY--RDD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1117 QPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGTIRD 1196
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLA 433
|
410 420 430
....*....|....*....|....*....|...
gi 407923078 1197 NILLGADrenVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:PRK10790 434 NVTLGRD---ISEEQVWQALETVQLAELARSLP 463
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
434-655 |
8.27e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 96.29 E-value: 8.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 434 LRQVKHIYPSRpevTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEvLLDGvnvqELNLHWLRQQISLV 513
Cdd:PRK11247 15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAG----TAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 514 QQEPVLFA-TTIFDNIKHGLIGtqyehleheKVREmvynaakmsNAHDFVSALpeGYETNVGERGFLLSGGQKQRIAIAR 592
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGLKG---------QWRD---------AALQALAAV--GLADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 593 AIVSDPKILLLDEATSALD--TKSEgvVQAALDRAAQ--GRTTIVIAHRLS-TIKTADKIVVMSQGRI 655
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDalTRIE--MQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
444-666 |
9.29e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 101.28 E-value: 9.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 444 RPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVErFYDP----VGGEVLLDGVNVqelNLHWLRQQISLVQQEPVL 519
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 520 FATTifdnikhgligTQYEHL---EHEKVREMVYNAAKMSNAHDFVSA--LPEGYETNVGERGFL--LSGGQKQRIAIAR 592
Cdd:TIGR00955 111 IPTL-----------TVREHLmfqAHLRMPRRVTKKEKRERVDEVLQAlgLRKCANTRIGVPGRVkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 593 AIVSDPKILLLDEATSALDTKSEG-VVQAALDRAAQGRTTIVIAHRLST--IKTADKIVVMSQGRIVEQGTHNELLE 666
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYsVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
433-656 |
1.87e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.57 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 433 ELRQVKHIYPSRPE-VTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN---LHWLRQ 508
Cdd:PRK10535 6 ELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 QislvqqepvlfattifdniKHGLIGTQYE---HLEHEKVREM--VY----NAAKMSNAHDFVSALpeGYETNVGERGFL 579
Cdd:PRK10535 86 E-------------------HFGFIFQRYHllsHLTAAQNVEVpaVYagleRKQRLLRAQELLQRL--GLEDRVEYQPSQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTIKTADKIVVMSQGRIV 656
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
432-669 |
1.94e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 96.24 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIY-PSRP-EVTVMNGVDLVVEAGKTTALVGASGSGKSTIV----GLVErfydPVGGEVLL-DGV---NVQEL 501
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLqhlnGLLQ----PTSGTVTIgERVitaGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 502 NLHWLRQQISLVQQ--EPVLFATTIFDNIKHGLI--GTQYEHLEhEKVREMVYnaakmsnahdfVSALPEgyetNVGERG 577
Cdd:PRK13634 79 KLKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMnfGVSEEDAK-QKAREMIE-----------LVGLPE----ELLARS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 578 -FLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQ---AALDRaAQGRTTIVIAHRLSTI-KTADKIVVMSQ 652
Cdd:PRK13634 143 pFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAaRYADQIVVMHK 221
|
250
....*....|....*..
gi 407923078 653 GRIVEQGTHNELLERKQ 669
Cdd:PRK13634 222 GTVFLQGTPREIFADPD 238
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1102-1224 |
2.60e-21 |
|
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: 93.94 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPtrPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIA 1181
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 407923078 1182 LVSQEPT--LYQGTIRDNIL-----LGADRENVpEEAIIKACKDANIYDF 1224
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAfgpenLGLPREEI-RERVEEALELVGLEHL 127
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
448-665 |
2.87e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.70 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 448 TVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLV-QQEPVLFATTIFD 526
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLpQHHLTPEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 527 NIKHGligtQYEHLEH-----EKVREMVYNAakMSNAHdfVSALPEGYETNvgergflLSGGQKQRIAIARAIVSDPKIL 601
Cdd:PRK11231 96 LVAYG----RSPWLSLwgrlsAEDNARVNQA--MEQTR--INHLADRRLTD-------LSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 602 LLDEATSALDTKSegvvQAAL-----DRAAQGRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK11231 161 LLDEPTTYLDINH----QVELmrlmrELNTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
436-661 |
4.22e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.93 E-value: 4.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDG------VNVQELNLHWLRQQ 509
Cdd:PRK11124 4 QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEPVLFA-TTIFDNikhgLIgtqyehlehE---KVREMVYNAAKmSNAHDFVSALpegYETNVGERGFL-LSGGQ 584
Cdd:PRK11124 84 VGMVFQQYNLWPhLTVQQN----LI---------EapcRVLGLSKDQAL-ARAEKLLERL---RLKPYADRFPLhLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 585 KQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTH 661
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDA 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
432-669 |
5.25e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.90 E-value: 5.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIY-PSRP-EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDG----VNVQELNLHW 505
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 506 LRQQISLVQQ--EPVLFATTIFDNIKHGL--IGTQYEHLEHEKVREMvynaAKMSNAHDFVSALPegyetnvgergFLLS 581
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPknFGFSEDEAKEKALKWL----KKVGLSEDLISKSP-----------FELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 582 GGQKQRIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQG 659
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHA 227
|
250
....*....|
gi 407923078 660 THNELLERKQ 669
Cdd:PRK13641 228 SPKEIFSDKE 237
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
432-669 |
6.17e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.43 E-value: 6.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPS-RP-EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNV--QELN--LHW 505
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItsTSKNkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 506 LRQQISLVQQ--EPVLFATTIFDNI-----KHGLIGTQYEHLEHEKVReMVynaakmsnahdfvsalpeGYETNVGERG- 577
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVafgpqNFGVSQEEAEALAREKLA-LV------------------GISESLFEKNp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 578 FLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIV-IAHRLSTIKT-ADKIVVMSQGRI 655
Cdd:PRK13649 144 FELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKL 223
|
250 260
....*....|....*....|
gi 407923078 656 VEQGT------HNELLERKQ 669
Cdd:PRK13649 224 VLSGKpkdifqDVDFLEEKQ 243
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1099-1229 |
6.49e-21 |
|
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: 98.28 E-value: 6.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1099 EGHIEFRNVHFRYPTRpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRS 1178
Cdd:COG4618 328 KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 407923078 1179 YIALVSQEPTLYQGTIRDNIllgADRENVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENI---ARFGDADPEKVVAAAKLAGVHEMILRLP 454
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
445-653 |
1.11e-20 |
|
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: 92.01 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 445 PEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWL----RQQISLVQQEPVLF 520
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 521 ATTIFDNIkhgLIGTQYEHLEHEkvreMVYNAAKMSNAHDFvsaLPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKI 600
Cdd:cd03290 92 NATVEENI---TFGSPFNKQRYK----AVTDACSLQPDIDL---LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 601 LLLDEATSALDTK-SEGVVQAALDRAAQG--RTTIVIAHRLSTIKTADKIVVMSQG 653
Cdd:cd03290 162 VFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1102-1212 |
1.21e-20 |
|
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: 91.76 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPT-RPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINdyrsyI 1180
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110
....*....|....*....|....*....|...
gi 407923078 1181 ALVSQEPTLYQ-GTIRDNILLGADRENVPEEAI 1212
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEA 108
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
106-379 |
1.32e-20 |
|
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: 93.64 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 106 IVVSSICAIAAGAVLPLMTVVFGSLsgtFQGMFQGTmsngefNDELVKFV-LYFVYLFIGEFFTCYIATVGWIYVGERIS 184
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPL---LDDIFVEK------DLEALLLVpLAIIGLFLLRGLASYLQTYLMAYVGQRVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 185 SRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKV-GLVQQSLaTFITAFVIGFVKYWKLTLILCSTIF 263
Cdd:cd18552 72 RDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALtVLVRDPL-TVIGLLGVLFYLDWKLTLIALVVLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 264 AIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEhlVIAEYWGKKMKTVLAS-MLGAM 342
Cdd:cd18552 151 LAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRK--ANERLRRLSMKIARARaLSSPL 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 407923078 343 M-TIVYLNYGLAFWMGSRYLVKGEMSLSDVLTILLAVM 379
Cdd:cd18552 229 MeLLGAIAIALVLWYGGYQVISGELTPGEFISFITALL 266
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
446-670 |
1.33e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 92.72 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 446 EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQEL-------------NLHWLRQQISL 512
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 513 VQQEPVLFA-TTIFDNIKHGLIgtQYEHLEHEKVREmvyNAAKMSNAHDFVSALPEGYETNvgergflLSGGQKQRIAIA 591
Cdd:PRK10619 97 VFQHFNLWShMTVLENVMEAPI--QVLGLSKQEARE---RAVKYLAKVGIDERAQGKYPVH-------LSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 592 RAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTIK-TADKIVVMSQGRIVEQGTHNELLERKQ 669
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
.
gi 407923078 670 A 670
Cdd:PRK10619 245 S 245
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
431-662 |
1.54e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 96.63 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 431 RVELRQVKHIYPSrpeVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGvnvQELNLH----WL 506
Cdd:COG3845 5 ALELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRsprdAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 507 RQQISLVQQEPVLFAT-TIFDNIKHGLIGTQYEHLEHEKVREMVynaAKMSNAHDF-------VSALPegyetnVGERgf 578
Cdd:COG3845 79 ALGIGMVHQHFMLVPNlTVAENIVLGLEPTKGGRLDRKAARARI---RELSERYGLdvdpdakVEDLS------VGEQ-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 579 llsggqkQRIAIARAIVSDPKILLLDEATSALdTKSEgvVQ---AALDR-AAQGRTTIVIAHRLSTIKT-ADKIVVMSQG 653
Cdd:COG3845 148 -------QRVEILKALYRGARILILDEPTAVL-TPQE--ADelfEILRRlAAEGKSIIFITHKLREVMAiADRVTVLRRG 217
|
....*....
gi 407923078 654 RIVeqGTHN 662
Cdd:COG3845 218 KVV--GTVD 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
433-658 |
1.57e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 92.62 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 433 ELRQVKHIYP-SRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQ----ElnlhwlR 507
Cdd:COG4525 5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgaD------R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 508 qqiSLVQQEPVLFA-TTIFDNIKHGL-IGTQYEHLEHEKVREMVynaaKMSNAHDFVSALPegYEtnvgergflLSGGQK 585
Cdd:COG4525 79 ---GVVFQKDALLPwLNVLDNVAFGLrLRGVPKAERRARAEELL----ALVGLADFARRRI--WQ---------LSGGMR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 586 QRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAHR------LSTiktadKIVVMS--QGRI 655
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITHSveealfLAT-----RLVVMSpgPGRI 215
|
...
gi 407923078 656 VEQ 658
Cdd:COG4525 216 VER 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
436-659 |
1.87e-20 |
|
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: 91.28 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIY----PSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVqelnlhwLRQQIS 511
Cdd:cd03266 3 TADALTkrfrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-------VKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFATTifdnikhGLigtqYEHLeheKVREMV-YNAA----KMSNAHDFVSALPE--GYETNVGERGFLLSGGQ 584
Cdd:cd03266 76 ARRRLGFVSDST-------GL----YDRL---TARENLeYFAGlyglKGDELTARLEELADrlGMEELLDRRVGGFSTGM 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 585 KQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTIKT-ADKIVVMSQGRIVEQG 659
Cdd:cd03266 142 RQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
436-667 |
1.93e-20 |
|
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: 90.66 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfYDPVGGEVLLDGVNVQELNLH-WLRQQI 510
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTlaktIMGHPK--YEVTEGEILFKGEDITDLPPEeRARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 511 SLVQQEPVLFattifdnikhgligtqyehlehekvrEMVYNAakmsnahDFVSALPEGyetnvgergflLSGGQKQRIAI 590
Cdd:cd03217 80 FLAFQYPPEI--------------------------PGVKNA-------DFLRYVNEG-----------FSGGEKKRNEI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 591 ARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAH--RLSTIKTADKIVVMSQGRIVEQGThNELLER 667
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
434-664 |
2.02e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.52 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 434 LRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN---LHWLRQQI 510
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 511 SLVQQEPVLFA-TTIFDNIKHGLigtqyehLEHEKVREMVYNAAKMSNAHdfvsalpegyetNVGERGFL------LSGG 583
Cdd:PRK11831 87 SMLFQSGALFTdMNVFDNVAYPL-------REHTQLPAPLLHSTVMMKLE------------AVGLRGAAklmpseLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 584 QKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAHRL-STIKTADKIVVMSQGRIVEQGT 660
Cdd:PRK11831 148 MARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnSALGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGS 227
|
....
gi 407923078 661 HNEL 664
Cdd:PRK11831 228 AQAL 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
449-1198 |
2.34e-20 |
|
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: 98.06 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGvnvqelnlhwlrqQISLVQQEPVLFATTIFDNI 528
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 529 KHGLIGTQYEHLEhekvremVYNAAKMsnaHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATS 608
Cdd:TIGR01271 508 IFGLSYDEYRYTS-------VIKACQL---EEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 609 ALDTKSEG-VVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERKQAY---------YNLVEAQ 678
Cdd:TIGR01271 578 HLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFsslllgleaFDNFSAE 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 679 R---IAAANEKIEEEEEEEEEVDLTEVDDETIKRTVSPQSEKRS------------------------------------ 719
Cdd:TIGR01271 658 RrnsILTETLRRVSIDGDSTVFSGPETIKQSFKQPPPEFAEKRKqsiilnpiasarkfsfvqmgpqkaqattiedavrep 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 720 ----YSVDPDDD-VAARLKRT---------QSGKSESSVALA----------KKQPASEQKYSLATLIKLIAS------- 768
Cdd:TIGR01271 738 serkFSLVPEDEqGEESLPRGnqyhhglqhQAQRRQSVLQLMthsnrgenrrEQLQTSFRKKSSITQQNELASeldiysr 817
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 769 -----------------------FNRQE-------W----------------LLMVQGLFWSIIAG--------GGNPTQ 794
Cdd:TIGR01271 818 rlskdsvyeiseeineedlkecfADEREnvfetttWntylryittnrnlvfvLIFCLVIFLAEVAAsllglwliTDNPSA 897
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 795 AVFFAKSISALSRPPSEYGKLRSEANFWSLMYLMLALTQLISFTG--QGLCFA---ICSEKLIHRvrdTAFRTMLRQDIS 869
Cdd:TIGR01271 898 PNYVDQQHANASSPDVQKPVIITPTSAYYIFYIYVGTADSVLALGffRGLPLVhtlLTVSKRLHE---QMLHSVLQAPMA 974
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 870 FFDQEEnsAGALTSFLSTETTSLAGLSGATLGTIFTVLTTLIGALVLgIAIGWKLGLVcaSTIPVLLACGFLRFWILaRF 949
Cdd:TIGR01271 975 VLNTMK--AGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFV-VSVLQPYIFI--AAIPVAVIFIMLRAYFL-RT 1048
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 950 EQRSKKayeksasYACEATSAIRT--VASLtreedvyasyhqqlvdQGAKNLRSILKSSTLYALSQSGMFLCTALGFWYG 1027
Cdd:TIGR01271 1049 SQQLKQ-------LESEARSPIFShlITSL----------------KGLWTIRAFGRQSYFETLFHKALNLHTANWFLYL 1105
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1028 GTLiskgEYSLFQ----FFVCFSAITFGA---------------------------------------QSAGTIFSF--- 1061
Cdd:TIGR01271 1106 STL----RWFQMRidiiFVFFFIAVTFIAigtnqdgegevgiiltlamnilstlqwavnssidvdglmRSVSRVFKFidl 1181
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1062 APDMGKAK--HAAIQLKT--LFDRKPEIDTWSSdgekinnmEGHIEFRNVHFRYpTRPEQPVLRGLNLSVKPGQYVALVG 1137
Cdd:TIGR01271 1182 PQEEPRPSggGGKYQLSTvlVIENPHAQKCWPS--------GGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLG 1252
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 1138 ASGCGKSTTIALLERFYNPlTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGTIRDNI 1198
Cdd:TIGR01271 1253 RTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL 1312
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
432-667 |
2.70e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.14 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPEVtvMNGVDLVVEAGKTTALVGASGSGKST----IVGLvERFydpVGGEVLLDGVNVQEL-----N 502
Cdd:PRK11650 4 LKLQAVRKSYDGKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTllrmVAGL-ERI---TSGEIWIGGRVVNELepadrD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 503 lhwlrqqISLVQQEPVLFA-TTIFDNIKHGL--IGTQYEHLEhEKVREmvynAAKMSNAHDFVSALPEGyetnvgergfl 579
Cdd:PRK11650 78 -------IAMVFQNYALYPhMSVRENMAYGLkiRGMPKAEIE-ERVAE----AARILELEPLLDRKPRE----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEgvVQAALD-RAAQGR---TTIVIAH-RLSTIKTADKIVVMSQGR 654
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR--VQMRLEiQRLHRRlktTSLYVTHdQVEAMTLADRVVVMNGGV 212
|
250
....*....|....
gi 407923078 655 IvEQ-GTHNELLER 667
Cdd:PRK11650 213 A-EQiGTPVEVYEK 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-666 |
3.05e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.83 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 439 HIYPSRPEVtvMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYD-----PVGGEVLLDGVNV--QELNLHWLRQQIS 511
Cdd:PRK14267 11 RVYYGSNHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFA-TTIFDNIKhglIGTQYEHL--EHEKVREMVYNAAKMSNAHDFVSALPEGYETNvgergflLSGGQKQRI 588
Cdd:PRK14267 89 MVFQYPNPFPhLTIYDNVA---IGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 589 AIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHR-LSTIKTADKIVVMSQGRIVEQGTHNELLE 666
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
449-670 |
3.32e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.99 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDG--VNVQELNLHWLRQQISLVQQEP--VLFATTI 524
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 525 FDNIKHGL--IGtqyehLEHEKVREMVYNAAKMSNAHDFVSALPEgyetnvgergfLLSGGQKQRIAIARAIVSDPKILL 602
Cdd:PRK13638 96 DSDIAFSLrnLG-----VPEAEITRRVDEALTLVDAQHFRHQPIQ-----------CLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 603 LDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNELLERKQA 670
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
448-665 |
5.20e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.70 E-value: 5.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 448 TVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGG-----EVLLDGVNV-QELNLHWLRQQISLVQQEPVLFA 521
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 522 TTIFDNIkhgLIGTQYEHLEHEKVREMVYNAaKMSNAhdfvsALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKIL 601
Cdd:PRK14271 115 MSIMDNV---LAGVRAHKLVPRKEFRGVAQA-RLTEV-----GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 602 LLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
820-1038 |
8.66e-20 |
|
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: 91.38 E-value: 8.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 820 NFWSLMYLMLALTQLISFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTETTSLAGLSGAT 899
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDS--RPVGKILSRVINDVNSLSDLLSNG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 900 LGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLlacgflrFWILARFEQRSKKAY----EKSA---SYACEATSAIR 972
Cdd:cd18545 118 LINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLL-------VLVVFLLRRRARKAWqrvrKKISnlnAYLHESISGIR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 973 TVASLTREEDVYASYHQQLVDqgakNLRSILKSSTLYALSQSGMFLCTALG----FWYGGTLISKGEYSL 1038
Cdd:cd18545 191 VIQSFAREDENEEIFDELNRE----NRKANMRAVRLNALFWPLVELISALGtalvYWYGGKLVLGGAITV 256
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
448-672 |
9.38e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.39 E-value: 9.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 448 TVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFY--DPV---GGEVLLDG---VNVQELNLHWLR-QQISLVQQEPV 518
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsPPVvypSGDIRFHGeslLHASEQTLRGVRgNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 519 LFAttifdNIKHGLIGTQYEHLE-HekvREMVYNAAK-----------MSNAHDFVSALPEGyetnvgergflLSGGQKQ 586
Cdd:PRK15134 103 VSL-----NPLHTLEKQLYEVLSlH---RGMRREAARgeilncldrvgIRQAAKRLTDYPHQ-----------LSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 587 RIAIARAIVSDPKILLLDEATSALDTKsegvVQA---ALDRAAQ---GRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQG 659
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVS----VQAqilQLLRELQqelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQN 239
|
250
....*....|...
gi 407923078 660 THNELLERKQAYY 672
Cdd:PRK15134 240 RAATLFSAPTHPY 252
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
909-1229 |
9.88e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 94.78 E-value: 9.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 909 TLIGALVLGIA--------IGWKLGLVCASTIPVLlACGFLRFWilARFEQRSKKAYEKSAS---YACEATSAIRTVASL 977
Cdd:PRK10789 116 TLVDSLVMGCAvlivmstqISWQLTLLALLPMPVM-AIMIKRYG--DQLHERFKLAQAAFSSlndRTQESLTSIRMIKAF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 978 TREEDVYASYHQQLVDQGAKNLR----SILKSSTLYALSQSGMFLCTALGFWyggtLISKGEYSLFQF--FVCFSAITFG 1051
Cdd:PRK10789 193 GLEDRQSALFAADAEDTGKKNMRvariDARFDPTIYIAIGMANLLAIGGGSW----MVVNGSLTLGQLtsFVMYLGLMIW 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1052 AQSA-GTIFSFApDMGKAKHAAIQlkTLFDRKPEIDtwssDGEK-INNMEGHIEFRNVHFRYPTRpEQPVLRGLNLSVKP 1129
Cdd:PRK10789 269 PMLAlAWMFNIV-ERGSAAYSRIR--AMLAEAPVVK----DGSEpVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKP 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1130 GQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGTIRDNILLGadRENVPE 1209
Cdd:PRK10789 341 GQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALG--RPDATQ 418
|
330 340
....*....|....*....|
gi 407923078 1210 EAIIKACKDANIYDFIMSLP 1229
Cdd:PRK10789 419 QEIEHVARLASVHDDILRLP 438
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
436-659 |
1.14e-19 |
|
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: 88.88 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNlhwlRQQISLVQQ 515
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 516 EPVLF-ATTIFDNIKHGligTQYEHLEHEKVREmvynaakmsNAHDFVSALP-EGYETNVGERgflLSGGQKQRIAIARA 593
Cdd:cd03269 78 ERGLYpKMKVIDQLVYL---AQLKGLKKEEARR---------RIDEWLERLElSEYANKRVEE---LSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 594 IVSDPKILLLDEATSALDTKSEGVV-QAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQG 659
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLkDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
450-653 |
1.20e-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: 89.45 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 450 MNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNlhwlRQQISLVQQEPVLFATTIFDNIK 529
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG----PDRMVVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 530 HGlIGTQYEHLEHEKVREMVYNAAKMSNahdfvsaLPEGYETNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSA 609
Cdd:TIGR01184 77 LA-VDRVLPDLSKSERRAIVEEHIALVG-------LTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 407923078 610 LDTKSEGVVQAALDRAAQ--GRTTIVIAHRL-STIKTADKIVVMSQG 653
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
452-612 |
1.92e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 88.31 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 452 GVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDP---VGGEVLLDGVNVQELNLHwlRQQISLVQQEPVLFA-TTIFDN 527
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 528 IKHGLIGTqyehLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQRIAIARAIVSDPKILLLDEAT 607
Cdd:COG4136 97 LAFALPPT----IGRAQRRARVEQALEEAGLAGFADRDPAT-----------LSGGQRARVALLRALLAEPRALLLDEPF 161
|
....*
gi 407923078 608 SALDT 612
Cdd:COG4136 162 SKLDA 166
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
450-663 |
2.92e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.01 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 450 MNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN---LHWLRQQISLV-QQEPVLFATTIF 525
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIfQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 526 DNIKHGLIgtqYEHLEHEKVREMVynaakmSNAHDFVSALPEGYETNVGergflLSGGQKQRIAIARAIVSDPKILLLDE 605
Cdd:PRK10908 98 DNVAIPLI---IAGASGDDIRRRV------SAALDKVGLLDKAKNFPIQ-----LSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 606 ATSALDTK-SEGVVQAALDRAAQGRTTIVIAHRLSTIKTAD-KIVVMSQGRIVEqGTHNE 663
Cdd:PRK10908 164 PTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLHG-GVGGE 222
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
157-389 |
3.08e-19 |
|
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: 89.47 E-value: 3.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 157 YFVYLF-------IGEFFTCYiaTVGWIyvGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEK 229
Cdd:cd18575 38 AFLLLLavalvlaLASALRFY--LVSWL--GERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 230 VGLVQQSLATFITAFVIGFVKYWKLTLILCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGT 309
Cdd:cd18575 114 LSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 310 QDKLARQYNEHLVIAEYWGKKMKTVLASMLGAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVLTILLAVMIGAFSLGNIG 389
Cdd:cd18575 194 EDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALS 273
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
431-679 |
3.10e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.60 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 431 RVELRQVKhIYPSRPEVtvmNGVDLVVEAGKTTALVGASGSGKS-TIVGL-------VERfydpVGGEVLLDGvnvQELN 502
Cdd:PRK10418 4 QIELRNIA-LQAAQPLV---HGVSLTLQRGRVLALVGGSGSGKSlTCAAAlgilpagVRQ----TAGRVLLDG---KPVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 503 LHWLR-QQISLVQQEPvlfaTTIFDNIKhgligTQYEHlehekVREMVYNAAKMSNAHDFVSALPEgyetnVG----ER- 576
Cdd:PRK10418 73 PCALRgRKIATIMQNP----RSAFNPLH-----TMHTH-----ARETCLALGKPADDATLTAALEA-----VGlenaARv 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 577 ----GFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTksegVVQA-ALD-----RAAQGRTTIVIAHRLSTI-KTAD 645
Cdd:PRK10418 134 lklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV----VAQArILDllesiVQKRALGMLLVTHDMGVVaRLAD 209
|
250 260 270
....*....|....*....|....*....|....*.
gi 407923078 646 KIVVMSQGRIVEQGTHNELLERKQ--AYYNLVEAQR 679
Cdd:PRK10418 210 DVAVMSHGRIVEQGDVETLFNAPKhaVTRSLVSAHL 245
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1098-1211 |
3.87e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.79 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1098 MEGHIEFRNVHFRYPTRPEQ-PVLRGLNLSVKPGQYVALVGASGCGKST---TIALLERfynPLTGGIYADGKEISSLNI 1173
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSE 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 407923078 1174 ND---YR-SYIALVSQE----PTLyqgTIRDNILL-----GADRENVPEEA 1211
Cdd:COG1136 78 RElarLRrRHIGFVFQFfnllPEL---TALENVALplllaGVSRKERRERA 125
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
444-665 |
6.07e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 88.31 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 444 RPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPvlfATT 523
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 524 IFDNIKHGLI-------GTQYEHLEHEKvreMVYNAAKMsnahdfVSALPEgyetNVGERGFLLSGGQKQRIAIARAIVS 596
Cdd:PRK15112 100 LNPRQRISQIldfplrlNTDLEPEQREK---QIIETLRQ------VGLLPD----HASYYPHMLAPGQKQRLGLARALIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 597 DPKILLLDEATSALD-TKSEGVVQAALD-RAAQGRTTIVIAHRLSTIK-TADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK15112 167 RPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKhISDQVLVMHQGEVVERGSTADVL 238
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1102-1201 |
6.25e-19 |
|
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: 87.79 E-value: 6.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIA 1181
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100
....*....|....*....|.
gi 407923078 1182 LVSQEPTLYQG-TIRDNILLG 1201
Cdd:COG1120 79 YVPQEPPAPFGlTVRELVALG 99
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
437-665 |
6.71e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.67 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 437 VKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQE 516
Cdd:PRK09536 6 VSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 517 PVL-FATTIFDNIKHGligtQYEHLEHekvremvynAAKMSNAHDFV--SALPEGYETNVGERGFL-LSGGQKQRIAIAR 592
Cdd:PRK09536 86 TSLsFEFDVRQVVEMG----RTPHRSR---------FDTWTETDRAAveRAMERTGVAQFADRPVTsLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 593 AIVSDPKILLLDEATSALDTKSE-GVVQAALDRAAQGRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
432-665 |
9.21e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.74 E-value: 9.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPS-RPEVTVMNgvdLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN-LHWLRQQ 509
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENIN---LVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEP--VLFATTIFDNIKhglIGTQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQR 587
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLA---FGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKT-----------LSGGQGQC 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 588 IAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
448-672 |
1.00e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 448 TVMNGVDLVVEAGKTTALVGASGSGKSTiVGLVERFYDPVGGEVLLDGVNVQELN---LHWLRQQISLVQQEPV------ 518
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKST-TGLALLRLINSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPNsslnpr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 519 LFATTIfdnIKHGLiGTQYEHLEHEKVREMVYNAAKMsnahdfVSALPEGYETNVGErgflLSGGQKQRIAIARAIVSDP 598
Cdd:PRK15134 379 LNVLQI---IEEGL-RVHQPTLSAAQREQQVIAVMEE------VGLDPETRHRYPAE----FSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 599 KILLLDEATSALDTksegVVQA---ALDRAAQGR---TTIVIAHRLSTIKT-ADKIVVMSQGRIVEQGTHNELLERKQAY 671
Cdd:PRK15134 445 SLIILDEPTSSLDK----TVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQE 520
|
.
gi 407923078 672 Y 672
Cdd:PRK15134 521 Y 521
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
141-381 |
1.17e-18 |
|
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: 87.95 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 141 TMSNGEFNDELVKFVLYFVYLFIGEFFTC-YIATVGWIY----VGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRI 215
Cdd:cd18573 25 VASKESGDIEIFGLSLKTFALALLGVFVVgAAANFGRVYllriAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 216 TADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLILCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVE 295
Cdd:cd18573 105 SSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 296 EVFSSIRNAVAFGTQDKLARQYNEHLVIAEYWGKKMKTVLASMLGAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVLTIL 375
Cdd:cd18573 185 ERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFL 264
|
....*..
gi 407923078 376 L-AVMIG 381
Cdd:cd18573 265 MyAVYVG 271
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
797-1037 |
1.38e-18 |
|
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: 87.69 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 797 FFAKSISALSRPPSEYGKLRSEANFWSLMYLMLALTqLISFTG--QGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQe 874
Cdd:cd18780 18 FFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVL-IGSIATflRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDV- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 875 eNSAGALTSFLSTETTSLAGLSGATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLLACGFLRFWILARFEQRSK 954
Cdd:cd18780 96 -TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 955 KAYEKSASYACEATSAIRTVASLTREEDVYASYHQQlVDQgakNLRSILKSSTLYALSQSGMFLC----TALGFWYGGTL 1030
Cdd:cd18780 175 DALAAASTVAEESISNIRTVRSFAKETKEVSRYSEK-INE---SYLLGKKLARASGGFNGFMGAAaqlaIVLVLWYGGRL 250
|
....*..
gi 407923078 1031 ISKGEYS 1037
Cdd:cd18780 251 VIDGELT 257
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
447-664 |
1.43e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 88.63 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 447 VTVMNGVDLVVEAGKTTALVGASGSGKS----TIVGLVERfYDPVGGEVLLDG---VNVQELNLHWLR-QQISLVQQEPV 518
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGreiLNLPEKELNKLRaEQISMIFQDPM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 519 lfaTTIFDNIKhglIGTQ-------YEHLEH-----EKVReMVyNAAKMSNAHDFVSALPEGYetnvgergfllSGGQKQ 586
Cdd:PRK09473 108 ---TSLNPYMR---VGEQlmevlmlHKGMSKaeafeESVR-ML-DAVKMPEARKRMKMYPHEF-----------SGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 587 RIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTT--IVIAHRLSTIK-TADKIVVMSQGRIVEQGTHNE 663
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAgICDKVLVMYAGRTMEYGNARD 248
|
.
gi 407923078 664 L 664
Cdd:PRK09473 249 V 249
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
457-665 |
1.53e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 86.53 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 457 VEAGKTTALVGASGSGKST----IVGLVerfydPVGGEVLLDGVNVQELNLHWL-RQQISLVQQEPVLFATTIFdnikHG 531
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTllarMAGLL-----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVF----QY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 532 LIGTQYEHLEHEKVREMVYNAAKMSNAHDFVsalpegyETNVGErgflLSGGQKQRIAIA-------RAIVSDPKILLLD 604
Cdd:PRK03695 90 LTLHQPDKTRTEAVASALNEVAEALGLDDKL-------GRSVNQ----LSGGEWQRVRLAavvlqvwPDINPAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 605 EATSALDTKSegvvQAALDR-----AAQGRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK03695 159 EPMNSLDVAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
464-665 |
1.62e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.64 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 464 ALVGASGSGKSTIVGLVERF---YDP---VGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFA-TTIFDNIKHGLI--G 534
Cdd:PRK14246 40 GIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPhLSIYDNIAYPLKshG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 535 TQYEHLEHEKVREMVYNAAKMSNAHDFVSAlPEGYetnvgergflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKS 614
Cdd:PRK14246 120 IKEKREIKKIVEECLRKVGLWKEVYDRLNS-PASQ----------LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVN 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 407923078 615 EGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK14246 189 SQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1102-1201 |
1.85e-18 |
|
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: 85.70 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYN-----PLTGGIYADGKEISSLNINDY 1176
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVL 77
|
90 100
....*....|....*....|....*..
gi 407923078 1177 --RSYIALVSQEPTLYQGTIRDNILLG 1201
Cdd:cd03260 78 elRRRVGMVFQKPNPFPGSIYDNVAYG 104
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
436-676 |
2.13e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.09 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGvnvQELNlHWLRQQISLVQQ 515
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLD-PEDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 516 EPvlfattifdnikhGLigtqYEHLeheKVRE-MVY---------NAAKmSNAHDFVSA--LPEGYETNVGErgflLSGG 583
Cdd:COG4152 79 ER-------------GL----YPKM---KVGEqLVYlarlkglskAEAK-RRADEWLERlgLGDRANKKVEE----LSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 584 QKQRIAIARAIVSDPKILLLDEATSALD-TKSEGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTH 661
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDpVNVELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSV 213
|
250
....*....|....*
gi 407923078 662 NELleRKQAYYNLVE 676
Cdd:COG4152 214 DEI--RRQFGRNTLR 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1095-1225 |
2.20e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 86.58 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1095 INNMEGHIEFRNVHFRYPTRpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIN 1174
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLK 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 1175 DYRSYIALVSQEP-TLYQG-TIRDNILLGADRENVPEE---AII-KACKDANIYDFI 1225
Cdd:PRK13632 80 EIRKKIGIIFQNPdNQFIGaTVEDDIAFGLENKKVPPKkmkDIIdDLAKKVGMEDYL 136
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
452-638 |
2.40e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 86.37 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 452 GVDLVVEAGKTTALVGASGSGKSTIVGLVERFYD-----PVGGEVLLDGVNV--QELNLHWLRQQISLVQQEPVLFATTI 524
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 525 FDNIKHGLIGTQYEHLEHEKVREMVYNAAKMSNAHDfvsalpegyetNVGERGFLLSGGQKQRIAIARAIVSDPKILLLD 604
Cdd:PRK14243 108 YDNIAYGARINGYKGDMDELVERSLRQAALWDEVKD-----------KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190
....*....|....*....|....*....|....
gi 407923078 605 EATSALDTKSEGVVQAALDRAAQGRTTIVIAHRL 638
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
436-657 |
2.71e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.91 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNlhwlRQQISLVQQ 515
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 516 EPVLFATTIFDNIKHGLigtQYEHLEHEKVREMvynAAKMSNAHDFvsalpEGYETnvgERGFLLSGGQKQRIAIARAIV 595
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGL---QLAGVEKMQRLEI---AHQMLKKVGL-----EGAEK---RYIWQLSGGQRQRVGIARALA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 596 SDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAHRL-STIKTADKIVVMS--QGRIVE 657
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIeEAVFMATELVLLSpgPGRVVE 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
434-654 |
3.02e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.60 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 434 LRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYdPVG---GEVLLDGvnvQELNLHWLRQQ- 509
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEG---EELQASNIRDTe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ---ISLVQQEPVLFAT-TIFDNIkhgligtqyeHLEHEKVREMVYNAAKM-SNAHDFVSALpeGYETNVGERGFLLSGGQ 584
Cdd:PRK13549 81 ragIAIIHQELALVKElSVLENI----------FLGNEITPGGIMDYDAMyLRAQKLLAQL--KLDINPATPVGNLGLGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407923078 585 KQRIAIARAIVSDPKILLLDEATSALdTKSEGVVQAAL--DRAAQGRTTIVIAHRLSTIKT-ADKIVVMSQGR 654
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
449-660 |
3.20e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQEL---NLHWLR-QQISLVQQ-EPVLFATT 523
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRnQKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 524 IFDNIKHGL-IGTQYEHLEHEKVREMVynAAKmsnahdfvsalpeGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILL 602
Cdd:PRK11629 104 ALENVAMPLlIGKKKPAEINSRALEML--AAV-------------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 603 LDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGT 660
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
449-664 |
3.24e-18 |
|
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: 86.45 E-value: 3.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGvnvqelnlhwlrqQISLVQQEPVLFATTIFDNI 528
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 529 KHGLIGTQYEHLehekvremvyNAAKMSNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATS 608
Cdd:cd03291 119 IFGVSYDEYRYK----------SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 609 ALDTKSEG-VVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNEL 664
Cdd:cd03291 189 YLDVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
434-664 |
4.29e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.34 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 434 LRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN---LHWLrqQI 510
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQL--GI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 511 SLVQQEPVLFAT-TIFDNIKHGLIGTQyehLEHEKVREMVYNAAKMSNAHDFVSALpegyetNVGERgfllsggqkQRIA 589
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENILFGLPKRQ---ASMQKMKQLLAALGCQLDLDSSAGSL------EVADR---------QIVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 590 IARAIVSDPKILLLDEATSALdTKSE-----GVVQAALDraaQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNE 663
Cdd:PRK15439 151 ILRGLMRDSRILILDEPTASL-TPAEterlfSRIRELLA---QGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTAD 226
|
.
gi 407923078 664 L 664
Cdd:PRK15439 227 L 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1120-1203 |
4.62e-18 |
|
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: 82.31 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1120 LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQG-TIRDNI 1198
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
....*
gi 407923078 1199 LLGAD 1203
Cdd:pfam00005 81 RLGLL 85
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
432-666 |
5.82e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIY-PSRPEVT-VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNV----QELNLHW 505
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 506 LRQQISLVQQEP--VLFATTIFDNIKHGLIGTQYEHLEHEKVRemvynAAKMsnahDFVSALPEGYEtnvgERGFLLSGG 583
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIA-----AEKL----EMVGLADEFWE----KSPFELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 584 QKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ-GRTTIVIAHRLSTIKT-ADKIVVMSQGRIVEQGTH 661
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
....*
gi 407923078 662 NELLE 666
Cdd:PRK13643 229 SDVFQ 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
432-668 |
5.84e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.01 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRpevTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQElNLHWLRQQIS 511
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQepvlfattiFDN-------IKHGLIGTQYEHLEHEKVREMV---YNAAKMSNAHDfvsalpegyeTNVGErgflLS 581
Cdd:PRK13537 84 VVPQ---------FDNldpdftvRENLLVFGRYFGLSAAAARALVpplLEFAKLENKAD----------AKVGE----LS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 582 GGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQG 659
Cdd:PRK13537 141 GGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEG 220
|
....*....
gi 407923078 660 THNELLERK 668
Cdd:PRK13537 221 APHALIESE 229
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1102-1219 |
6.05e-18 |
|
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: 83.72 E-value: 6.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIndYRSYIA 1181
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP--ERRNIG 75
|
90 100 110
....*....|....*....|....*....|....*....
gi 407923078 1182 LVSQEPTLYQG-TIRDNILLGADRENVPEEAIIKACKDA 1219
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVPKAEIRARVREL 114
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
438-614 |
6.15e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.45 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 438 KHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHW---LR-QQISLV 513
Cdd:PRK10584 14 KSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRaKHVGFV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 514 QQEPVLFAT-TIFDNIK-HGLIGTQYEHLEHEKVREMVynaakmsnahdfvsalpegYETNVGER----GFLLSGGQKQR 587
Cdd:PRK10584 94 FQSFMLIPTlNALENVElPALLRGESSRQSRNGAKALL-------------------EQLGLGKRldhlPAQLSGGEQQR 154
|
170 180
....*....|....*....|....*..
gi 407923078 588 IAIARAIVSDPKILLLDEATSALDTKS 614
Cdd:PRK10584 155 VALARAFNGRPDVLFADEPTGNLDRQT 181
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1102-1201 |
8.02e-18 |
|
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: 82.62 E-value: 8.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIN--DYRSY 1179
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRR 77
|
90 100
....*....|....*....|...
gi 407923078 1180 IALVSQEPTLYQG-TIRDNILLG 1201
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG 100
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
434-686 |
8.08e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 434 LRQVKHIYPSRPevtVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGvnvqelnlhwlRQQISLV 513
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 514 QQEPVLFAT-TIFDNIKHGL-----IGTQYEHLEHeKVREMVYNAAKMSNAHDFVSALpEGYE----------------- 570
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDaelraLEAELEELEA-KLAEPDEDLERLAELQEEFEAL-GGWEaearaeeilsglgfpee 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 571 ---TNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKS----EGVVqaaldRAAQGrTTIVIAH-R--LSt 640
Cdd:COG0488 145 dldRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSHdRyfLD- 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 407923078 641 iKTADKIVVMSQGRIVE-QGTHNELLERKQAyynlvEAQRIAAANEK 686
Cdd:COG0488 214 -RVATRILELDRGKLTLyPGNYSAYLEQRAE-----RLEQEAAAYAK 254
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
763-1211 |
9.05e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 88.32 E-value: 9.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 763 IKLIASFNRQEWLLMVQGLFWSIIAGGGNptqAVFFAKSISALSRPPSEYGKLrseanFWslMYLMLALTQLISFTGQGL 842
Cdd:COG4615 1 MNLLRLLLRESRWLLLLALLLGLLSGLAN---AGLIALINQALNATGAALARL-----LL--LFAGLLVLLLLSRLASQL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 843 CFAICSEKLIHRVRDTAFRTMLRQDISFFdqEENSAGALTSFLSTETTSLAGLSGAtLGTIFTVLTTLIGALVLgiaIGW 922
Cdd:COG4615 71 LLTRLGQHAVARLRLRLSRRILAAPLERL--ERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAY---LAW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 923 KLGLVCASTIPVLLACGFLRFWILARFEQRSKKAYEKsasyaceatsairtvasltrEEDVYASYhQQLVDqGAKNLR-S 1001
Cdd:COG4615 145 LSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREA--------------------EDRLFKHF-RALLE-GFKELKlN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1002 ILKSSTLY-----ALSQSGMFLCTALGFWYGgTLISKGEYSLFQF--FVCFSAITFGAQSAGTIFSFA------------ 1062
Cdd:COG4615 203 RRRRRAFFdedlqPTAERYRDLRIRADTIFA-LANNWGNLLFFALigLILFLLPALGWADPAVLSGFVlvllflrgplsq 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1063 -----PDMGKAKHAAIQLKTLFDRKPEIDTWSSDGEKINNMEG--HIEFRNVHFRYPTRPEQPVLR-G-LNLSVKPGQYV 1133
Cdd:COG4615 282 lvgalPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGDEGFTlGpIDLTIRRGELV 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 1134 ALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGtirdniLLGADRENVPEEA 1211
Cdd:COG4615 362 FIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGEADPARA 433
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
436-672 |
1.04e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.93 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHI---YPSRpevTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQELNLHwLRQ 508
Cdd:COG1137 5 EAENLvksYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHLPMH-KRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 Q--ISLVQQEPVLFAT-TIFDNIKhgligtqyehleheKVREMVYNAAKMSNAHdfVSALPEgyETNVGE----RGFLLS 581
Cdd:COG1137 77 RlgIGYLPQEASIFRKlTVEDNIL--------------AVLELRKLSKKEREER--LEELLE--EFGITHlrksKAYSLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 582 GGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIA-H--RlSTIKTADKIVVMSQGRIVEQ 658
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITdHnvR-ETLGICDRAYIISEGKVLAE 217
|
250
....*....|....*.
gi 407923078 659 GTHNELLERKQA--YY 672
Cdd:COG1137 218 GTPEEILNNPLVrkVY 233
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
104-389 |
1.07e-17 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 84.79 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 104 IIIVVSSICAIAAGAVLPLMTvvfgslsgtfqgmfQGTMSNGEFNDELVKFVLYFVYLFIGEFFTCYIATVGWIYVGERI 183
Cdd:cd18551 2 ILALLLSLLGTAASLAQPLLV--------------KNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 184 SSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEkvGLVQ--QSLATFITAFVIGFVKYWKLTLILCST 261
Cdd:cd18551 68 VLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITS--GLPQlvTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 262 IFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLVIAEYWGKKMKTVLASMLGA 341
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 407923078 342 MMTIVYLNYGLAFWMGSrYLV-KGEMSLSDVLTILLAVMIGAFSLGNIG 389
Cdd:cd18551 226 MGLAVQLALLVVLGVGG-ARVaSGALTVGTLVAFLLYLFQLITPLSQLS 273
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
431-666 |
1.36e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.14 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 431 RVELRQVKHIYPSRP--EVTVMNGVDLVVEAGKTTALVGASGSGKSTIV-----------GLVERFYD-------PVGGE 490
Cdd:PRK13651 2 QIKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehlnalllpdtGTIEWIFKdeknkkkTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 491 VLLDGVNVQEL------NLHWLRQQISLVQQ--EPVLFATTIFDNIKHGLIGTQYEHLEHEKVremvynAAKMSNahdfV 562
Cdd:PRK13651 82 KVLEKLVIQKTrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKR------AAKYIE----L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 563 SALPEGYetnVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDtkSEGVVQaALD----RAAQGRTTIVIAHRL 638
Cdd:PRK13651 152 VGLDESY---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD--PQGVKE-ILEifdnLNKQGKTIILVTHDL 225
|
250 260
....*....|....*....|....*....
gi 407923078 639 -STIKTADKIVVMSQGRIVEQGTHNELLE 666
Cdd:PRK13651 226 dNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1102-1200 |
1.40e-17 |
|
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: 81.68 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSlNINDYRSYIA 1181
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100
....*....|....*....|
gi 407923078 1182 LVSQEPTLYQG-TIRDNILL 1200
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL 96
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1102-1214 |
1.40e-17 |
|
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: 83.50 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRpeQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIA 1181
Cdd:cd03295 1 IEFENVTKRYGGG--KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110
....*....|....*....|....*....|....
gi 407923078 1182 LVSQEPTLY-QGTIRDNILLGADRENVPEEAIIK 1214
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALVPKLLKWPKEKIRE 112
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
103-657 |
2.00e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 87.16 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 103 WIIIVVSSICAIAAGAVLPLMTVVFGSLSGTFQGMFQGtmsngefndeLVKFVLYFVYLFIGEFFTCYIATvgwiYVGER 182
Cdd:COG4615 13 WLLLLALLLGLLSGLANAGLIALINQALNATGAALARL----------LLLFAGLLVLLLLSRLASQLLLT----RLGQH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 183 ISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQqSLATFITAFVigfvkY--WKLTLILCS 260
Cdd:COG4615 79 AVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQ-SVALVLGCLA-----YlaWLSPPLFLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 261 TIFAIVFTMGGGSTFIMKYNKQSLAS-------YALGGTVVE---EV-FSSIRNAVAFGTQ-DKLARQYNEHLVIAEYWg 328
Cdd:COG4615 153 TLVLLGLGVAGYRLLVRRARRHLRRAreaedrlFKHFRALLEgfkELkLNRRRRRAFFDEDlQPTAERYRDLRIRADTI- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 329 kkmkTVLASMLGAMMtiVYLNYGLAFWMGSRYlvkGEMSLSD----VLTIL-----LAVMIGAF--------SLGNIgpw 391
Cdd:COG4615 232 ----FALANNWGNLL--FFALIGLILFLLPAL---GWADPAVlsgfVLVLLflrgpLSQLVGALptlsranvALRKI--- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 392 lqafttataaaSKMYSTIDRVSPLDPTSKEGRRLENLQgRVELRQVKHIYPSRPE---VTVmnG-VDLVVEAGKTTALVG 467
Cdd:COG4615 300 -----------EELELALAAAEPAAADAAAPPAPADFQ-TLELRGVTYRYPGEDGdegFTL--GpIDLTIRRGELVFIVG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 468 ASGSGKST----IVGLverfYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATtifdnikhgLIGTQYEHLEhE 543
Cdd:COG4615 366 GNGSGKSTlaklLTGL----YRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR---------LLGLDGEADP-A 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 544 KVREMVynaAKMSNAHdfvsalpegyETNVGERGFL---LSGGQKQRIAIARAIVSDPKILLLDEatsaldtksegvvQA 620
Cdd:COG4615 432 RARELL---ERLELDH----------KVSVEDGRFSttdLSQGQRKRLALLVALLEDRPILVFDE-------------WA 485
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 407923078 621 AlD-----RA-----------AQGRTTIVIAHRLSTIKTADKIVVMSQGRIVE 657
Cdd:COG4615 486 A-DqdpefRRvfytellpelkARGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
451-664 |
2.37e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.12 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 451 NGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLR--------QQISLVQQ----EPV 518
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIArmgvvrtfQHVRLFREmtviENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 519 LFA--TTIFDNIKHGLIGT-QYEHLEHEKVREMVYNAAKMsNAHDFVSAlpegyetnvgERGfLLSGGQKQRIAIARAIV 595
Cdd:PRK11300 102 LVAqhQQLKTGLFSGLLKTpAFRRAESEALDRAATWLERV-GLLEHANR----------QAG-NLAYGQQRRLEIARCMV 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 596 SDPKILLLDEATSALDTKSEGVVQAALD--RAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNEL 664
Cdd:PRK11300 170 TQPEILMLDEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
436-664 |
3.56e-17 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 81.65 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQElNLHWLRQQISLVQQ 515
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 516 EPVL-FATTIFDN--IKHGLIGTQYEHLEhEKVREMVYNAAKMSNAHDFVSALpegyetnvgergfllSGGQKQRIAIAR 592
Cdd:cd03265 81 DLSVdDELTGWENlyIHARLYGVPGAERR-ERIDELLDFVGLLEAADRLVKTY---------------SGGMRRRLEIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 593 AIVSDPKILLLDEATSALDTKS-EGV---VQAALDRaaQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNEL 664
Cdd:cd03265 145 SLVHRPEVLFLDEPTIGLDPQTrAHVweyIEKLKEE--FGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
814-1048 |
4.16e-17 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 83.24 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 814 KLRSEANFWSLMYLMLALtqLISFTGQGLCF-------AICSEKLIHRVRDTAFRTMLRQDISFFDqeENSAGALTSFLS 886
Cdd:cd18552 28 DIFVEKDLEALLLVPLAI--IGLFLLRGLASylqtylmAYVGQRVVRDLRNDLFDKLLRLPLSFFD--RNSSGDLISRIT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 887 TETTSLAGLSGATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVllaCGFLRFWILARFEQRSKKAYEKSA---SY 963
Cdd:cd18552 104 NDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPL---AALPIRRIGKRLRKISRRSQESMGdltSV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 964 ACEATSAIRTVASLTREEDVYASYHQQLvdqgAKNLRSILKSSTLYALSQSGMFLCTALGF----WYGGTLISKGEYSLF 1039
Cdd:cd18552 181 LQETLSGIRVVKAFGAEDYEIKRFRKAN----ERLRRLSMKIARARALSSPLMELLGAIAIalvlWYGGYQVISGELTPG 256
|
....*....
gi 407923078 1040 QFFVCFSAI 1048
Cdd:cd18552 257 EFISFITAL 265
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1102-1202 |
4.38e-17 |
|
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: 81.38 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPEQ-PVLRGLNLSVKPGQYVALVGASGCGKST---TIALLERfynPLTGGIYADGKEISSLNIND-- 1175
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKEla 77
|
90 100 110
....*....|....*....|....*....|...
gi 407923078 1176 --YRSYIALVSQE----PTLyqgTIRDNILLGA 1202
Cdd:cd03255 78 afRRRHIGFVFQSfnllPDL---TALENVELPL 107
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
432-664 |
4.64e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 84.70 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVkhiYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHwlRQQIS 511
Cdd:PRK11000 4 VTLRNV---TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQEPVLFA-TTIFDNIKHGLigtQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQRIAI 590
Cdd:PRK11000 79 MVFQSYALYPhLSVAENMSFGL---KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 591 ARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAH-RLSTIKTADKIVVMSQGRIVEQGTHNEL 664
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1102-1187 |
5.49e-17 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 85.73 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRP--EQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN---INDY 1176
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90
....*....|.
gi 407923078 1177 RSYIALVSQEP 1187
Cdd:COG1123 341 RRRVQMVFQDP 351
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1103-1185 |
5.50e-17 |
|
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: 79.21 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1103 EFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIAL 1182
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
...
gi 407923078 1183 VSQ 1185
Cdd:cd00267 78 VPQ 80
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
450-682 |
6.42e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 450 MNGVDLVVEAGKTTALVGASGSGKSTIV----GLVERFYDPvGGEVLLDGVNVQ------------ELNLHWLRQQISLV 513
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSA-GSHIELLGRTVQregrlardirksRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 514 QQepvlfaTTIFDNIKHGLIGTQ---------YEHLEHEKVREMVYNAAKMSNAHDFVSALpegyetnvgergfllSGGQ 584
Cdd:PRK09984 99 NR------LSVLENVLIGALGSTpfwrtcfswFTREQKQRALQALTRVGMVHFAHQRVSTL---------------SGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 585 KQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQGTH 661
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSS 237
|
250 260
....*....|....*....|....*
gi 407923078 662 ----NELLERKQAYYNLVEAQRIAA 682
Cdd:PRK09984 238 qqfdNERFDHLYRSINRVEENAKAA 262
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
848-1058 |
7.87e-17 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 82.53 E-value: 7.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 848 SEKLIHRVRDTAFRTMLRQDISFFdqEENSAGALTSFLSTETTSLAGLSGATLGTIFTVLTTLIGALVLGIAIGWKLGLV 927
Cdd:cd18575 64 GERVVADLRKAVFAHLLRLSPSFF--ETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 928 CASTIPVLLacgfLRFWILARFEQR-SKKAYEK---SASYACEATSAIRTVASLTREEDVYASYHQQLVDQGAKNLRSIL 1003
Cdd:cd18575 142 VLLVIPLVV----LPIILFGRRVRRlSRASQDRladLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIR 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 1004 KSSTLYALSQSGMFLCTALGFWYGGTLISKGEYS---LFQFfvCFSAItFGAQSAGTI 1058
Cdd:cd18575 218 ARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSageLSQF--VFYAV-LAAGSVGAL 272
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1102-1187 |
8.12e-17 |
|
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: 81.01 E-value: 8.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRP-EQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN---INDYR 1177
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90
....*....|
gi 407923078 1178 SYIALVSQEP 1187
Cdd:cd03257 82 KEIQMVFQDP 91
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
446-672 |
1.21e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.29 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 446 EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN---LHWLRQQISLVQQEPvlFAT 522
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDP--YAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 523 -----TIFDNIK-----HGLigtqyehLEHEKVREMVynaakmSNAHDFVSALPEGYETNVGErgflLSGGQKQRIAIAR 592
Cdd:PRK10261 414 ldprqTVGDSIMeplrvHGL-------LPGKAAAARV------AWLLERVGLLPEHAWRYPHE----FSGGQRQRICIAR 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 593 AIVSDPKILLLDEATSALDTKSEG-VVQAALD-RAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNELLERKQ 669
Cdd:PRK10261 477 ALALNPKVIIADEAVSALDVSIRGqIINLLLDlQRDFGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
...
gi 407923078 670 AYY 672
Cdd:PRK10261 557 HPY 559
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
822-1038 |
1.22e-16 |
|
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: 82.05 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 822 WSLMYLMLALTQLISFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTETTSLAGLSGATLG 901
Cdd:cd18544 43 LALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDR--TPVGRLVTRVTNDTEALNELFTSGLV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 902 TIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLlacgflrFWILARFEQRSKKAYEK-----SA--SYACEATSAIRTV 974
Cdd:cd18544 121 TLIGDLLLLIGILIAMFLLNWRLALISLLVLPLL-------LLATYLFRKKSRKAYREvreklSRlnAFLQESISGMSVI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 975 ASLTREEDVYASYH---QQLVDQgakNLRSILKSSTLYALSQSGMFLCTALGFWYGGTLISKGEYSL 1038
Cdd:cd18544 194 QLFNREKREFEEFDeinQEYRKA---NLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTL 257
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
451-655 |
1.28e-16 |
|
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: 79.01 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 451 NGVDLVVEAGKTTALVGASGSGKS----TIVGLVErfydPVGGEVLLDGVNVQELNLH-WLRQQISLVQQepvlfattif 525
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTelaeALFGLRP----PASGEITLDGKPVTRRSPRdAIRAGIAYVPE---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 526 DNIKHGLIGTQyehleheKVREmvynaakmsNAhdfvsALPegyetnvgergFLLSGGQKQRIAIARAIVSDPKILLLDE 605
Cdd:cd03215 83 DRKREGLVLDL-------SVAE---------NI-----ALS-----------SLLSGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 606 ATSALD--TKSEgVVQAALDRAAQGRTTIVIahrlST-----IKTADKIVVMSQGRI 655
Cdd:cd03215 131 PTRGVDvgAKAE-IYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1102-1216 |
1.55e-16 |
|
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: 79.44 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPEQ--PVLRGLNLSVKPGQYVALVGASGCGKSTTI-ALL-ErfYNPLTGGIYADGKeisslnindyr 1177
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLsALLgE--LEKLSGSVSVPGS----------- 67
|
90 100 110
....*....|....*....|....*....|....*....
gi 407923078 1178 syIALVSQEPTLYQGTIRDNILLGADRENVPEEAIIKAC 1216
Cdd:cd03250 68 --IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKAC 104
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1102-1188 |
1.69e-16 |
|
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: 80.62 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPE-QPVLRGLNLSVKPGQYVALVGASGCGKST---TIALLERfynPLTGGIYADGKEISSLNINDYR 1177
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTllrALAGLER---PWSGEVTFDGRPVTRRRRKAFR 78
|
90
....*....|.
gi 407923078 1178 SYIALVSQEPT 1188
Cdd:COG1124 79 RRVQMVFQDPY 89
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1098-1212 |
1.71e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 82.45 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1098 MEGHIEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTT---IALLERfynPLTGGIYADGKEISSLNIN 1174
Cdd:COG3842 2 AMPALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLlrmIAGFET---PDSGRILLDGRDVTGLPPE 75
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 407923078 1175 DyRSyIALVSQE----PTLyqgTIRDNILLGADRENVPEEAI 1212
Cdd:COG3842 76 K-RN-VGMVFQDyalfPHL---TVAENVAFGLRMRGVPKAEI 112
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
448-668 |
2.01e-16 |
|
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: 81.05 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 448 TVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDpVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDN 527
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 528 IK-HGligtQYEHLEHEKVREMVynaakmsNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEA 606
Cdd:cd03289 97 LDpYG----KWSDEEIWKVAEEV-------GLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 607 TSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHNELLERK 668
Cdd:cd03289 166 SAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
432-668 |
2.25e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.19 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPevtVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQElNLHWLRQQIS 511
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 512 LVQQepvlfattiFDNikhgligtqyehLEHE-KVRE--MVYNAAKMSNAHDFVSALPE-----GYETNVGERGFLLSGG 583
Cdd:PRK13536 118 VVPQ---------FDN------------LDLEfTVREnlLVFGRYFGMSTREIEAVIPSllefaRLESKADARVSDLSGG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 584 QKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALdRA--AQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGT 660
Cdd:PRK13536 177 MKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL-RSllARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGR 255
|
....*...
gi 407923078 661 HNELLERK 668
Cdd:PRK13536 256 PHALIDEH 263
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
409-660 |
2.27e-16 |
|
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: 85.07 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 409 IDRVSPL-----DPTSKEG-------RRLENLQGRVELRQVKHIY-PS-RPEVTVMNgvdLVVEAGKTTALVGASGSGKS 474
Cdd:TIGR01257 894 LEKTEPLteemeDPEHPEGindsffeRELPGLVPGVCVKNLVKIFePSgRPAVDRLN---ITFYENQITAFLGHNGAGKT 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 475 TIVGLVERFYDPVGGEVLLDGVNVqELNLHWLRQQISLVQQEPVLFattifdnikHGLigTQYEH-LEHEKVREMVYNAA 553
Cdd:TIGR01257 971 TTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILF---------HHL--TVAEHiLFYAQLKGRSWEEA 1038
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 554 KMSnahdfVSALPE--GYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTT 631
Cdd:TIGR01257 1039 QLE-----MEAMLEdtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTI 1113
|
250 260 270
....*....|....*....|....*....|
gi 407923078 632 IVIAHRLSTIKT-ADKIVVMSQGRIVEQGT 660
Cdd:TIGR01257 1114 IMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
448-669 |
2.29e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 79.94 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 448 TVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVERfydpVGGEVLLDGVNVQELNLHW-LRQQISLVQQEPVLFAT 522
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 523 -TIFDN------IKHGLIGTQYEHLEHEKVREmvYNAAKMSNahdfvsalpegyetNVGERgflLSGGQKQRIAIARAIV 595
Cdd:PRK10895 93 lSVYDNlmavlqIRDDLSAEQREDRANELMEE--FHIEHLRD--------------SMGQS---LSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 596 SDPKILLLDEATSALDTKS----EGVVQAALDRaaqGRTTIVIAHRL-STIKTADKIVVMSQGRIVEQGTHNELLERKQ 669
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISvidiKRIIEHLRDS---GLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1098-1219 |
2.61e-16 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 83.41 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1098 MEGHIEFRNVHFRYPTRPEqPVLRGLNLSVKPGQYVALVGASGCGKSTT---IALLERFYNPLTGGIYADGKEISSLNIN 1174
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDV-PAVDGVSLTIAPGETVALVGESGSGKSTLalaLMGLLPHGGRISGEVLLDGRDLLELSEA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 407923078 1175 DYRSYIALVSQEPT--LYQGTIRDNILLGADRENVPEEAIIKACKDA 1219
Cdd:COG1123 80 LRGRRIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLEL 126
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
434-656 |
3.28e-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: 83.34 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 434 LRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYdPVG---GEVLLDGVNVQELNLHWL-RQQ 509
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTeRAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEPVLFAT-TIFDNIkhgLIGTQYEHleheKVREMVYNAAKMsNAHDF-----VSALPEgyETNVGERGfllsGG 583
Cdd:TIGR02633 80 IVIIHQELTLVPElSVAENI---FLGNEITL----PGGRMAYNAMYL-RAKNLlrelqLDADNV--TRPVGDYG----GG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 584 QKQRIAIARAIVSDPKILLLDEATSAL-DTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKT-ADKIVVMSQGRIV 656
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1102-1212 |
3.94e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 81.27 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTT---IALLERfynpLTGG-IYADGKEISSLNINDyR 1177
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmIAGLED----PTSGeILIGGRDVTDLPPKD-R 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 407923078 1178 SyIALVSQEPTLY-QGTIRDNILLGADRENVPEEAI 1212
Cdd:COG3839 76 N-IAMVFQSYALYpHMTVYENIAFPLKLRKVPKAEI 110
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
359-653 |
6.70e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 359 RYLvKGEMSLSDVLTILLAV--MIGAFSL-----GNIGPWlqafttataaaskmYSTIDRVSPLD--------PTSKEGR 423
Cdd:COG4178 290 RYF-AGEITLGGLMQAASAFgqVQGALSWfvdnyQSLAEW--------------RATVDRLAGFEealeaadaLPEAASR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 424 RLENLQGRVELRQVKhIYPSRPEVTVmNGVDLVVEAGKTTALVGASGSGKST----IVGL-------VERfydPVGGEVL 492
Cdd:COG4178 355 IETSEDGALALEDLT-LRTPDGRPLL-EDLSLSLKPGERLLITGPSGSGKSTllraIAGLwpygsgrIAR---PAGARVL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 493 LdgvnvqelnlhwlrqqislVQQEPVLFATTIFDNIKHGLIGTQYEHLEHEKVREMVynaakmsNAHDFVSALPEgyETN 572
Cdd:COG4178 430 F-------------------LPQRPYLPLGTLREALLYPATAEAFSDAELREALEAV-------GLGHLAERLDE--EAD 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 573 VGERgflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVMSQ 652
Cdd:COG4178 482 WDQV---LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTG 558
|
.
gi 407923078 653 G 653
Cdd:COG4178 559 D 559
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1102-1203 |
6.97e-16 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 78.57 E-value: 6.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSlNINDYRSYIA 1181
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100
....*....|....*....|...
gi 407923078 1182 LVSQEPTLYQG-TIRDNILLGAD 1203
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFAR 99
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
111-389 |
1.16e-15 |
|
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: 79.13 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 111 ICAIAAGAVLPLMTVVFGSLSGTFQGMFQGTmsNGEFNDELVKFV--LYFVYLFIGEFFTCYIATVGwiYVGERISSRIR 188
Cdd:cd18574 3 LSALAAALVNIQIPLLLGDLVNVISRSLKET--NGDFIEDLKKPAlkLLGLYLLQSLLTFAYISLLS--VVGERVAARLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 189 EYYLSAILRQNVGYFDKLGAGEITTRITADanlVQDGISEKVGLVQQSLATFiTAFVIGFVKYW----KLTLILCSTIFA 264
Cdd:cd18574 79 NDLFSSLLRQDIAFFDTHRTGELVNRLTAD---VQEFKSSFKQCVSQGLRSV-TQTVGCVVSLYlispKLTLLLLVIVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 265 IVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLVIAEywgkKMKTVLASMLGA--M 342
Cdd:cd18574 155 VVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAA----KLNEKLGLGIGIfqG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 407923078 343 MTIVYLNyGLA---FWMGSRYLVKGEMSLSDVLTILLAVMIGAFSLGNIG 389
Cdd:cd18574 231 LSNLALN-GIVlgvLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLS 279
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
183-638 |
2.12e-15 |
|
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: 81.88 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 183 ISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKV-GLVQQSLATFITAFVIGFVKYWkltlILCST 261
Cdd:TIGR01271 956 VSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLfDFIQLTLIVLGAIFVVSVLQPY----IFIAA 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 262 I-FAIVFTMGggSTFIMKYNKQ--SLASYALGgTVVEEVFSSIR---NAVAFGTQDKLA----RQYNEHLVIaeyWGKKM 331
Cdd:TIGR01271 1032 IpVAVIFIML--RAYFLRTSQQlkQLESEARS-PIFSHLITSLKglwTIRAFGRQSYFEtlfhKALNLHTAN---WFLYL 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 332 KTVLASMLGAMMTIVYLNYGLAFW-MGSRYLVKGEMSLsdvltILLAVMigafslgNIGPWLQAFTTATAAASKMYSTID 410
Cdd:TIGR01271 1106 STLRWFQMRIDIIFVFFFIAVTFIaIGTNQDGEGEVGI-----ILTLAM-------NILSTLQWAVNSSIDVDGLMRSVS 1173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 411 RVSPLDPTSKEGRRLENLQGR--------VELRQVKHIYPSRPEVTVMN--------------GVDLVVEAGKTTALVGA 468
Cdd:TIGR01271 1174 RVFKFIDLPQEEPRPSGGGGKyqlstvlvIENPHAQKCWPSGGQMDVQGltakyteagravlqDLSFSVEGGQRVGLLGR 1253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 469 SGSGKSTIVGLVERFYDpVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFATTIFDNIKHGligTQYEHLEHEKVREM 548
Cdd:TIGR01271 1254 TGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPY---EQWSDEEIWKVAEE 1329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 549 VynaakmsNAHDFVSALPEGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQG 628
Cdd:TIGR01271 1330 V-------GLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN 1402
|
490
....*....|
gi 407923078 629 RTTIVIAHRL 638
Cdd:TIGR01271 1403 CTVILSEHRV 1412
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
442-659 |
2.26e-15 |
|
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: 76.15 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 442 PSRPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVERFYDpVGGEVLLDGVNVQELNLHWlRQQISLVQQEP 517
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVS-VEGDIHYNGIPYKEFAEKY-PGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 518 VLFAT-TifdnikhgligtqyehlehekVREMVYNAAKMsNAHDFVsalpegyetnvgeRGFllSGGQKQRIAIARAIVS 596
Cdd:cd03233 93 VHFPTlT---------------------VRETLDFALRC-KGNEFV-------------RGI--SGGERKRVSIAEALVS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407923078 597 DPKILLLDEATSALDTKSegvvqaALDRA--------AQGRTTIVIAHRLS--TIKTADKIVVMSQGRIVEQG 659
Cdd:cd03233 136 RASVLCWDNSTRGLDSST------ALEILkcirtmadVLKTTTFVSLYQASdeIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1103-1185 |
2.34e-15 |
|
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: 75.55 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1103 EFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIAL 1182
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
...
gi 407923078 1183 VSQ 1185
Cdd:cd03214 78 VPQ 80
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
419-679 |
4.85e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 4.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 419 SKEGRRLENLQGRVELRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGvnv 498
Cdd:COG1134 11 SKSYRLYHEPSRSLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 499 qelNLHWLrqqISLvqqepvlfaTTIF-------DNIK-----HGLIGTQYEhlehEKVREMVynaakmsnahDFvsalp 566
Cdd:COG1134 88 ---RVSAL---LEL---------GAGFhpeltgrENIYlngrlLGLSRKEID----EKFDEIV----------EF----- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 567 egyeTNVGErgFL------LSGGQKQRIAIARAIVSDPKILLLDEATSALDT----KSEGVVQaalDRAAQGRTTIVIAH 636
Cdd:COG1134 134 ----AELGD--FIdqpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLARIR---ELRESGRTVIFVSH 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 407923078 637 RLSTIKT-ADKIVVMSQGRIVEQGTHNELLErkqAYYNLVEAQR 679
Cdd:COG1134 205 SMGAVRRlCDRAIWLEKGRLVMDGDPEEVIA---AYEALLAGRE 245
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
419-659 |
7.55e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 75.26 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 419 SKEGRRLENLQGRVELRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGvnv 498
Cdd:cd03220 7 SKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 499 qelnlhwlrqQISlvqqePVLFATTIF-------DNIKhgLIGTQYEHleheKVREMvynAAKMSNAHDFvSALPEGYET 571
Cdd:cd03220 84 ----------RVS-----SLLGLGGGFnpeltgrENIY--LNGRLLGL----SRKEI---DEKIDEIIEF-SELGDFIDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 572 NVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTK-SEGVVQAALDRAAQGRTTIVIAHRLSTIK-TADKIVV 649
Cdd:cd03220 139 PVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKrLCDRALV 214
|
250
....*....|
gi 407923078 650 MSQGRIVEQG 659
Cdd:cd03220 215 LEKGKIRFDG 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
422-656 |
8.62e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.52 E-value: 8.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 422 GRRLENL-------QGRVELRqVKHIypSRPEVTvmNGVDLVVEAGKTTALVGASGSGKS----TIVGLverfYDPVGGE 490
Cdd:COG1129 238 GRELEDLfpkraaaPGEVVLE-VEGL--SVGGVV--RDVSFSVRAGEILGIAGLVGAGRTelarALFGA----DPADSGE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 491 VLLDGvnvQELNLH----WLRQQISLV----QQEPVLFATTIFDNI---------KHGLIGTQyehLEHEKVREMVynaa 553
Cdd:COG1129 309 IRLDG---KPVRIRsprdAIRAGIAYVpedrKGEGLVLDLSIRENItlasldrlsRGGLLDRR---RERALAEEYI---- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 554 kmsnahdfvSAL---PEGYETNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSEgvVQAALDR-AAQ 627
Cdd:COG1129 379 ---------KRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAE--IYRLIRElAAE 443
|
250 260 270
....*....|....*....|....*....|....
gi 407923078 628 GRTTIVIahrlST-----IKTADKIVVMSQGRIV 656
Cdd:COG1129 444 GKAVIVI----SSelpelLGLSDRILVMREGRIV 473
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
436-659 |
8.63e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 8.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNlHWLRQQ--ISLV 513
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQlgIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 514 QQE-PVLFATTIFDNIKHGLIGTQyehleheKV--------REMVYNAAKMSNAHDFVSALpegyETNVGErgflLSGGQ 584
Cdd:PRK09700 86 YQElSVIDELTVLENLYIGRHLTK-------KVcgvniidwREMRVRAAMMLLRVGLKVDL----DEKVAN----LSISH 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 585 KQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTIK-TADKIVVMSQGRIVEQG 659
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQlRKEGTAIVYISHKLAEIRrICDRYTVMKDGSSVCSG 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
448-665 |
1.41e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 448 TVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEpvlfATTIFDN 527
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN----ATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 528 IKHGLIGT-QYEHlehekvrEMVYNAAKMSNAHDFVSALPEGYETNVGERGF-LLSGGQKQRIAIARAIVSDPKILLLDE 605
Cdd:PRK10253 97 TVQELVARgRYPH-------QPLFTRWRKEDEEAVTKAMQATGITHLADQSVdTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 606 ATSALDTKSE---GVVQAALDRaAQGRTTIVIAHRLS-TIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK10253 170 PTTWLDISHQidlLELLSELNR-EKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
843-1035 |
1.92e-14 |
|
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: 75.24 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 843 CFAICSEKLIHRVRDTAFRTMLRQDISFFDqeENSAGALTSFLSTETTslagLSGATLGTIFT-----VLTTLIGALVLg 917
Cdd:cd18573 64 LLRIAGERIVARLRKRLFKSILRQDAAFFD--KNKTGELVSRLSSDTS----VVGKSLTQNLSdglrsLVSGVGGIGMM- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 918 IAIGWKLGLVCASTIPVLLACGFL--RFwiLARFEQRSKKAYEKSASYACEATSAIRTVASLTREEDVYASYHQQlvdqg 995
Cdd:cd18573 137 LYISPKLTLVMLLVVPPIAVGAVFygRY--VRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKK----- 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 407923078 996 aknLRSILKSSTLYALSQSGMFLCTALG--------FWYGGTLISKGE 1035
Cdd:cd18573 210 ---VDEVFDLAKKEALASGLFFGSTGFSgnlsllsvLYYGGSLVASGE 254
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
104-376 |
2.07e-14 |
|
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: 75.52 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 104 IIIVVSSICAIAAGAVLPLM-----TVVFGSLSGTFQGMFQGtmsngefndeLVKFVLYFVYLFIGEFFTCYIATVGWIY 178
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLlgkaiDLIIEGLGGGGGVDFSG----------LLRILLLLLGLYLLSALFSYLQNRLMAR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 179 VGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEkvGLVQ--QSLATFITAFVIGFVKYWKLTL 256
Cdd:cd18547 72 VSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQ--SLTQliSSILTIVGTLIMMLYISPLLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 257 I-LCSTIFAIVFTMgggstFIMK-----YNKQSLASYALGGTvVEEVFSSIRNAVAFGTQDKLARQ---YNEHLVIAEYW 327
Cdd:cd18547 150 IvLVTVPLSLLVTK-----FIAKrsqkyFRKQQKALGELNGY-IEEMISGQKVVKAFNREEEAIEEfdeINEELYKASFK 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 407923078 328 GkkmkTVLASMLG-AMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVLTILL 376
Cdd:cd18547 224 A----QFYSGLLMpIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQ 269
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1102-1201 |
2.26e-14 |
|
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: 73.33 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKST---TIALLERfynPLTGGIYADGKEI--SSLNINDY 1176
Cdd:cd03262 1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTIIIDGLKLtdDKKNINEL 74
|
90 100
....*....|....*....|....*.
gi 407923078 1177 RSYIALVSQEPTLY-QGTIRDNILLG 1201
Cdd:cd03262 75 RQKVGMVFQQFNLFpHLTVLENITLA 100
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1098-1200 |
2.43e-14 |
|
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: 73.86 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1098 MEGHIEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKST---TIALLERfynPLTGGIYADGKEISSLN-- 1172
Cdd:COG1127 2 SEPMIEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVllkLIIGLLR---PDSGEILVDGQDITGLSek 75
|
90 100 110
....*....|....*....|....*....|
gi 407923078 1173 -INDYRSYIALVSQEPTLYQG-TIRDNILL 1200
Cdd:COG1127 76 eLYELRRRIGMLFQGGALFDSlTVFENVAF 105
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
453-659 |
2.44e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.07 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 453 VDLVVEAGKTTALVGASGSGKST----IVGLV--ERFYDPVGGEVLLDgvNVQELNLHWLRQQISLVQQEPVLFAttifd 526
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSlinaISGLTrpQKGRIVLNGRVLFD--AEKGICLPPEKRRIGYVFQDARLFP----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 527 nikhgligtqyehleHEKVR-EMVYNAAKMSNAH--DFVSALpeGYETNVGERGFLLSGGQKQRIAIARAIVSDPKILLL 603
Cdd:PRK11144 90 ---------------HYKVRgNLRYGMAKSMVAQfdKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 604 DEATSALDT--KSEgvVQAALDRAAQG-RTTIV-IAHRLSTI-KTADKIVVMSQGRIVEQG 659
Cdd:PRK11144 153 DEPLASLDLprKRE--LLPYLERLAREiNIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1098-1219 |
2.48e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.77 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1098 MEGHIEFRNVHFRYPTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYR 1177
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 407923078 1178 SYIALVSQEP--TLYQGTIRDNILLGADRENVPEEAIIKACKDA 1219
Cdd:PRK13650 81 HKIGMVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEA 124
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
830-1038 |
3.21e-14 |
|
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: 74.86 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 830 ALTQLISFtGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTETTSLAGLSGATLGTIFTVLTT 909
Cdd:cd18564 65 LLRGLASY-AGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDR--RRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 910 LIGALVLGIAIGWKLGLVCASTIPVLlacgflrFWILARFEQRSKKAYEKS-------ASYACEATSAIRTVASLTREED 982
Cdd:cd18564 142 LVGMLGVMFWLDWQLALIALAVAPLL-------LLAARRFSRRIKEASREQrrregalASVAQESLSAIRVVQAFGREEH 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 983 VyasyHQQLVDQGAKNLRSILKSSTLYALSQSG----MFLCTALGFWYGGTLISKGEYSL 1038
Cdd:cd18564 215 E----ERRFARENRKSLRAGLRAARLQALLSPVvdvlVAVGTALVLWFGAWLVLAGRLTP 270
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
829-1038 |
3.72e-14 |
|
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: 74.39 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 829 LALTQLISFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTETTSLAGLSGATLGTIFTVLT 908
Cdd:cd18551 45 LFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDR--RRSGDLVSRVTNDTTLLRELITSGLPQLVTGVL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 909 TLIGALVLGIAIGWKLGLVCASTIPVLlacGFLRFWILARFEQRSKKAYEKSA---SYACEATSAIRTVASLTREEDVYA 985
Cdd:cd18551 123 TVVGAVVLMFLLDWVLTLVTLAVVPLA---FLIILPLGRRIRKASKRAQDALGelsAALERALSAIRTVKASNAEERETK 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 986 SyhqqlVDQGAKNLRSI-LKSSTLYA----LSQSGMFLCTALGFWYGGTLISKGEYSL 1038
Cdd:cd18551 200 R-----GGEAAERLYRAgLKAAKIEAligpLMGLAVQLALLVVLGVGGARVASGALTV 252
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1098-1229 |
4.02e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 74.36 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1098 MEGHIEFRNVHFRYPTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYR 1177
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 1178 SYIALVSQEP--TLYQGTIRDNILLGADRENVPEEAIIKACKDA----NIYDFIMSLP 1229
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEAllavNMLDFKTREP 138
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1102-1219 |
5.35e-14 |
|
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: 72.29 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDyRSyIA 1181
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IA 75
|
90 100 110
....*....|....*....|....*....|....*....
gi 407923078 1182 LVSQEPTLY-QGTIRDNILLGADRENVPEEAIIKACKDA 1219
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGLKLRKVPKDEIDERVREV 114
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
443-635 |
5.63e-14 |
|
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: 72.01 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 443 SRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFAT 522
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 523 TIFDNIkhgligtQYEHLEHEKVREMVYNAAKMSNAHDFvSALPEGYetnvgergflLSGGQKQRIAIARAIVSDPKILL 602
Cdd:TIGR01189 89 SALENL-------HFWAAIHGGAQRTIEDALAAVGLTGF-EDLPAAQ----------LSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190
....*....|....*....|....*....|....
gi 407923078 603 LDEATSALDtkSEGVVQ-AALDRAAQGRTTIVIA 635
Cdd:TIGR01189 151 LDEPTTALD--KAGVALlAGLLRAHLARGGIVLL 182
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
143-388 |
6.05e-14 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 73.98 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 143 SNGEFNDELVKFVLYFVYLFIGEFFTCYIATVGWIYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLV 222
Cdd:cd18541 31 AGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 223 QDGISEkvGLVQ--QSLATFITAFVIGFVKYWKLTLILCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSS 300
Cdd:cd18541 111 RMALGP--GILYlvDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 301 IRnaV--AFGTQDKLARQYNEhlVIAEYWGKKMKTV-LASMLGAMMT-IVYLNYGLAFWMGSRYLVKGEMSLSDV--LTI 374
Cdd:cd18541 189 IR--VikAFVQEEAEIERFDK--LNEEYVEKNLRLArVDALFFPLIGlLIGLSFLIVLWYGGRLVIRGTITLGDLvaFNS 264
|
250
....*....|....*
gi 407923078 375 LLAVMIG-AFSLGNI 388
Cdd:cd18541 265 YLGMLIWpMMALGWV 279
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
436-668 |
6.78e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.14 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGlvERFYDPVGGEVLLDGVNVQELNLHwLRQQ-- 509
Cdd:CHL00131 9 EIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTlskvIAG--HPAYKILEGDILFKGESILDLEPE-ERAHlg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEPVL--------FATTIFDNIKHGLIGTQYEHLEHEKVremvynaakMSNAHDFVSALPEGYETNVGErGFllS 581
Cdd:CHL00131 86 IFLAFQYPIEipgvsnadFLRLAYNSKRKFQGLPELDPLEFLEI---------INEKLKLVGMDPSFLSRNVNE-GF--S 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 582 GGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAH--RLSTIKTADKIVVMSQGRIVEQ 658
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKT 233
|
250
....*....|..
gi 407923078 659 GTHN--ELLERK 668
Cdd:CHL00131 234 GDAElaKELEKK 245
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1102-1198 |
7.10e-14 |
|
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: 72.53 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKST---TIALLERfynPLTGGIYADGKEISSLNINDY-- 1176
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTllrLIVGLLR---PDSGEVLIDGEDISGLSEAELyr 74
|
90 100
....*....|....*....|....
gi 407923078 1177 -RSYIALVSQEPTLYQG-TIRDNI 1198
Cdd:cd03261 75 lRRRMGMLFQSGALFDSlTVFENV 98
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
437-659 |
7.88e-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: 72.37 E-value: 7.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 437 VKHIY-PSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGvnvqelNLHWlRQQISLVQQ 515
Cdd:cd03267 23 LKSLFkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPW-KRRKKFLRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 516 EPVLFA--TTIFDNIKhglIGTQYEHLEHekvremVYN---AAKMSNAHDFVSALPEGYETNVGERGflLSGGQKQRIAI 590
Cdd:cd03267 96 IGVVFGqkTQLWWDLP---VIDSFYLLAA------IYDlppARFKKRLDELSELLDLEELLDTPVRQ--LSLGQRMRAEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 591 ARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVI--AHRLSTI-KTADKIVVMSQGRIVEQG 659
Cdd:cd03267 165 AAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1096-1223 |
8.91e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 72.76 E-value: 8.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1096 NNMEGHIEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFY--NP---LTGGIYADGKEI-- 1168
Cdd:COG1117 6 STLEPKIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPgarVEGEILLDGEDIyd 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 1169 SSLNINDYRSYIALVSQEPTLYQGTIRDNILLGA------DRENVpEEAIIKACKDANIYD 1223
Cdd:COG1117 83 PDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgikSKSEL-DEIVEESLRKAALWD 142
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
182-351 |
1.05e-13 |
|
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: 73.11 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 182 RISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTlILCST 261
Cdd:cd18784 66 RLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLS-LVTLI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 262 IFAIVFTMG---GgsTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLVIAEYWGKKMKTVLAS- 337
Cdd:cd18784 145 GLPLIAIVSkvyG--DYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGy 222
|
170
....*....|....*....
gi 407923078 338 -----MLGAMMTIVYLNYG 351
Cdd:cd18784 223 vwsneLTELALTVSTLYYG 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
444-672 |
1.19e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.66 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 444 RPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEV-----LLDGVNVQELNLHWLRQQ--------- 509
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSRQVIELSEQSAAqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEPVLFATTIF-------DNIK-HGLIGTQYEHLEHEKVREMVynaaKMSNAHDFVSALPEGyetnvgergflLS 581
Cdd:PRK10261 106 MAMIFQEPMTSLNPVFtvgeqiaESIRlHQGASREEAMVEAKRMLDQV----RIPEAQTILSRYPHQ-----------LS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 582 GGQKQRIAIARAIVSDPKILLLDEATSALDTKSEG-------VVQAALDRAaqgrtTIVIAHRLSTI-KTADKIVVMSQG 653
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAqilqlikVLQKEMSMG-----VIFITHDMGVVaEIADRVLVMYQG 245
|
250
....*....|....*....
gi 407923078 654 RIVEQGTHNELLERKQAYY 672
Cdd:PRK10261 246 EAVETGSVEQIFHAPQHPY 264
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1102-1219 |
1.22e-13 |
|
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: 71.28 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPtrPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN---INDYRS 1178
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 407923078 1179 YIALVSQE-PTLYQGTIRDNILLGADRENVPEEAIIKACKDA 1219
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAA 120
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
440-659 |
1.24e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 440 IYPSRPEVTVMNG------VDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELnlhwLRQQ-ISL 512
Cdd:PRK15056 7 IVVNDVTVTWRNGhtalrdASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 513 VQQE-------PVLFATTIFDNiKHGLIGTQYEHLEHEkvREMVYNAAKMSNAHDFvsalpegYETNVGErgflLSGGQK 585
Cdd:PRK15056 83 VPQSeevdwsfPVLVEDVVMMG-RYGHMGWLRRAKKRD--RQIVTAALARVDMVEF-------RHRQIGE----LSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 586 QRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAAL-DRAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQG 659
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLrELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
452-672 |
1.24e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 72.27 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 452 GVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNL---------HWLRQQISLVQQEP---VL 519
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerrRLLRTEWGFVHQHPrdgLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 520 FATTIFDNIKHGLIGT---QYEHLEHEKVREMvynaAKMSNAHDFVSALPegyetnvgeRGFllSGGQKQRIAIARAIVS 596
Cdd:PRK11701 104 MQVSAGGNIGERLMAVgarHYGDIRATAGDWL----ERVEIDAARIDDLP---------TTF--SGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 597 DPKILLLDEATSALDTKsegvVQAA-LD--R---AAQGRTTIVIAHRLSTIK-TADKIVVMSQGRIVEQGTHNELLERKQ 669
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVS----VQARlLDllRglvRELGLAVVIVTHDLAVARlLAHRLLVMKQGRVVESGLTDQVLDDPQ 244
|
...
gi 407923078 670 AYY 672
Cdd:PRK11701 245 HPY 247
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
445-657 |
1.29e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 445 PEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYdPVG---GEVLLDGvnvQELNLHWLRQQ----ISLVQQE- 516
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDG---EVCRFKDIRDSealgIVIIHQEl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 517 ---PVLfatTIFDNI-------KHGLIGTQYEHLEHEKVREMVynaakmsnahdfvsALPEGYETNVGERGFllsgGQKQ 586
Cdd:NF040905 88 aliPYL---SIAENIflgneraKRGVIDWNETNRRARELLAKV--------------GLDESPDTLVTDIGV----GKQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407923078 587 RIAIARAIVSDPKILLLDEATSAL-DTKSEGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVE 657
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
823-1037 |
1.39e-13 |
|
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: 72.89 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 823 SLMYLMLALTQLISftgqGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTETTSLAGLSGATLGT 902
Cdd:cd18589 43 SLLTIASAVSEFVC----DLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDS--NQTGDIVSRVTTDTEDMSESLSENLSL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 903 IFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLlacgflrfWILARF--------EQRSKKAYEKSASYACEATSAIRTV 974
Cdd:cd18589 117 LMWYLARGLFLFIFMLWLSPKLALLTALGLPLL--------LLVPKFvgkfqqslAVQVQKSLARANQVAVETFSAMKTV 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 975 ASLTREEDVYASYHQQLvdQGAKNLRSilKSSTLYALSQ-----SGMFLCTALgFWYGGTLISKGEYS 1037
Cdd:cd18589 189 RSFANEEGEAQRYRQRL--QKTYRLNK--KEAAAYAVSMwtssfSGLALKVGI-LYYGGQLVTAGTVS 251
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1102-1200 |
1.84e-13 |
|
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: 71.00 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSlNINDYRSYIA 1181
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100
....*....|....*....|
gi 407923078 1182 LVSQEPTLYQG-TIRDNILL 1200
Cdd:cd03263 79 YCPQFDALFDElTVREHLRF 98
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
813-1043 |
1.89e-13 |
|
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: 72.46 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 813 GKLRSEANFWSLMYLMLALTQLISFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGAL----TS----- 883
Cdd:cd18542 32 GGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDK--ARTGDLmsrcTSdvdti 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 884 --FLSTEttslaglsgatLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLlacgflrFWILARFEQRSKKAYEKS- 960
Cdd:cd18542 110 rrFLAFG-----------LVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFI-------ALFSYVFFKKVRPAFEEIr 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 961 ------ASYACEATSAIRTVASLTREEdvyasYHQQLVDQGAKNLRSI-LKSSTLYALSQSGM-FLC---TALGFWYGGT 1029
Cdd:cd18542 172 eqegelNTVLQENLTGVRVVKAFARED-----YEIEKFDKENEEYRDLnIKLAKLLAKYWPLMdFLSglqIVLVLWVGGY 246
|
250
....*....|....
gi 407923078 1030 LISKGEYSLFQFFV 1043
Cdd:cd18542 247 LVINGEITLGELVA 260
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
432-666 |
2.53e-13 |
|
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: 74.07 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPS--RPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLL----DGVNVQE---LN 502
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKpgpDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 503 LHWLRQQISLVQQEPVLFA-TTIFDNIKHGlIGTqyehlehekvrEMVYNAAKMSNAHDFVSA-LPEGYETNVGER-GFL 579
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPhRTVLDNLTEA-IGL-----------ELPDELARMKAVITLKMVgFDEEKAEEILDKyPDE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTI-KTADKIVVMSQGRIV 656
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVlDVCDRAALMRDGKIV 507
|
250
....*....|
gi 407923078 657 EQGTHNELLE 666
Cdd:TIGR03269 508 KIGDPEEIVE 517
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
434-666 |
2.99e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.88 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 434 LRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNV--------QELNLHW 505
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 506 LRQQISLVQQepvlfaTTIFDNIKHGligtqyehlehekvREMV-----YNAAKMSNAHDFVSA---LPEGYETNVGErg 577
Cdd:PRK10762 84 IHQELNLIPQ------LTIAENIFLG--------------REFVnrfgrIDWKKMYAEADKLLArlnLRFSSDKLVGE-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 578 flLSGGQKQRIAIARAIVSDPKILLLDEATSAL-DTKSEGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRI 655
Cdd:PRK10762 142 --LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDGQF 219
|
250
....*....|.
gi 407923078 656 VEQGTHNELLE 666
Cdd:PRK10762 220 IAEREVADLTE 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1102-1215 |
3.20e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.51 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIA 1181
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110
....*....|....*....|....*....|....*
gi 407923078 1182 LVSQEPTLYQGTIRDNILLGAD-RENVPEEAIIKA 1215
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPWQiRNQQPDPAIFLD 119
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
314-676 |
3.53e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.85 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 314 ARQYNEHLVIAEY-------WGKKMktvlasMLGAMmtivylnyGLAFWMGSRYlvkGEMSLSDVLTILLAV-------- 378
Cdd:PRK10522 218 AQEYRHHIIRADTfhlsavnWSNIM------MLGAI--------GLVFYMANSL---GWADTNVAATYSLTLlflrtpll 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 379 -MIGAFslgnigPWLQAFTTATAAASKMystidRVSPLDPTSKEGRRLENLQgRVELRQVKHIYPSRP-EVtvmNGVDLV 456
Cdd:PRK10522 281 sAVGAL------PTLLSAQVAFNKLNKL-----ALAPYKAEFPRPQAFPDWQ-TLELRNVTFAYQDNGfSV---GPINLT 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 457 VEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFattifdnikHGLIGTQ 536
Cdd:PRK10522 346 IKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLF---------DQLLGPE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 537 YEHLEHEKVREMVyNAAKMSNAHDFVsalpEGYETNVGergflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEG 616
Cdd:PRK10522 417 GKPANPALVEKWL-ERLKMAHKLELE----DGRISNLK-----LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRR 486
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 617 VV-QAALDR-AAQGRTTIVIAHRLSTIKTADKIVVMSQGRIVEQGTHnellERKQAYYNLVE 676
Cdd:PRK10522 487 EFyQVLLPLlQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGE----ERDAASRDAVA 544
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1102-1187 |
3.97e-13 |
|
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: 72.01 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPEQ-PVLRGLNLSVKPGQYVALVGASGCGKSTT----IALLERfyNPLTGG-IYADGKEISSLNIND 1175
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPP--PGITSGeILFDGEDLLKLSEKE 79
|
90
....*....|....*.
gi 407923078 1176 YRSY----IALVSQEP 1187
Cdd:COG0444 80 LRKIrgreIQMIFQDP 95
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
450-653 |
4.02e-13 |
|
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: 69.19 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 450 MNGVDLVVEAGKTTALVGASGSGKSTIVG-LVERFYD-PVGGEVLLDGvnvQELNLHWLRQqISLVQQEPVlfattifdn 527
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAgVITGEILING---RPLDKNFQRS-TGYVEQQDV--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 528 ikhgligtqyeHLEHEKVREmvynaakmsnAHDFVSALpegyetnvgeRGflLSGGQKQRIAIARAIVSDPKILLLDEAT 607
Cdd:cd03232 90 -----------HSPNLTVRE----------ALRFSALL----------RG--LSVEQRKRLTIGVELAAKPSILFLDEPT 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 407923078 608 SALDTKSEGVVQAALDR-AAQGRTTIVIAHRLS--TIKTADKIVVMSQG 653
Cdd:cd03232 137 SGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1098-1224 |
4.68e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1098 MEGHIEFRNVHFRYPTRPEqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYR 1177
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 407923078 1178 SYIALVSQEP--TLYQGTIRDNIL-----LGADRENVpEEAIIKACKDANIYDF 1224
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAfgpvnMGLDKDEV-ERRVEEALKAVRMWDF 131
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
580-651 |
4.91e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 68.33 E-value: 4.91e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAaqGRTTIVIAHRLSTIKTADKIVVMS 651
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHRPSLWKFHDRVLDLD 161
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
177-376 |
5.35e-13 |
|
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: 70.96 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 177 IYVG--ERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKL 254
Cdd:cd18589 59 IYNItmSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 255 TL--ILCSTIFAIVftmgggSTFIMKYNkQSLA-----SYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLVIAEYW 327
Cdd:cd18589 139 ALltALGLPLLLLV------PKFVGKFQ-QSLAvqvqkSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRL 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 407923078 328 GKKMKTVLA-SMLGAMMTIVYLNYGLAFWmGSRYLVKGEMSLSDVLTILL 376
Cdd:cd18589 212 NKKEAAAYAvSMWTSSFSGLALKVGILYY-GGQLVTAGTVSSGDLVTFVL 260
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
457-664 |
6.50e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 71.31 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 457 VEAGKTTALVGASGSGKS----TIVGLVErFYDPVGGEVL-LDGVNVQELNLHWLRQ----QISLVQQEPVlfaTTIFDN 527
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSvsslAIMGLID-YPGRVMAEKLeFNGQDLQRISEKERRNlvgaEVAMIFQDPM---TSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 528 IKHGligtqYEHLEHEKVREMVYNAAKMSNAHDFVS--ALPEGyETNVGERGFLLSGGQKQRIAIARAIVSDPKILLLDE 605
Cdd:PRK11022 106 YTVG-----FQIMEAIKVHQGGNKKTRRQRAIDLLNqvGIPDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 606 ATSALD-TKSEGVVQAALD-RAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNEL 664
Cdd:PRK11022 180 PTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
446-665 |
6.75e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.91 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 446 EVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQelnlHW-----LRQQISLVQQEPVLF 520
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT----DWqtakiMREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 521 A-TTIFDNIKHGliGTQYEHLEHEKVREMVYNAakmsnahdfvsaLPEGYETNVgERGFLLSGGQKQRIAIARAIVSDPK 599
Cdd:PRK11614 93 SrMTVEENLAMG--GFFAERDQFQERIKWVYEL------------FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 600 ILLLDEATSALdtkSEGVVQAALDRAAQGRT---TIVIAHRLS--TIKTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK11614 158 LLLLDEPSLGL---APIIIQQIFDTIEQLREqgmTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
151-368 |
8.26e-13 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 70.54 E-value: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 151 LVKFVLYFVYLFIGEfftcyiatvgwiYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKV 230
Cdd:cd18542 50 LLRGVFRYLQGYLAE------------KASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 231 GLVQQSLATFITAFVIGFVKYWKLTLILCSTI-----FAIVFTMGGGSTFimkynkqSLASYALG--GTVVEEVFSSIRN 303
Cdd:cd18542 118 VELVRAVLLFIGALIIMFSINWKLTLISLAIIpfialFSYVFFKKVRPAF-------EEIREQEGelNTVLQENLTGVRV 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 304 AVAFGTQD----KLARQyNEhlviaEYWGKKMKT--VLASMLGAMMTIVYLNYGLAFWMGSRYLVKGEMSL 368
Cdd:cd18542 191 VKAFAREDyeieKFDKE-NE-----EYRDLNIKLakLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITL 255
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
444-635 |
1.24e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.36 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 444 RPEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLDGVNVQELNL----HWLRQQISLvqq 515
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTllrlIAGLLP----PAAGTIKLDGGDIDDPDVaeacHYLGHRNAM--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 516 EPVLfatTIFDNIK--HGLIGTQyehlehekvREMVYNAAKMSNAHDfVSALPEGYetnvgergflLSGGQKQRIAIARA 593
Cdd:PRK13539 85 KPAL---TVAENLEfwAAFLGGE---------ELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 407923078 594 IVSDPKILLLDEATSALDTKSEGVVQAAL-DRAAQGrtTIVIA 635
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAAAVALFAELIrAHLAQG--GIVIA 182
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
445-1169 |
1.53e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.45 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 445 PEVTVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQE---P 517
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDvhfP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 518 VLfatTIFDN----IKHGLIGTQYEHLEHEkvremVYnAAKMSNAHDFVSALPEGYETNVGE---RGflLSGGQKQRIAI 590
Cdd:TIGR00956 152 HL---TVGETldfaARCKTPQNRPDGVSRE-----EY-AKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 591 ARAIVSDPKILLLDEATSALDTKSegvvqaALDRAAQGRTTIVIAHRLSTI----------KTADKIVVMSQGRIVEQGT 660
Cdd:TIGR00956 221 AEASLGGAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsqdayELFDKVIVLYEGYQIYFGP 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 661 HNELLE--RKQAYynlVEAQRIAAANEkieeeeeeeeevdLTEVDDETiKRTVSPQSEKRSYSVdPDD------------ 726
Cdd:TIGR00956 295 ADKAKQyfEKMGF---KCPDRQTTADF-------------LTSLTSPA-ERQIKPGYEKKVPRT-PQEfetywrnspeya 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 727 ----DVAARLKRTQSGKS-----ESSVALAKK--QPASEQKYSLATLIKLIASfnrQEWLLMVQGLFWSIIAGGGNPTQA 795
Cdd:TIGR00956 357 qlmkEIDEYLDRCSESDTkeayrESHVAKQSKrtRPSSPYTVSFSMQVKYCLA---RNFLRMKGNPSFTLFMVFGNIIMA 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 796 vFFAKSISALSRPPSEYGKLRSEANFWSLMYLML-ALTQLISFTGQGLCFAICSEKLIHRVRDTAFRTMLRQ-------D 867
Cdd:TIGR00956 434 -LILSSVFYNLPKNTSDFYSRGGALFFAILFNAFsSLLEIASMYEARPIVEKHRKYALYHPSADAIASIISEipfkiieS 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 868 ISFF-------DQEENSAGALTSFLSTETTSLAglSGATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLLACGF 940
Cdd:TIGR00956 513 VVFNiilyfmvNFRRTAGRFFFYLLILFICTLA--MSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGW 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 941 LRfWIlarfeqrskkAYEKSASYACEatsairtvaSLTREEdvyasYH------QQLVDQGA--KNLRSILKSSTLYALS 1012
Cdd:TIGR00956 591 SK-WI----------YYVNPLAYAFE---------SLMVNE-----FHgrrfecSQYVPSGGgyDNLGVTNKVCTVVGAE 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1013 ------QSGMFLCTALGFWYGGTLISKG---EYSLFQFFVCFSAITF--GAQSAGTIFSF----APDMGKAKHAAIQLKT 1077
Cdd:TIGR00956 646 pgqdyvDGDDYLKLSFQYYNSHKWRNFGiiiGFTVFFFFVYILLTEFnkGAKQKGEILVFrrgsLKRAKKAGETSASNKN 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1078 LFDRKPEIDTWSSDGEKINNME--------GHIEF--RNVHFRYPTRPEQPV-LRGLNLSVKPGQYVALVGASGCGKSTT 1146
Cdd:TIGR00956 726 DIEAGEVLGSTDLTDESDDVNDekdmekesGEDIFhwRNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTTL 805
|
810 820
....*....|....*....|....
gi 407923078 1147 I-ALLERfynpLTGGIYADGKEIS 1169
Cdd:TIGR00956 806 LnVLAER----VTTGVITGGDRLV 825
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
443-636 |
2.07e-12 |
|
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: 67.52 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 443 SRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQQEPVLFAT 522
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 523 TIFDNIkhgligtQYEHLEHEkvREMVYNAAKMSNAHDFvSALPEGYetnvgergflLSGGQKQRIAIARAIVSDPKILL 602
Cdd:cd03231 89 SVLENL-------RFWHADHS--DEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190
....*....|....*....|....*....|....*
gi 407923078 603 LDEATSALDTKSEGVVQAAL-DRAAQGRTTIVIAH 636
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
447-723 |
2.18e-12 |
|
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: 70.99 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 447 VTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERF--YDPVGGEVL-------------------------------- 492
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 493 -LDGVNVQELNLHWLRQQISLVQQEPvlFA----TTIFDNIKHGLIGTQYEhlehekVREMVYNAAKMSNahdfvsalpe 567
Cdd:TIGR03269 93 eVDFWNLSDKLRRRIRKRIAIMLQRT--FAlygdDTVLDNVLEALEEIGYE------GKEAVGRAVDLIE---------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 568 gyETNVGER----GFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTI 641
Cdd:TIGR03269 155 --MVQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 642 -KTADKIVVMSQGRIVEQGTHNELLERKQAYYNLVEAQRIaaanekieeeeeeeeevdlTEVDDETIK-RTVSpqseKRS 719
Cdd:TIGR03269 233 eDLSDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECE-------------------VEVGEPIIKvRNVS----KRY 289
|
....
gi 407923078 720 YSVD 723
Cdd:TIGR03269 290 ISVD 293
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1102-1185 |
2.32e-12 |
|
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: 66.30 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTrpeQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIND-YRSYI 1180
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGI 77
|
....*
gi 407923078 1181 ALVSQ 1185
Cdd:cd03216 78 AMVYQ 82
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
432-667 |
2.51e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPevtVMNGVDLVVEAGKTTALVGASGSGKST----IVGLVErfydPVGGEVLLdGVNVQelnlhwlr 507
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTllklLAGELE----PDSGTVKL-GETVK-------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 508 qqISLVQQEpvlfattifdnikhgligtqYEHLEHEK-VREMVYNAAkmsnahdfvsalPEGYETNVgeRGFL------- 579
Cdd:COG0488 380 --IGYFDQH--------------------QEELDPDKtVLDELRDGA------------PGGTEQEV--RGYLgrflfsg 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 ---------LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDrAAQGrTTIVIAH-R--LSTIktADKI 647
Cdd:COG0488 424 ddafkpvgvLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRI 499
|
250 260
....*....|....*....|.
gi 407923078 648 VVMSQGRIVE-QGTHNELLER 667
Cdd:COG0488 500 LEFEDGGVREyPGGYDDYLEK 520
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
413-637 |
2.93e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 413 SPLDPTSKEGRRLENLQgrVELRQVKHiypsrpevTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFY--DPVGGE 490
Cdd:COG2401 19 SVLDLSERVAIVLEAFG--VELRVVER--------YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 491 VLLDgvnvqelNLHWLRQqislvqqepvlfaTTIFDNIkhGLIGTQYEHLEhekvremVYNAAKMSNAHDFVSALPEgye 570
Cdd:COG2401 89 VDVP-------DNQFGRE-------------ASLIDAI--GRKGDFKDAVE-------LLNAVGLSDAVLWLRRFKE--- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 571 tnvgergflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHR 637
Cdd:COG2401 137 ---------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARraGITLVVATHH 196
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
445-664 |
3.33e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 445 PEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLH-WLRQQISLVQQE----PVL 519
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 520 fatTIFDNI-------KHGLIgtqyehleheKVREMVYNAAKMSN--AHDFVSALPEGYetnvgergflLSGGQKQRIAI 590
Cdd:PRK11288 95 ---TVAENLylgqlphKGGIV----------NRRLLNYEAREQLEhlGVDIDPDTPLKY----------LSIGQRQMVEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 591 ARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEqgTHNEL 664
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAREIEQLFRVIRElRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
844-1037 |
3.45e-12 |
|
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: 68.49 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 844 FAICSEKLIHRVRDTAFRTMLRQDISFFDqeENSAGALTSFLSTETTSLAGLSGATLGTIFTVLTTLIGALVLGIAIGWK 923
Cdd:cd18784 60 FTLAMARLNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 924 LGLVCASTIPVLLACGFLRFWILARFEQRSKKAYEKSASYACEATSAIRTVASLTREEDVYASYHQQLVDQGAKNLRSIL 1003
Cdd:cd18784 138 LSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEAL 217
|
170 180 190
....*....|....*....|....*....|....*
gi 407923078 1004 kSSTLYALSQSGMFLC-TALGFWYGGTLISKGEYS 1037
Cdd:cd18784 218 -AYGGYVWSNELTELAlTVSTLYYGGHLVITGQIS 251
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1088-1229 |
6.14e-12 |
|
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: 67.24 E-value: 6.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1088 WSSDGEKINNMEGHIEFRNVHFRYPTRpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKE 1167
Cdd:cd03288 6 SGSSNSGLVGLGGEIKIHDLCVRYENN-LKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGID 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407923078 1168 ISSLNINDYRSYIALVSQEPTLYQGTIRDNIllgaDRE-NVPEEAIIKACKDANIYDFIMSLP 1229
Cdd:cd03288 85 ISKLPLHTLRSRLSIILQDPILFSGSIRFNL----DPEcKCTDDRLWEALEIAQLKNMVKSLP 143
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
823-1035 |
6.90e-12 |
|
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: 67.51 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 823 SLMYLMLALTQLISFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFdqEENSAGALTSFLSTETTSLAGLSGATLGT 902
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFH--ERETSGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 903 IFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLLAcgfLRFWilarFEQRSKKAY----EKSA---SYACEATSAIRTVA 975
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPRLALVALAALPPLAL---ATRW----FRRRSSRAYrrarERIAavnADLQETLAGIRVVQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 976 SLTREEDVYASYHQQLVDQGAKNLRSIlKSSTLY-----ALSQsgmfLCTALGFWYGGTLISKGE 1035
Cdd:cd18546 193 AFRRERRNAERFAELSDDYRDARLRAQ-RLVAIYfpgveLLGN----LATAAVLLVGAWRVAAGT 252
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
159-393 |
7.88e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 67.53 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 159 VYLFIGEFFTCYIAT--VGWI------YVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKV 230
Cdd:cd18563 42 LLLLVLGLAGAYVLSalLGILrgrllaRLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 231 GLVQQSLATFITAFVIGFVKYWKLTLILCSTIFAIVFtmggGSTFIMK-----YNKQSLASYALgGTVVEEVFSSIRNAV 305
Cdd:cd18563 122 PDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVW----GSYFFWKkirrlFHRQWRRWSRL-NSVLNDTLPGIRVVK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 306 AFGTQDKLA---RQYNEHLVIAeywGKKMKTVLASMLGAMMTIVYLnyGLAF--WMGSRYLVKGEMSLSDVLT-ILLAVM 379
Cdd:cd18563 197 AFGQEKREIkrfDEANQELLDA---NIRAEKLWATFFPLLTFLTSL--GTLIvwYFGGRQVLSGTMTLGTLVAfLSYLGM 271
|
250
....*....|....*.
gi 407923078 380 IGA--FSLGNIGPWLQ 393
Cdd:cd18563 272 FYGplQWLSRLNNWIT 287
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
437-665 |
8.06e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 67.16 E-value: 8.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 437 VKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVG-LVERFYDP-------VGGEVLLDGVNVQELNLHWL-R 507
Cdd:PRK13547 4 ADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLaR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 508 QQISLVQQEPVLFATTIFDNIkhgLIGtQYEH------LEHEKvREMVYNAAKMSNAhdfvsalpegyETNVGERGFLLS 581
Cdd:PRK13547 84 LRAVLPQAAQPAFAFSAREIV---LLG-RYPHarragaLTHRD-GEIAWQALALAGA-----------TALVGRDVTTLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 582 GGQKQRIAIARAI---------VSDPKILLLDEATSALDTKSEGVVQAALDRAAQ----GRTTIVIAHRLSTiKTADKIV 648
Cdd:PRK13547 148 GGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwnlGVLAIVHDPNLAA-RHADRIA 226
|
250
....*....|....*..
gi 407923078 649 VMSQGRIVEQGTHNELL 665
Cdd:PRK13547 227 MLADGAIVAHGAPADVL 243
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1102-1183 |
8.79e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 69.23 E-value: 8.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPEQpvLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIA 1181
Cdd:PRK10522 323 LELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
..
gi 407923078 1182 LV 1183
Cdd:PRK10522 401 AV 402
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1102-1201 |
1.26e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTrpeQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSY-I 1180
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100
....*....|....*....|..
gi 407923078 1181 ALVSQEPTLYQG-TIRDNILLG 1201
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLG 103
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1102-1219 |
1.32e-11 |
|
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: 65.72 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTrpeQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEIssLNINDYRSYIA 1181
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110
....*....|....*....|....*....|....*....
gi 407923078 1182 LVSQEPTLY-QGTIRDNILLGADRENVPEEAIIKACKDA 1219
Cdd:cd03300 76 TVFQNYALFpHLTVFENIAFGLRLKKLPKAEIKERVAEA 114
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1102-1215 |
1.39e-11 |
|
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: 65.82 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKST---TIALLERfynPLTGGIYADGKEISSLNINDYRs 1178
Cdd:cd03296 3 IEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTllrLIAGLER---PDSGTILFGGEDATDVPVQERN- 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 407923078 1179 yIALVSQEPTLYQG-TIRDNILLGAD---RENVPEEAIIKA 1215
Cdd:cd03296 76 -VGFVFQHYALFRHmTVFDNVAFGLRvkpRSERPPEAEIRA 115
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1102-1212 |
1.75e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 67.09 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTT---IALLERfynPLTGGIYADGKEISSlNINDYRS 1178
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLlriIAGLET---PDSGRIVLNGRDLFT-NLPPRER 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 407923078 1179 YIALVSQE----PTLyqgTIRDNILLGADRENVPEEAI 1212
Cdd:COG1118 76 RVGFVFQHyalfPHM---TVAENIAFGLRVRPPSKAEI 110
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1116-1196 |
1.93e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.81 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1116 EQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQG-TI 1194
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTV 93
|
..
gi 407923078 1195 RD 1196
Cdd:PRK11231 94 RE 95
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
820-1072 |
3.04e-11 |
|
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: 65.93 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 820 NFWSLMYLMLALTQLISFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQEEnsAGALTS-FLSTETTSLAgLSGA 898
Cdd:cd18570 42 NIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRK--TGEIISrFNDANKIREA-ISST 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 899 TLGTIFTVLTTLIGALVLgIAIGWKLGLVCASTIPVLLacgFLRFWILARFEQRSKKAYEKSA---SYACEATSAIRTVA 975
Cdd:cd18570 119 TISLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYI---LIILLFNKPFKKKNREVMESNAelnSYLIESLKGIETIK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 976 SLTREEDVYASYHQQLVDQGAKNLRSILKSSTLYALSQSGMFLCTALGFWYGGTLISKGEYSLFQFFVCFSAITFGAQSA 1055
Cdd:cd18570 195 SLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPI 274
|
250
....*....|....*..
gi 407923078 1056 GTIFSFAPDMGKAKHAA 1072
Cdd:cd18570 275 ENLINLQPKIQEAKVAA 291
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1102-1204 |
3.40e-11 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 64.38 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN---INdyRS 1178
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpheRA--RA 75
|
90 100 110
....*....|....*....|....*....|
gi 407923078 1179 YIALVSQE----PTLyqgTIRDNILLGADR 1204
Cdd:cd03224 76 GIGYVPEGrrifPEL---TVEENLLLGAYA 102
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
436-656 |
3.51e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.36 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 436 QVKHI-YPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKS----TIVGLVErfydPVGGEVLLDGVNVQELNLHWLRQQ- 509
Cdd:COG3845 259 EVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSelaeALAGLRP----PASGSIRLDGEDITGLSPRERRRLg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 510 ISLVQQEPVLFAT----TIFDNIkhgLIGTQYEH-------LEHEKVREmvyNAAKMSNAHDfVSalPEGYETNVGergf 578
Cdd:COG3845 335 VAYIPEDRLGRGLvpdmSVAENL---ILGRYRRPpfsrggfLDRKAIRA---FAEELIEEFD-VR--TPGPDTPAR---- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 579 LLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKS-EGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIV 656
Cdd:COG3845 402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEIlALSDRIAVMYEGRIV 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
454-682 |
3.70e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 454 DLVVEAGKTTALVGASGSGKSTIVGLVerfydpvGGEVLLD-GVNVQELNLhwlrqQISLVQQEPVLFAT-TIFDNIKHG 531
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQDL-----IVARLQQDPPRNVEgTVYDFVAEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 532 L--IG---TQYEHLEH--------------EKVREMV--YNAAKMSN-AHDFVSALPEGYETNVGErgflLSGGQKQRIA 589
Cdd:PRK11147 91 IeeQAeylKRYHDISHlvetdpseknlnelAKLQEQLdhHNLWQLENrINEVLAQLGLDPDAALSS----LSGGWLRKAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 590 IARAIVSDPKILLLDEATSALDTKS-EGVVQAALDraAQGrTTIVIAHRLSTIKT-ADKIVVMSQGRIVE-QGTHNELLE 666
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIETiEWLEGFLKT--FQG-SIIFISHDRSFIRNmATRIVDLDRGKLVSyPGNYDQYLL 243
|
250
....*....|....*.
gi 407923078 667 RKQayynlvEAQRIAA 682
Cdd:PRK11147 244 EKE------EALRVEE 253
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
177-374 |
3.86e-11 |
|
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: 65.54 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 177 IYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITaDANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTL 256
Cdd:cd18570 67 LKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 257 ILCSTIFAIVFTMGGGSTFIMKYNKQSLASYA-LGGTVVeEVFSSIRNAVAFGTQDKLARQYNEHLViaEYWGKKMKT-V 334
Cdd:cd18570 146 ITLLIIPLYILIILLFNKPFKKKNREVMESNAeLNSYLI-ESLKGIETIKSLNAEEQFLKKIEKKFS--KLLKKSFKLgK 222
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 407923078 335 LASMLGAMMTIVYLNYGLA-FWMGSRYLVKGEMSLSDVLTI 374
Cdd:cd18570 223 LSNLQSSIKGLISLIGSLLiLWIGSYLVIKGQLSLGQLIAF 263
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
815-1037 |
4.35e-11 |
|
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: 65.44 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 815 LRSEANFWSLMY--LMLALTQLIS--FTG-QGLCFAICSEKLIHRVRDTAFRTMLRQDISFFdqEENSAGALTSFLSTET 889
Cdd:cd18590 26 LGGEYQHNAFTSaiGLMCLFSLGSslSAGlRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFF--EKTKTGDLTSRLSTDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 890 TSLAGLSGATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLLACGFLRFWILARFEQRSKKAYEKSASYACEATS 969
Cdd:cd18590 104 TLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVS 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 970 AIRTVASLTREEDVYASYHQQLVDQ-GAKNLRSILksSTLYALSQSGMFLCT-ALGFWYGGTLISKGEYS 1037
Cdd:cd18590 184 SIRTVRSFKAEEEEACRYSEALERTyNLKDRRDTV--RAVYLLVRRVLQLGVqVLMLYCGRQLIQSGHLT 251
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1102-1225 |
6.63e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.29 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTrpeQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFyNPLTGGIYADGK-EI-------SSLNI 1173
Cdd:PRK14258 8 IKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRvEFfnqniyeRRVNL 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 1174 NDYRSYIALVSQEPTLYQGTIRDNILLGAD----RENVPEEAIIK-ACKDANIYDFI 1225
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVEsALKDADLWDEI 140
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1102-1186 |
7.14e-11 |
|
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: 63.95 E-value: 7.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGG-IYADGKEISSLNINDYRSYI 1180
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
....*.
gi 407923078 1181 ALVSQE 1186
Cdd:COG1119 81 GLVSPA 86
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1102-1219 |
8.81e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.94 E-value: 8.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPEqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN--INDYRSY 1179
Cdd:PRK13639 2 LETRDLKYSYPDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksLLEVRKT 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 407923078 1180 IALVSQEP--TLYQGTIRDNILLGADRENVPEEAIIKACKDA 1219
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEA 121
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1102-1229 |
9.81e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 64.05 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPEqPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGG---IYADGKEISSLNINDYRS 1178
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 1179 YIALVSQEP--TLYQGTIRDNILLGADRENVPEEAIIK----ACKDANIYDFIMSLP 1229
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKivrdVLADVGMLDYIDSEP 141
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1106-1224 |
1.37e-10 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 62.27 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1106 NVHFRYPTRPEqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSlniNDYRSYIALVSQ 1185
Cdd:cd03226 4 NISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQ 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 407923078 1186 EPT--LYQGTIRDNILLGADRENVPEEAIIKACKDANIYDF 1224
Cdd:cd03226 79 DVDyqLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYAL 119
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1102-1219 |
1.65e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.58 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTrpeQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSL-----NIND- 1175
Cdd:PRK09452 15 VELRGISKSFDG---KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaenrHVNTv 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 407923078 1176 YRSYiALVsqePTLyqgTIRDNILLGADRENVPEEAIIKACKDA 1219
Cdd:PRK09452 92 FQSY-ALF---PHM---TVFENVAFGLRMQKTPAAEITPRVMEA 128
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
453-668 |
1.86e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 453 VDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELN-LHWLRQQISLV----QQEPVLFATTIFDN 527
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIRAGIMLCpedrKAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 528 IKhglIGTQYEHLeheKVREMVYNAAKMSNAHDFVSAL----PEGyETNVGergfLLSGGQKQRIAIARAIVSDPKILLL 603
Cdd:PRK11288 352 IN---ISARRHHL---RAGCLINNRWEAENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 604 DEATSALD--TKSEgVVQAALDRAAQGRTTIVIAHRL-STIKTADKIVVMSQGRIVEQGTHNELLERK 668
Cdd:PRK11288 421 DEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQATERQ 487
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
437-678 |
2.40e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.50 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 437 VKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLV--ERFYDPVGGEVLLDGVNVQELNLH-WLRQQISLV 513
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEdRAGEGIFMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 514 QQEPV--------LFATTIFDNIKHGligTQYEHLEHEKVREMVYNAAKMSNahdfvsaLPEGYETNVGERGFllSGGQK 585
Cdd:PRK09580 84 FQYPVeipgvsnqFFLQTALNAVRSY---RGQEPLDRFDFQDLMEEKIALLK-------MPEDLLTRSVNVGF--SGGEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 586 QRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQG-RTTIVIAHR---LSTIKtADKIVVMSQGRIVEQGTH 661
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHYqriLDYIK-PDYVHVLYQGRIVKSGDF 230
|
250
....*....|....*....
gi 407923078 662 N--ELLErKQAYYNLVEAQ 678
Cdd:PRK09580 231 TlvKQLE-EQGYGWLTEQQ 248
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1120-1204 |
2.91e-10 |
|
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: 61.71 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1120 LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIND---YRSYIALvsqePTLyqgTIRD 1196
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRmvvFQNYSLL----PWL---TVRE 73
|
....*...
gi 407923078 1197 NILLGADR 1204
Cdd:TIGR01184 74 NIALAVDR 81
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1098-1219 |
3.05e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 62.56 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1098 MEGHI-EFRNVHFRYPTRPEqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEI--SSLNIN 1174
Cdd:PRK13636 1 MEDYIlKVEELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLM 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 407923078 1175 DYRSYIALVSQEP--TLYQGTIRDNILLGADRENVPEEAIIKACKDA 1219
Cdd:PRK13636 79 KLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNA 125
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
164-376 |
3.63e-10 |
|
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: 62.36 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 164 GEFFTCYIAtvgwiyvgeRISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATfiTA 243
Cdd:cd18590 57 GGLFMCTLS---------RLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVK--TL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 244 FVIGFVKY--WKLTLILCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHL 321
Cdd:cd18590 126 GMLGFMLSlsWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEAL 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 322 VIAEYWGKKMKTVLASMLGAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVLTILL 376
Cdd:cd18590 206 ERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFIL 260
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
151-368 |
4.44e-10 |
|
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: 62.41 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 151 LVKFVLYFVYLFIGEFFTCYIATVGWIYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITAD----ANLVQDGI 226
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDtealNELFTSGL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 227 sekVGLVqQSLATFITAFVIGFVKYWKLTLILCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVA 306
Cdd:cd18544 120 ---VTLI-GDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQL 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 307 FGTQDKLARQYNEHLviAEYWGKKMKTV-LASMLGAMMTIVY-LNYGLAFWMGSRYLVKGEMSL 368
Cdd:cd18544 196 FNREKREFEEFDEIN--QEYRKANLKSIkLFALFRPLVELLSsLALALVLWYGGGQVLSGAVTL 257
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
178-383 |
5.28e-10 |
|
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: 62.03 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 178 YVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLI 257
Cdd:cd18548 65 KASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 258 LCSTIFAIVFTMGGGSTFIMKYNKQSLASY-ALgGTVVEEVFSSIRnaV--AFGTQDKLARQYNEhlVIAEY--WGKKMK 332
Cdd:cd18548 145 LLVAIPILALVVFLIMKKAIPLFKKVQKKLdRL-NRVVRENLTGIR--VirAFNREDYEEERFDK--ANDDLtdTSLKAG 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 333 TVLASMLGAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDV-------LTILLAVMIGAF 383
Cdd:cd18548 220 RLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMMLSM 277
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
170-372 |
6.05e-10 |
|
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: 62.14 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 170 YIATVGWIYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFV 249
Cdd:cd18564 72 YAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFW 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 250 KYWKLTLILCSTIFAIVFTMGGGSTFIMKYNKQ------SLASyalggtVVEEVFSSIRNAVAFGTQDKLARQYNEHlvI 323
Cdd:cd18564 152 LDWQLALIALAVAPLLLLAARRFSRRIKEASREqrrregALAS------VAQESLSAIRVVQAFGREEHEERRFARE--N 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 407923078 324 AEYWGKKMKTV-LASMLGAMM-TIVYLNYGLAFWMGSRYLVKGEMSLSDVL 372
Cdd:cd18564 224 RKSLRAGLRAArLQALLSPVVdVLVAVGTALVLWFGAWLVLAGRLTPGDLL 274
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1102-1212 |
7.80e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.17 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRpeQPVLRGLNLSVKPGQYVALVGASGCGKST---TIALLERfynpLTGG-IYADGKEISSLNINDyR 1177
Cdd:PRK11650 4 LKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTllrMVAGLER----ITSGeIWIGGRVVNELEPAD-R 76
|
90 100 110
....*....|....*....|....*....|....*.
gi 407923078 1178 SyIALVSQEPTLY-QGTIRDNILLGADRENVPEEAI 1212
Cdd:PRK11650 77 D-IAMVFQNYALYpHMSVRENMAYGLKIRGMPKAEI 111
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
440-656 |
9.64e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 440 IYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGvnvQELNL----HWLRQQISLVQQ 515
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFksskEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 516 E-PVLFATTIFDNIKHGLIGTQYEHLEHEKvremVYNAAKmsnahdfvsALPEGYETNVG--ERGFLLSGGQKQRIAIAR 592
Cdd:PRK10982 81 ElNLVLQRSVMDNMWLGRYPTKGMFVDQDK----MYRDTK---------AIFDELDIDIDprAKVATLSVSQMQMIEIAK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 593 AIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIV 656
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKlKERGCGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
816-1042 |
1.13e-09 |
|
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: 61.07 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 816 RSEANFWSLMYLMLALT--QLISFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDqeENSAGALTSFLSTETTSLA 893
Cdd:cd18782 36 QDLATLYVIGVVMLVAAllEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFD--KRPVGELSTRISELDTIRG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 894 GLSGATLGTIFTVLTTLIGALVLgIAIGWKLGLVCASTIPVLLACGFLRFWILARFEQRSKKAYEKSASYACEATSAIRT 973
Cdd:cd18782 114 FLTGTALTTLLDVLFSVIYIAVL-FSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQT 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 974 VASLTREEDVYASYHQQLVDQGAKNLRSILKSSTLYALSQSGMFLCTALGFWYGGTLISKGEYSLFQFF 1042
Cdd:cd18782 193 VKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLI 261
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
452-636 |
1.19e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 452 GVDLVVEAGKTTALVGASGSGKST----IVGLVerfyDPVGGEVLLDGVNVQEL------NLHWLRQQislvqqepvlfa 521
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSllriLAGLA----RPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 522 ttifDNIKHGLigTQYEHLEhekvremvYNAAKMSNAHDFV--SALpegyeTNVGERGFL------LSGGQKQRIAIARA 593
Cdd:PRK13538 83 ----PGIKTEL--TALENLR--------FYQRLHGPGDDEAlwEAL-----AQVGLAGFEdvpvrqLSAGQQRRVALARL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 407923078 594 IVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAH 636
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
449-653 |
1.20e-09 |
|
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: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIVG-LVERFYDPV--GGEVLLDGVNVQELnlhwLRQQISLVQQEPVlfattif 525
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERVTTGVitGGDRLVNGRPLDSS----FQRSIGYVQQQDL------- 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 526 dnikhgligtqyeHLEHEKVREMVYNAAKM--------SNAHDFVSAL-----PEGY-ETNVGERGFLLSGGQKQRIAIA 591
Cdd:TIGR00956 847 -------------HLPTSTVRESLRFSAYLrqpksvskSEKMEYVEEViklleMESYaDAVVGVPGEGLNVEQRKRLTIG 913
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 592 RAIVSDPKILL-LDEATSALDTKSE-GVVQAALDRAAQGRTTIVIAHRLSTIKTA--DKIVVMSQG 653
Cdd:TIGR00956 914 VELVAKPKLLLfLDEPTSGLDSQTAwSICKLMRKLADHGQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1120-1223 |
1.28e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.17 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1120 LRGLNLSVKPGQYVALVGASGCGKSTTIALLERF--YNP---LTGGIYADGKEISSLNIN--DYRSYIALVSQEPTLYQG 1192
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYSPRTDtvDLRKEIGMVFQQPNPFPM 100
|
90 100 110
....*....|....*....|....*....|....*..
gi 407923078 1193 TIRDNILLG------ADREnVPEEAIIKACKDANIYD 1223
Cdd:PRK14239 101 SIYENVVYGlrlkgiKDKQ-VLDEAVEKSLKGASIWD 136
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1102-1177 |
1.41e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 61.36 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPT-RPEQPVLRGLNLSVKPGQYVALVGASGCGKST---TIALLERfynPLTGGIYADGKEISSLNINDYR 1177
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
446-654 |
1.78e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.20 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 446 EVTVMNGVDLVVEAGKTTALVGASGSGKSTIV-GLVERFY-DPVGGEVLLDGVNVQELNLhwlrQQISLVQQEPVLFATT 523
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLnALAGRIQgNNFTGTILANNRKPTKQIL----KRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 524 ifdNIKHGLIGTQYEHLEHEKVREmvynaAKMSNAHDFVS--ALPEGYETNVGE---RGflLSGGQKQRIAIARAIVSDP 598
Cdd:PLN03211 156 ---TVRETLVFCSLLRLPKSLTKQ-----EKILVAESVISelGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 599 KILLLDEATSALD-TKSEGVVQAALDRAAQGRTTIVIAHRLST--IKTADKIVVMSQGR 654
Cdd:PLN03211 226 SLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1104-1204 |
1.90e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 61.62 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1104 FRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALlerfynpLTGGIYADGKEISSLniNDYRsyIALV 1183
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKI-------LAGELEPDSGEVSIP--KGLR--IGYL 66
|
90 100
....*....|....*....|..
gi 407923078 1184 SQEPTLYQG-TIRDNILLGADR 1204
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAE 88
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1102-1219 |
2.20e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.89 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTrpeQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEI--SSLNINDyrsy 1179
Cdd:PRK11432 7 VVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD---- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 407923078 1180 IALVSQEPTLY-QGTIRDNILLGADRENVPEEAIIKACKDA 1219
Cdd:PRK11432 80 ICMVFQSYALFpHMSLGENVGYGLKMLGVPKEERKQRVKEA 120
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
824-1038 |
2.43e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 59.80 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 824 LMYLMLALTQLISFtGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQEEnsAGALTSFLSTETTSLAGLSGATLGTI 903
Cdd:cd18550 44 GMVAVAVASALLGV-VQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGTLTSV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 904 FTVLTTLIGALVLGIAIGWKLGLVCASTIPVLlacgflrFWILARFEQR----SKKAYEKSASYACEAT-----SAIRTV 974
Cdd:cd18550 121 VSNVVTLVATLVAMLALDWRLALLSLVLLPLF-------VLPTRRVGRRrrklTREQQEKLAELNSIMQetlsvSGALLV 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 975 ASLTREEDVYASYHQQlvdqgAKNLRSI-LKSSTLYALSQSGMFLCTALG----FWYGGTLISKGEYSL 1038
Cdd:cd18550 194 KLFGREDDEAARFARR-----SRELRDLgVRQALAGRWFFAALGLFTAIGpalvYWVGGLLVIGGGLTI 257
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
447-665 |
2.59e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.20 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 447 VTVMNGVDLVVEAGKTTALVGASGSGKS----TIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQ----QISLVQQEP- 517
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSliakAICGVTKDNWRVTADRMRFDDIDLLRLSPRERRKlvghNVSMIFQEPq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 518 --VLFATTIFDNIKHGLIGTQYE-------HLEHEKVREMVYNAAkMSNAHDFVSALPegYEtnvgergflLSGGQKQRI 588
Cdd:PRK15093 100 scLDPSERVGRQLMQNIPGWTYKgrwwqrfGWRKRRAIELLHRVG-IKDHKDAMRSFP--YE---------LTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 589 AIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNELL 665
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKELV 247
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1119-1202 |
3.17e-09 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 58.60 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1119 VLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIND-YRSYIALVSQEPTLYQG-TIRD 1196
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiARLGIGRTFQIPRLFPElTVLE 94
|
....*.
gi 407923078 1197 NILLGA 1202
Cdd:cd03219 95 NVMVAA 100
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1102-1211 |
4.65e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.99 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYP--TRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIN----D 1175
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQ 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 407923078 1176 YRSYIALVSQ--EPTLYQGTIRDNILLGADRENV-PEEA 1211
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVsQEEA 121
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
821-1041 |
5.18e-09 |
|
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: 58.96 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 821 FWSLMYLMLALTQLISFTGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTETTSLAGLSGATL 900
Cdd:cd18541 41 RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQK--NRTGDLMARATNDLNAVRMALGPGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 901 GTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLLacgFLRFWILARFEQRSKK---AYEKSASYACEATSAIRTVASL 977
Cdd:cd18541 119 LYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA---LLVYRLGKKIHKRFRKvqeAFSDLSDRVQESFSGIRVIKAF 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 978 TREEDVYASYHQQLVDQGAKNLRSILKSSTLYALSQSGMFLCTALGFWYGGTLISKGEYSLFQF 1041
Cdd:cd18541 196 VQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDL 259
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
824-983 |
5.59e-09 |
|
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: 58.95 E-value: 5.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 824 LMYLMLALTQLIsftgQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTETTSLAGLSGATLGTI 903
Cdd:cd18547 53 GLYLLSALFSYL----QNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDT--HSHGDIMSRVTNDVDNISQALSQSLTQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 904 FTVLTTLIGALVLGIAIGWKLGLVCASTIPVLlacgflrFWILARFEQRSKKAYEKSA-------SYACEATSAIRTVAS 976
Cdd:cd18547 127 ISSILTIVGTLIMMLYISPLLTLIVLVTVPLS-------LLVTKFIAKRSQKYFRKQQkalgelnGYIEEMISGQKVVKA 199
|
....*..
gi 407923078 977 LTREEDV 983
Cdd:cd18547 200 FNREEEA 206
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1099-1220 |
5.72e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.21 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1099 EGHIEFRNVHFRYPTrpEQPVLRGLNLSVKPGQYVALVGASGCGKST---TIAllerfynpltgGI--YADGKeISSLNI 1173
Cdd:COG4178 360 DGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKSTllrAIA-----------GLwpYGSGR-IARPAG 425
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 407923078 1174 NDyrsyIALVSQEPTLYQGTIRDNILLGADRENVPEEAIIKACKDAN 1220
Cdd:COG4178 426 AR----VLFLPQRPYLPLGTLREALLYPATAEAFSDAELREALEAVG 468
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1106-1187 |
6.53e-09 |
|
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: 60.08 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1106 NVHFRYPTRpEQPVLRGLNLSVKPGQYVALVGASGCGKSTT----IALLERFYNPLTGGIYADGKEISSLNINDYRSY-- 1179
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrg 91
|
90
....*....|
gi 407923078 1180 --IALVSQEP 1187
Cdd:COG4172 92 nrIAMIFQEP 101
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
821-1042 |
8.38e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 58.73 E-value: 8.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 821 FWSLMYLMLALTQLISFT--GQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDqeENSAGALTSFLSTETTSLAGLSGA 898
Cdd:cd18565 53 LWLLGGLTVAAFLLESLFqyLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFE--DRQTGDLMSVLNNDVNQLERFLDD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 899 TLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLLACGFlrfwilaRFEQRSKKAYEKSASYACE-------ATSAI 971
Cdd:cd18565 131 GANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTY-------WFQRRIEPRYRAVREAVGDlnarlenNLSGI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 972 RTVASLTRE-------EDVYASYHQqlvdqgaKNLRSILKSSTLYALSQ---SGMFLCTalgFWYGG-----------TL 1030
Cdd:cd18565 204 AVIKAFTAEdferervADASEEYRD-------ANWRAIRLRAAFFPVIRlvaGAGFVAT---FVVGGywvldgpplftGT 273
|
250
....*....|..
gi 407923078 1031 ISKGEYSLFQFF 1042
Cdd:cd18565 274 LTVGTLVTFLFY 285
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1109-1219 |
8.52e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.09 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1109 FRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEI--SSLNINDYRSYIALVSQE 1186
Cdd:PRK13638 9 FRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQD 85
|
90 100 110
....*....|....*....|....*....|....*
gi 407923078 1187 P--TLYQGTIRDNILLGADRENVPEEAIIKACKDA 1219
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEA 120
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
856-1038 |
8.84e-09 |
|
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: 58.23 E-value: 8.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 856 RDTAFRTMLRQDISFFDqeENSAGALTSFLSTETTSLAGLSGATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVL 935
Cdd:cd18549 78 RRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 936 LacgFLRFWILARFEQRSKKAYEKSA---SYACEATSAIRTVASLTREEdvyasYHQQLVDQGAKNLRSILKSSTLY-AL 1011
Cdd:cd18549 156 I---IFTIYFNKKMKKAFRRVREKIGeinAQLEDSLSGIRVVKAFANEE-----YEIEKFDEGNDRFLESKKKAYKAmAY 227
|
170 180 190
....*....|....*....|....*....|.
gi 407923078 1012 SQSGMFLCTALGFW----YGGTLISKGEYSL 1038
Cdd:cd18549 228 FFSGMNFFTNLLNLvvlvAGGYFIIKGEITL 258
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
1058-1183 |
9.28e-09 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 59.59 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1058 IFSFAPDMGKAKHAAIQLKTLFDR--KPEIDTWSSDGEKINNME-----GHIEFRNVHFRYPT-RPEQPVLRG-LNLSVK 1128
Cdd:TIGR01194 287 LVSALPILAQAQIACQRLADFGERfnEPEPELELSDADNVLLLAhdksvDSIELKDVHMNPKApEGSEGFALGpIDLRIA 366
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 1129 PGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALV 1183
Cdd:TIGR01194 367 QGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDYRDLFSAI 421
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1105-1187 |
9.76e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.77 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1105 RNVHFRYPT------RPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN---IND 1175
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKA 86
|
90
....*....|..
gi 407923078 1176 YRSYIALVSQEP 1187
Cdd:PRK10419 87 FRRDIQMVFQDS 98
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1103-1219 |
1.00e-08 |
|
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: 56.77 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1103 EFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISslninDYRSYIAL 1182
Cdd:cd03235 1 EVEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGY 72
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 407923078 1183 VSQEPTL---YQGTIRDNILLGADRENVPEEAIIKACKDA 1219
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAK 112
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
460-656 |
1.26e-08 |
|
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: 55.07 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 460 GKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISlvqqepvlfattifdnikhgligtqyeh 539
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII---------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 540 lehekvremvynaakmsnahdfvsalpegyetnVGERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQ 619
Cdd:smart00382 54 ---------------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLL 100
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 407923078 620 AALD------RAAQGRTTIVIAHRLSTIKTADKIVVMSQGRIV 656
Cdd:smart00382 101 LLEElrllllLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
154-380 |
1.36e-08 |
|
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: 57.85 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 154 FVLYFVYLFIgEFFTCYIATVgwiyVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLvqdgISEkvgLV 233
Cdd:cd18549 49 LALYILRTLL-NYFVTYWGHV----MGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFD----ISE---LA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 234 QQ-------SLATFITAFVIGFVKYWKLTLILCSTI-FAIVFTMgggsTFIMKYNKQSLASYALGGTV---VEEVFSSIR 302
Cdd:cd18549 117 HHgpedlfiSIITIIGSFIILLTINVPLTLIVFALLpLMIIFTI----YFNKKMKKAFRRVREKIGEInaqLEDSLSGIR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 303 NAVAFGTQD---KLARQYNEHLVIAEYWGKKMKTVLASMLGAMMTIVYLnygLAFWMGSRYLVKGEMSLSDVLTILLAVM 379
Cdd:cd18549 193 VVKAFANEEyeiEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNL---VVLVAGGYFIIKGEITLGDLVAFLLYVN 269
|
.
gi 407923078 380 I 380
Cdd:cd18549 270 V 270
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1113-1201 |
1.77e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 55.95 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1113 TRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNP---LTGGIYADGKEISSLNINDYRsyIALVSQEPTL 1189
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRR--IGILFQDDLL 87
|
90
....*....|...
gi 407923078 1190 Y-QGTIRDNILLG 1201
Cdd:COG4136 88 FpHLSVGENLAFA 100
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1117-1212 |
1.99e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.92 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1117 QPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISslNINDYRSYIALVSQEPTLY-QGTIR 1195
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVE 109
|
90
....*....|....*..
gi 407923078 1196 DNILLGADRENVPEEAI 1212
Cdd:PRK11607 110 QNIAFGLKQDKLPKAEI 126
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
161-368 |
2.03e-08 |
|
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: 57.09 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 161 LFIGEFFTCYIATVGWIY----VGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKV-GLVQQ 235
Cdd:cd18545 45 LFLALNLVNWVASRLRIYlmakVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLiNLIPD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 236 SLaTFITAFVIGFVKYWKLTLILCSTI---FAIVFTMGGGS--TFIMKYNKQSLASyalggTVVEEVFSSIRNAVAFGTQ 310
Cdd:cd18545 125 LL-TLVGIVIIMFSLNVRLALVTLAVLpllVLVVFLLRRRArkAWQRVRKKISNLN-----AYLHESISGIRVIQSFARE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 311 DKLARQYNEhlVIAEYWGKKMKTV-LASMLGAMM-TIVYLNYGLAFWMGSRYLVKGEMSL 368
Cdd:cd18545 199 DENEEIFDE--LNRENRKANMRAVrLNALFWPLVeLISALGTALVYWYGGKLVLGGAITV 256
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
568-666 |
2.16e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.20 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 568 GYETNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSEgVVQAALDRAAQGRTTIVIAHRL-STIKTA 644
Cdd:PRK10982 384 GHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFE-IYQLIAELAKKDKGIIIISSEMpELLGIT 458
|
90 100
....*....|....*....|....*..
gi 407923078 645 DKIVVMSQGR---IVE--QGTHNELLE 666
Cdd:PRK10982 459 DRILVMSNGLvagIVDtkTTTQNEILR 485
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1070-1216 |
2.86e-08 |
|
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: 58.42 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1070 HAAIQLKTL--FDRKPEIDTWSSDGEKINNMEGH-IEFRNVHFRYpTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTT 1146
Cdd:TIGR00957 602 QASVSLKRLriFLSHEELEPDSIERRTIKPGEGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSL 680
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1147 IALLERFYNPLTGGIYADGKeisslnindyrsyIALVSQEPTLYQGTIRDNILLGADRENVPEEAIIKAC 1216
Cdd:TIGR00957 681 LSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEAC 737
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1102-1205 |
3.30e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLtggiyadgkEISSLNIndyRSYIA 1181
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA---------ETSSVVI---RGSVA 682
|
90 100
....*....|....*....|....
gi 407923078 1182 LVSQEPTLYQGTIRDNILLGADRE 1205
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFGSDFE 706
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1102-1210 |
3.30e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTrpeQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSY-I 1180
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
|
90 100 110
....*....|....*....|....*....|.
gi 407923078 1181 ALVSQEPTLYQG-TIRDNILLGADRENVPEE 1210
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENILFGLPKRQASMQ 119
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
449-645 |
4.02e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.96 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQElNLHWLRQQISLVQQE----PVLfatTI 524
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRsginPYL---TL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 525 FDNIKHGlIGTQYEHLEhekVREMVyNAAKMSNAHDFvsalPEGyetnvgergfLLSGGQKQRIAIARAIVSDPKILLLD 604
Cdd:PRK13540 92 RENCLYD-IHFSPGAVG---ITELC-RLFSLEHLIDY----PCG----------LLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 407923078 605 EATSALDTKS-EGVVQAALDRAAQGRTTIVIAHRLSTIKTAD 645
Cdd:PRK13540 153 EPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
106-376 |
4.32e-08 |
|
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: 56.01 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 106 IVVSSICAI---AAGAVLPLMTvvfGSLSGTFQGmfqgtmsNGEFNDELVKFVLYFVYLFIG-EFFTC---YIA-TVGWI 177
Cdd:cd18778 1 LILTLLCALlstLLGLVPPWLI---RELVDLVTI-------GSKSLGLLLGLALLLLGAYLLrALLNFlriYLNhVAEQK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 178 YVGErissrIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLI 257
Cdd:cd18778 71 VVAD-----LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 258 lcsTIFAIVFTMGGGSTFIMK----YNKQSLASYALGGTVVEEVfSSIRNAVAFGTQD-------KLARQY-NEHLVIAE 325
Cdd:cd18778 146 ---TLIPIPFLALGAWLYSKKvrprYRKVREALGELNALLQDNL-SGIREIQAFGREEeeakrfeALSRRYrKAQLRAMK 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 407923078 326 YWGkkMKTVLASMLGAMMTIVYLnyglafWMGSRYLVKGEMSLSDVLTILL 376
Cdd:cd18778 222 LWA--IFHPLMEFLTSLGTVLVL------GFGGRLVLAGELTIGDLVAFLL 264
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1102-1202 |
5.37e-08 |
|
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: 54.48 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHF---RYPTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALL--ERFYNPLTGGIYADGKEISslnINDY 1176
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSF 80
|
90 100
....*....|....*....|....*..
gi 407923078 1177 RSYIALVSQEPTLY-QGTIRDNILLGA 1202
Cdd:cd03213 81 RKIIGYVPQDDILHpTLTVRETLMFAA 107
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
580-654 |
5.38e-08 |
|
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: 53.22 E-value: 5.38e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALdrAAQGRTTIVIAH-R--LSTIktADKIVVMSQGR 654
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL--KEYPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
819-1038 |
7.34e-08 |
|
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: 55.59 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 819 ANFWSLMYLMLAL--TQLISF---TGQGLCFAICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTETTSLA 893
Cdd:cd18563 37 GNTSLLLLLVLGLagAYVLSAllgILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDK--RQTGSLMSRVTSDTDRLQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 894 GLSGATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPvLLACGFLRFW--ILARFEQRSKKAYEKSASYAcEATSAI 971
Cdd:cd18563 115 DFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVP-LVVWGSYFFWkkIRRLFHRQWRRWSRLNSVLN-DTLPGI 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 972 RTVASLTREEDV---YASYHQQLVDQGAKNLRSilkSSTLYALsqsgMFLCTALGF----WYGGTLISKGEYSL 1038
Cdd:cd18563 193 RVVKAFGQEKREikrFDEANQELLDANIRAEKL---WATFFPL----LTFLTSLGTlivwYFGGRQVLSGTMTL 259
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
453-660 |
1.01e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.54 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 453 VDLVVEAGKTTALVGASGSGKSTIVGlvERFYDPVggEVLLDGVNVQELNLH--WLRQQIS---LVQQEPV--------L 519
Cdd:cd03271 14 IDVDIPLGVLTCVTGVSGSGKSSLIN--DTLYPAL--ARRLHLKKEQPGNHDriEGLEHIDkviVIDQSPIgrtprsnpA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 520 FATTIFDNIKhGLI-----GTQY--EHLE---HEK----VREM-VYNAAK----MSNAHDFVSALPE---GYETnVGERG 577
Cdd:cd03271 90 TYTGVFDEIR-ELFcevckGKRYnrETLEvryKGKsiadVLDMtVEEALEffenIPKIARKLQTLCDvglGYIK-LGQPA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 578 FLLSGGQKQRIAIARAI---VSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTIKTADKIVVMSQ- 652
Cdd:cd03271 168 TTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKCADWIIDLGPe 247
|
250
....*....|...
gi 407923078 653 -----GRIVEQGT 660
Cdd:cd03271 248 ggdggGQVVASGT 260
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1093-1212 |
1.13e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1093 EKINNMEGHIEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN 1172
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 407923078 1173 INDYRSYIALVSQEPTLYQG-TIRDNILLG-------------ADRENVpEEAI 1212
Cdd:PRK10575 80 SKAFARKVAYLPQQLPAAEGmTVRELVAIGrypwhgalgrfgaADREKV-EEAI 132
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1122-1187 |
1.15e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 55.12 E-value: 1.15e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407923078 1122 GLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN---INDYRSYIALVSQEP 1187
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP 104
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
579-665 |
1.20e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 579 LLSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSEgVVQAALDRAAQGRTTIVIAHRL-STIKTADKIVVMSQGRI 655
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgAKKE-IYQLINQFKAEGLSIILVSSEMpEVLGMSDRILVMHEGRI 473
|
90
....*....|....*
gi 407923078 656 -----VEQGTHNELL 665
Cdd:PRK10762 474 sgeftREQATQEKLM 488
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1102-1171 |
1.26e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.39 E-value: 1.26e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSL 1171
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADW 69
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1119-1188 |
1.43e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.22 E-value: 1.43e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1119 VLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPT 1188
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAT 91
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1120-1203 |
1.44e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1120 LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYnP---LTGGIYADGKEISSLNINDY-RSYIALVSQEPTLYQG-TI 1194
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKElSV 99
|
....*....
gi 407923078 1195 RDNILLGAD 1203
Cdd:PRK13549 100 LENIFLGNE 108
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
411-642 |
1.58e-07 |
|
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: 55.53 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 411 RVSPLDPTSKEGRRLENLQGRVELRQVKHI--YPSRPEVTVmNGVDLV------VEAGKTTALVGASGSGKSTIVGLVER 482
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGRGIVEYQDNGikFENIPLVTP-NGDVLIeslsfeVPSGNNLLICGPNGCGKSSLFRILGE 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 483 FYDPVGGEVLLDGvnvqelnlhwlRQQISLVQQEP----------VLFATTIFDNIKHGLIGTQYE------HLEHEKVR 546
Cdd:TIGR00954 501 LWPVYGGRLTKPA-----------KGKLFYVPQRPymtlgtlrdqIIYPDSSEDMKRRGLSDKDLEqildnvQLTHILER 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 547 EMVYNAakMSNAHDfvsalpegyetnvgergfLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAa 626
Cdd:TIGR00954 570 EGGWSA--VQDWMD------------------VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF- 628
|
250
....*....|....*.
gi 407923078 627 qGRTTIVIAHRLSTIK 642
Cdd:TIGR00954 629 -GITLFSVSHRKSLWK 643
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1100-1198 |
1.64e-07 |
|
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: 54.09 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1100 GHIEFRNVHFRYpTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNpLTGGIYADGKEISSLNINDYRSY 1179
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90
....*....|....*....
gi 407923078 1180 IALVSQEPTLYQGTIRDNI 1198
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNL 97
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1113-1189 |
1.77e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 54.85 E-value: 1.77e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 1113 TRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTL 1189
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSL 88
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1116-1192 |
2.86e-07 |
|
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: 52.14 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1116 EQPVLRGLNLSVKPGQYVALVGASGCGKST---TIALLERfYNPLTGGIYADGKEISSLNIND-YRSYIALVSQEPTLYQ 1191
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTlakTIMGHPK-YEVTEGEILFKGEDITDLPPEErARLGIFLAFQYPPEIP 90
|
.
gi 407923078 1192 G 1192
Cdd:cd03217 91 G 91
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1102-1217 |
2.96e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 53.68 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRY-PTRP-EQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEI----SSLNIND 1175
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 407923078 1176 YRSYIALVSQ--EPTLYQGTIRDNILLGADRENVPE-EAIIKACK 1217
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEdEAKEKALK 127
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
446-667 |
3.09e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.94 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 446 EVTVMNGVDLVVEAGKTTALVGASGSGKSTIV----GLVErfydPVGGEVLLDGVNVQELNLHWLRQqISLV----QQ-- 515
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIkmltGILV----PTSGEVRVLGYVPFKRRKEFARR-IGVVfgqrSQlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 516 --EPVLfattifDNIKhgLIGTQYEhLEHEKVREmvynaakmsNAHDFVSALpegyetNVGErgFL------LSGGQKQR 587
Cdd:COG4586 109 wdLPAI------DSFR--LLKAIYR-IPDAEYKK---------RLDELVELL------DLGE--LLdtpvrqLSLGQRMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 588 IAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR--AAQGRTTIVIAHRLSTI-KTADKIVVMSQGRIVEQGTHNEL 664
Cdd:COG4586 163 CELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIeALCDRVIVIDHGRIIYDGSLEEL 242
|
...
gi 407923078 665 LER 667
Cdd:COG4586 243 KER 245
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
816-1043 |
3.14e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 53.64 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 816 RSEANFWSLMYLMLALTQLISFTGQGLCFA--ICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTETTSLA 893
Cdd:cd18540 36 GTLDGLTGFILLYLGLILIQALSVFLFIRLagKIEMGVSYDLRKKAFEHLQTLSFSYFDK--TPVGWIMARVTSDTQRLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 894 GLSGATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLlacgflrFWILARFEQRSKKAYEK--------SASYAc 965
Cdd:cd18540 114 EIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVL-------AVVSIYFQKKILKAYRKvrkinsriTGAFN- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 966 EATSAIRTVASLTREEDVYASYhqqlvdqgaKNLRSILKSSTLYALSQSGMFL---------CTALGFWYGGTLISKG-- 1034
Cdd:cd18540 186 EGITGAKTTKTLVREEKNLREF---------KELTEEMRRASVRAARLSALFLpivlflgsiATALVLWYGGILVLAGai 256
|
....*....
gi 407923078 1035 EYSLFQFFV 1043
Cdd:cd18540 257 TIGTLVAFI 265
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
406-655 |
3.17e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 406 YSTIDRVSPLDPTSKEGRRLENLQGRVELRQVKHIY-PSRPEVTVMN-------GVDLVVEAGKTTALVGASGSGKS--- 474
Cdd:PRK15439 227 LSTDDIIQAITPAAREKSLSASQKLWLELPGNRRQQaAGAPVLTVEDltgegfrNISLEVRAGEILGLAGVVGAGRTela 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 475 -TIVGLVErfydPVGGEVLLDGVNVQELN--------LHWL---RQQ-------------ISLVQQEPVLFATTIFDNIK 529
Cdd:PRK15439 307 eTLYGLRP----ARGGRIMLNGKEINALStaqrlargLVYLpedRQSsglyldaplawnvCALTHNRRGFWIKPARENAV 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 530 ----HGLIGTQYEHLEHEkVREmvynaakmsnahdfvsalpegyetnvgergflLSGGQKQRIAIARAIVSDPKILLLDE 605
Cdd:PRK15439 383 leryRRALNIKFNHAEQA-ART--------------------------------LSGGNQQKVLIAKCLEASPQLLIVDE 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 407923078 606 ATSALDTKSEG-VVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVMSQGRI 655
Cdd:PRK15439 430 PTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1102-1186 |
4.03e-07 |
|
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: 52.89 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPT------RPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIND 1175
Cdd:TIGR02769 3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90
....*....|....
gi 407923078 1176 YRSY---IALVSQE 1186
Cdd:TIGR02769 83 RRAFrrdVQLVFQD 96
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1118-1217 |
4.24e-07 |
|
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: 54.53 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1118 PVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKeisslnindyrsyIALVSQEPTLYQGTIRDN 1197
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDN 506
|
90 100
....*....|....*....|
gi 407923078 1198 ILLGADRENVPEEAIIKACK 1217
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQ 526
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1102-1212 |
4.70e-07 |
|
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: 51.90 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDyrsyIA 1181
Cdd:cd03269 1 LEVENVTKRFGRVT---ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR----IG 73
|
90 100 110
....*....|....*....|....*....|..
gi 407923078 1182 LVSQEPTLYQG-TIRDNILLGADRENVPEEAI 1212
Cdd:cd03269 74 YLPEERGLYPKmKVIDQLVYLAQLKGLKKEEA 105
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1095-1229 |
5.05e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.83 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1095 INNMEGHIEFRNVHFRYPTrPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIN 1174
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 1175 DYRSYIALVSQEP--TLYQGTIRDNILLGADRENVP----EEAIIKACKDANIYDFIMSLP 1229
Cdd:PRK13648 80 KLRKHIGIVFQNPdnQFVGSIVKYDVAFGLENHAVPydemHRRVSEALKQVDMLERADYEP 140
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
422-655 |
5.10e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.78 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 422 GRRLENLQGRV------ELRQVKHI---YPSRPEVTVMNGVDLVVEAGKTTALVGASGSGK----STIVGLVERFYDpvg 488
Cdd:PRK13549 241 GRELTALYPREphtigeVILEVRNLtawDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRtelvQCLFGAYPGRWE--- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 489 GEVLLDGVNVQELN-LHWLRQQISLVQQepvlfattifDNIKHGLI---GTQYE----HLEHEKVREMVYNAAKMSNAHD 560
Cdd:PRK13549 318 GEIFIDGKPVKIRNpQQAIAQGIAMVPE----------DRKRDGIVpvmGVGKNitlaALDRFTGGSRIDDAAELKTILE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 561 FVSAL------PEGYETNvgergflLSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSEgVVQAALDRAAQGRTTI 632
Cdd:PRK13549 388 SIQRLkvktasPELAIAR-------LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYE-IYKLINQLVQQGVAII 459
|
250 260
....*....|....*....|....
gi 407923078 633 VIAHRLSTI-KTADKIVVMSQGRI 655
Cdd:PRK13549 460 VISSELPEVlGLSDRVLVMHEGKL 483
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
580-656 |
5.15e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.64 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSE--GVVQaalDRAAQGRTTIVIAHRL-STIKTADKIVVMSQGR 654
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgAKYEiyTIIN---ELAAEGKGVIVISSELpELLGMCDRIYVMNEGR 481
|
..
gi 407923078 655 IV 656
Cdd:NF040905 482 IT 483
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1118-1217 |
5.81e-07 |
|
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: 52.55 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1118 PVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKeisslnindyrsyIALVSQEPTLYQGTIRDN 1197
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
|
90 100
....*....|....*....|
gi 407923078 1198 ILLGADRENVPEEAIIKACK 1217
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQ 137
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
447-614 |
6.08e-07 |
|
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: 53.79 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 447 VTVMNGVDLVVEAGKTT--------------ALVGASGSGKST---IVGLVERFYDpvgGEVLL-DGVNVQELnlhwlrq 508
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKEIlkdislsffpgakiGVLGLNGAGKSTllrIMAGVDKDFN---GEARPqPGIKVGYL------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 509 qislvQQEPVLFAT-TIFDNIKHGLIGTQYEHLEHEKV--------REMVYNAAKM---------SNAHDFVSAL----- 565
Cdd:TIGR03719 74 -----PQEPQLDPTkTVRENVEEGVAEIKDALDRFNEIsakyaepdADFDKLAAEQaelqeiidaADAWDLDSQLeiamd 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 407923078 566 ----PEGyETNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKS 614
Cdd:TIGR03719 149 alrcPPW-DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
570-677 |
7.09e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.25 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 570 ETNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALD--TKSEgVVQAALDRAAQGRTTIVIAHRLSTIKTA-DK 646
Cdd:PRK09700 404 NQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgAKAE-IYKVMRQLADDGKVILMVSSELPEIITVcDR 478
|
90 100 110
....*....|....*....|....*....|..
gi 407923078 647 IVVMSQGRIVEQGTH-NELLERKQAYYNLVEA 677
Cdd:PRK09700 479 IAVFCEGRLTQILTNrDDMSEEEIMAWALPQE 510
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
558-664 |
7.18e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 53.86 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 558 AHDFVSALPE-------------GYETnVGERGFLLSGGQKQRIAIARAI---VSDPKILLLDEATSALDT----KSEGV 617
Cdd:TIGR00630 796 AYEFFEAVPSisrklqtlcdvglGYIR-LGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFddikKLLEV 874
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 407923078 618 VQAALDraaQGRTTIVIAHRLSTIKTADKIVVMSQ------GRIVEQGTHNEL 664
Cdd:TIGR00630 875 LQRLVD---KGNTVVVIEHNLDVIKTADYIIDLGPeggdggGTVVASGTPEEV 924
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1105-1201 |
7.95e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.99 E-value: 7.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1105 RNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYAdgkeiSSLNINDYRSYIALVS 1184
Cdd:PRK11247 16 NAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-----GTAPLAEAREDTRLMF 87
|
90
....*....|....*...
gi 407923078 1185 QEPTLYQ-GTIRDNILLG 1201
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLG 105
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1098-1172 |
8.23e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 53.19 E-value: 8.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 1098 MEGHIEFRNVHFRYPTRPEQ-PVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN 1172
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLD 76
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
816-1042 |
9.73e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 52.15 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 816 RSEANFWSLMYLMLALtqlisFTGQGLCFAI-------CSEKLIHRVRDTAFRTMLRQDISFFDQEenSAGALTSFLSTE 888
Cdd:cd18778 34 KSLGLLLGLALLLLGA-----YLLRALLNFLriylnhvAEQKVVADLRSDLYDKLQRLSLRYFDDR--QTGDLMSRVIND 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 889 TTSL-AGLSGATLGTIFTVLTtLIGALVLGIAIGWKLGLVCASTIPVLLACGfLRF--WILARFEQRSKKAYEKSAsYAC 965
Cdd:cd18778 107 VANVeRLIADGIPQGITNVLT-LVGVAIILFSINPKLALLTLIPIPFLALGA-WLYskKVRPRYRKVREALGELNA-LLQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 966 EATSAIRTVASLTREEdvyasYHQQLVDQGAKNLR-SILKSSTLYALSQSGMFLCTALGF----WYGGTLISKGEYS--- 1037
Cdd:cd18778 184 DNLSGIREIQAFGREE-----EEAKRFEALSRRYRkAQLRAMKLWAIFHPLMEFLTSLGTvlvlGFGGRLVLAGELTigd 258
|
....*
gi 407923078 1038 LFQFF 1042
Cdd:cd18778 259 LVAFL 263
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1102-1203 |
1.02e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYAdgkeisslnindYRSYIA 1181
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVA 682
|
90 100
....*....|....*....|..
gi 407923078 1182 LVSQEPTLYQGTIRDNILLGAD 1203
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFGSP 704
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
830-1035 |
1.04e-06 |
|
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: 51.78 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 830 ALTQLISFTGQGLC-FA------ICSEKLIHRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTET----TSLA----- 893
Cdd:cd18574 45 ALKLLGLYLLQSLLtFAyisllsVVGERVAARLRNDLFSSLLRQDIAFFDT--HRTGELVNRLTADVqefkSSFKqcvsq 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 894 GLSGATLgtiftvlttLIGALVLGIAIGWKLGLVCASTIPVLLACG-----FLRfwilaRFEQRSKKAYEKSASYACEAT 968
Cdd:cd18574 123 GLRSVTQ---------TVGCVVSLYLISPKLTLLLLVIVPVVVLVGtlygsFLR-----KLSRRAQAQVAKATGVADEAL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 969 SAIRTVASLTREEDVYASYHQQLvdQGAKNLRSILKSST-----LYALSQSGMFLCTalgFWYGGTLISKGE 1035
Cdd:cd18574 189 GNIRTVRAFAMEDRELELYEEEV--EKAAKLNEKLGLGIgifqgLSNLALNGIVLGV---LYYGGSLVSRGE 255
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1102-1187 |
1.15e-06 |
|
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: 52.76 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTR--------PEQPVLRGLNLSVKPGQYVALVGASGCGKSTT-IALLeRFyNPLTGGIYADGKEISSLN 1172
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RL-IPSEGEIRFDGQDLDGLS 353
|
90
....*....|....*...
gi 407923078 1173 IND---YRSYIALVSQEP 1187
Cdd:COG4172 354 RRAlrpLRRRMQVVFQDP 371
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1115-1216 |
1.31e-06 |
|
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: 50.79 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1115 PEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSY----IALVSQEPTLY 1190
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100
....*....|....*....|....*.
gi 407923078 1191 QGTIRDNILLGADRENVPEEAIIKAC 1216
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDAC 117
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1102-1210 |
1.36e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.56 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRY-PTRP-EQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISS----LNIND 1175
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknKKLKP 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 407923078 1176 YRSYIALVSQ--EPTLYQGTIRDNILLGADRENVPEE 1210
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEE 119
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
422-655 |
1.36e-06 |
|
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: 52.52 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 422 GRRLENLQGR---------VELRQVKHIYPSRPEVTVMNGVDLVVEAGKTTALVGASGSGKS-TIVGLVERFYDPVGGEV 491
Cdd:TIGR02633 239 GREITSLYPHepheigdviLEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNV 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 492 LLDGVNVQELN-LHWLRQQISLVQQE-------PVLfatTIFDNI------KHGLIGTQYEHLEHEKVREMVyNAAKMSN 557
Cdd:TIGR02633 319 FINGKPVDIRNpAQAIRAGIAMVPEDrkrhgivPIL---GVGKNItlsvlkSFCFKMRIDAAAELQIIGSAI-QRLKVKT 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 558 AHDFvsaLPEGYetnvgergflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAH 636
Cdd:TIGR02633 395 ASPF---LPIGR----------LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSS 461
|
250 260
....*....|....*....|
gi 407923078 637 RLSTI-KTADKIVVMSQGRI 655
Cdd:TIGR02633 462 ELAEVlGLSDRVLVIGEGKL 481
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1102-1228 |
1.70e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.32 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYP--TRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN----IND 1175
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 1176 YRSYIALVSQ--EPTLYQGTIRDNILLGADRENVPeeaiIKACKDaNIYDFIMSL 1228
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN----LDEVKN-YAHRLLMDL 132
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
444-666 |
1.83e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 444 RPEVTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDP---VGGEVLLDGvnvQELNLHWLRQQISLVQQEPVLF 520
Cdd:PLN03140 175 KTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPslkVSGEITYNG---YRLNEFVPRKTSAYISQNDVHV 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 521 A------TTIFDNIKHGlIGTQYEHLEHEKVRE------------MVYNAAKMSNAHdfvSALPEGY-----------ET 571
Cdd:PLN03140 252 GvmtvkeTLDFSARCQG-VGTRYDLLSELARREkdagifpeaevdLFMKATAMEGVK---SSLITDYtlkilgldickDT 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 572 NVGE---RGflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLS----TIKTA 644
Cdd:PLN03140 328 IVGDemiRG--ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapeTFDLF 405
|
250 260
....*....|....*....|..
gi 407923078 645 DKIVVMSQGRIVEQGTHNELLE 666
Cdd:PLN03140 406 DDIILLSEGQIVYQGPRDHILE 427
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
465-614 |
1.83e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 465 LVGASGSGKST---IVGLVERFYDpvgGE-VLLDGVNVQELnlhwlrqqislvQQEPVLFAT-TIFDNIKHGL-----IG 534
Cdd:PRK11819 38 VLGLNGAGKSTllrIMAGVDKEFE---GEaRPAPGIKVGYL------------PQEPQLDPEkTVRENVEEGVaevkaAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 535 TQYEHLEHEKVREMVYN---AAKM---------SNAHDFVSAL---------PEGyETNVGErgflLSGGQKQRIAIARA 593
Cdd:PRK11819 103 DRFNEIYAAYAEPDADFdalAAEQgelqeiidaADAWDLDSQLeiamdalrcPPW-DAKVTK----LSGGERRRVALCRL 177
|
170 180
....*....|....*....|.
gi 407923078 594 IVSDPKILLLDEATSALDTKS 614
Cdd:PRK11819 178 LLEKPDMLLLDEPTNHLDAES 198
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1106-1169 |
1.96e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.85 E-value: 1.96e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 1106 NVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEIS 1169
Cdd:PRK11248 6 HLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE 66
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1120-1207 |
1.98e-06 |
|
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: 50.06 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1120 LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSlNINDYRSYIALVSQEPTLyqgtirDNIL 1199
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV------DDEL 88
|
....*...
gi 407923078 1200 LGadRENV 1207
Cdd:cd03265 89 TG--WENL 94
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1119-1201 |
2.11e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 50.68 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1119 VLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYN-----PLTGGIYADGKEISSLNINDYRSYIALVSQEPT-LYQG 1192
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpIPNL 97
|
....*....
gi 407923078 1193 TIRDNILLG 1201
Cdd:PRK14247 98 SIFENVALG 106
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1102-1214 |
2.11e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.76 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN-INDYRSYI 1180
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 407923078 1181 ALVSQEP-TLYQG-TIRDNILLGADRENVPEEAIIK 1214
Cdd:PRK13644 80 GIVFQNPeTQFVGrTVEEDLAFGPENLCLPPIEIRK 115
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
103-388 |
2.47e-06 |
|
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: 50.56 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 103 WIIIVVSSICAIAAGAVLPLMT--VVFGSLSGTFQGmfqgtmsngefndELVKFVLYFVYLFIGEFftcyIATVGWIYVG 180
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTrrAIDGPIAHGDRS-------------ALWPLVLLLLALGVAEA----VLSFLRRYLA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 181 ERISSRIrEYYL-----SAILRQNVGYFDKLGAGEITTRITADANLVQDGISeKVGLVQQSLATFITAFVIGFVKYWKLT 255
Cdd:cd18543 64 GRLSLGV-EHDLrtdlfAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 256 LILCSTIFAIVFTmggGSTFIMKYNKQSLASYALGG---TVVEEVFSSIRNAVAFGTQDKLARQYnEHLVIAEYWgKKMK 332
Cdd:cd18543 142 LVALASLPPLVLV---ARRFRRRYFPASRRAQDQAGdlaTVVEESVTGIRVVKAFGRERRELDRF-EAAARRLRA-TRLR 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 333 TV--LASMLGAMMTIVYLNYGLAFWMGSRYLVKGEMSLSDVL--TILLAVMIGAF-SLGNI 388
Cdd:cd18543 217 AArlRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVafSAYLTMLVWPVrMLGWL 277
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1120-1201 |
2.81e-06 |
|
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: 51.36 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1120 LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFY--NPLTGGIYADGKEISSLNINDY-RSYIALVSQEPTLYQG-TIR 1195
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElSVA 96
|
....*.
gi 407923078 1196 DNILLG 1201
Cdd:TIGR02633 97 ENIFLG 102
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
853-1047 |
3.06e-06 |
|
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: 50.56 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 853 HRVRDTAFRTMLRQDISFFDQeeNSAGALTSFLSTETTSLAGLSgATLGTIFTVLTTLIGALVLGIAIGWKLGLVCASTI 932
Cdd:cd18543 72 HDLRTDLFAHLQRLDGAFHDR--WQSGQLLSRATSDLSLVQRFL-AFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 933 PVLlacgflrFWILARFEQR----SKKAYEKSASYAC---EATSAIRTVASLTREEDVYASYHQQ---LVDQG--AKNLR 1000
Cdd:cd18543 149 PPL-------VLVARRFRRRyfpaSRRAQDQAGDLATvveESVTGIRVVKAFGRERRELDRFEAAarrLRATRlrAARLR 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 407923078 1001 SILkSSTLYALSQSGMflctALGFWYGGTLISKGEYSLFQfFVCFSA 1047
Cdd:cd18543 222 ARF-WPLLEALPELGL----AAVLALGGWLVANGSLTLGT-LVAFSA 262
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
580-659 |
3.21e-06 |
|
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: 48.86 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 LSGGQKQRIAIARAIVSDPK--ILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTIKTADKIVVM------ 650
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFgpgsgk 167
|
....*....
gi 407923078 651 SQGRIVEQG 659
Cdd:cd03238 168 SGGKVVFSG 176
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
450-649 |
3.81e-06 |
|
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: 49.71 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 450 MNGVDLVVEAGKTT-----ALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQelnlhWLRQQISLVQQepvlfatti 524
Cdd:cd03237 10 LGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-----YKPQYIKADYE--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 525 fdnikhgliGTQYEHLeHEKVREMvYNAAKMSNahDFVSALP-EG-YETNVGErgflLSGGQKQRIAIARAIVSDPKILL 602
Cdd:cd03237 76 ---------GTVRDLL-SSITKDF-YTHPYFKT--EIAKPLQiEQiLDREVPE----LSGGELQRVAIAACLSKDADIYL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 407923078 603 LDEATSALDTKSEGVVQAALDRAAQG--RTTIVIAHRLSTIK-TADKIVV 649
Cdd:cd03237 139 LDEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEHDIIMIDyLADRLIV 188
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1120-1202 |
4.87e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.40 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1120 LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFyNPLTGGIYADGKEI-SSLNIND-------YRSYIALVSQEPTLYQ 1191
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRL-NDLIPGFRVEGKVTfHGKNLYApdvdpveVRRRIGMVFQKPNPFP 104
|
90
....*....|.
gi 407923078 1192 GTIRDNILLGA 1202
Cdd:PRK14243 105 KSIYDNIAYGA 115
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1120-1205 |
5.39e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.39 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1120 LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEIsslNINDYRSY----IALVSQEPTLY-QGTI 1194
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV---TFNGPKSSqeagIGIIHQELNLIpQLTI 96
|
90
....*....|.
gi 407923078 1195 RDNILLGadRE 1205
Cdd:PRK10762 97 AENIFLG--RE 105
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1108-1185 |
6.37e-06 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 48.87 E-value: 6.37e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 1108 HFRYPTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALlerfynpLTGGIYADGKEISSLNINDYRSYIALVSQ 1185
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKI-------LSGLLQPTSGEVRVAGLVPWKRRKKFLRR 95
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
449-611 |
6.95e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.96 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDgvnvQELNLHWLRQQISLvqqEPVLFATTifdni 528
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN----GKLRIGYVPQKLYL---DTTLPLTV----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 529 khgligTQYEHLEHEKVREMVYNAAKMSNAHDFVSALPEGyetnvgergflLSGGQKQRIAIARAIVSDPKILLLDEATS 608
Cdd:PRK09544 87 ------NRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
...
gi 407923078 609 ALD 611
Cdd:PRK09544 150 GVD 152
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1102-1199 |
7.04e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 47.53 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLerfynpltGGI--YADGKeISSLNINDyrsy 1179
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL--------AGLwpWGSGR-IGMPEGED---- 65
|
90 100
....*....|....*....|
gi 407923078 1180 IALVSQEPTLYQGTIRDNIL 1199
Cdd:cd03223 66 LLFLPQRPYLPLGTLREQLI 85
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
822-1034 |
7.76e-06 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 49.32 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 822 WSLMYLMLALTQLISFTGQGLCFAICSEKLIHRVRDTAFRTMlrQDISFFDQEENSAGALTSFLSTETTSLAGLSGATLG 901
Cdd:cd18548 41 TGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKI--QSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 902 TIFTVLTTLIGALVLGIAIGWKLGLVCASTIPVLLACGFLRFWILARFEQRSKKAYEKSASYACEATSAIRTVASLTREE 981
Cdd:cd18548 119 MLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNRED 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 982 dvyasYHQQLVDQGAKNLRSI-LKSSTLYALSQSGMFL----CTALGFWYGGTLISKG 1034
Cdd:cd18548 199 -----YEEERFDKANDDLTDTsLKAGRLMALLNPLMMLimnlAIVAILWFGGHLINAG 251
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1102-1224 |
9.16e-06 |
|
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: 48.30 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPT-------------------RPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIY 1162
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 1163 ADGKeISSLnindyrsyIAL-VSQEPTLyqgTIRDNI-----LLGADRENVPEeaiikacKDANIYDF 1224
Cdd:cd03220 81 VRGR-VSSL--------LGLgGGFNPEL---TGRENIylngrLLGLSRKEIDE-------KIDEIIEF 129
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1102-1145 |
9.79e-06 |
|
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: 46.67 E-value: 9.79e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 407923078 1102 IEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKST 1145
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKST 41
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1102-1150 |
9.90e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 49.68 E-value: 9.90e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 407923078 1102 IEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALL 1150
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL 361
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1102-1204 |
1.10e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.64 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPtrpeqPV--LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSY 1179
Cdd:COG3845 6 LELRGITKRFG-----GVvaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIAL 80
|
90 100
....*....|....*....|....*..
gi 407923078 1180 -IALVSQEPTLYQG-TIRDNILLGADR 1204
Cdd:COG3845 81 gIGMVHQHFMLVPNlTVAENIVLGLEP 107
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1098-1201 |
1.15e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1098 MEGHIEFRNVHFRYPTrpeqpV--LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIND 1175
Cdd:PRK11288 1 SSPYLSFDGIGKTFPG-----VkaLDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA 75
|
90 100 110
....*....|....*....|....*....|.
gi 407923078 1176 -YRSYIALVSQE----PTLyqgTIRDNILLG 1201
Cdd:PRK11288 76 aLAAGVAIIYQElhlvPEM---TVAENLYLG 103
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1102-1212 |
1.27e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 48.26 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPEqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIA 1181
Cdd:PRK13652 4 IETRDLCYSYSGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110
....*....|....*....|....*....|...
gi 407923078 1182 LVSQEP--TLYQGTIRDNILLGADRENVPEEAI 1212
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETV 114
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
465-636 |
1.52e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 465 LVGASGSGKSTIVGLVERFYDPVGGEVLLDgVNVQelnLHWLRQ-QISLVQQepvlfatTIFDNIKHGligtqyeHLEHE 543
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD-PNER---LGKLRQdQFAFEEF-------TVLDTVIMG-------HTELW 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 544 KV---REMVYNAAKMSN-----AHDFVSALPE--GY--ETNVGErgfLLSG-----------------GQKQRIAIARAI 594
Cdd:PRK15064 94 EVkqeRDRIYALPEMSEedgmkVADLEVKFAEmdGYtaEARAGE---LLLGvgipeeqhyglmsevapGWKLRVLLAQAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 407923078 595 VSDPKILLLDEATSALDTKS----EGVVQAaldRAAqgrTTIVIAH 636
Cdd:PRK15064 171 FSNPDILLLDEPTNNLDINTirwlEDVLNE---RNS---TMIIISH 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1102-1200 |
1.77e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 48.26 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSlNINDYRSYIA 1181
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100
....*....|....*....|...
gi 407923078 1182 LVSQ----EPTLyqgTIRDNILL 1200
Cdd:PRK13537 84 VVPQfdnlDPDF---TVRENLLV 103
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-389 |
1.78e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 48.25 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 179 VGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLIL 258
Cdd:cd18550 66 IGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 259 CSTI-FAIVFTMGGGSTfIMKYNKQSLASYALGGTVVEEVFS--SIRNAVAFGTQDKLARQYNEHL-------VIAEYWG 328
Cdd:cd18550 146 LVLLpLFVLPTRRVGRR-RRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSrelrdlgVRQALAG 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 329 KKMKTVLaSMLGAMMTIvylnygLAFWMGSRYLVKGEMSLSDV--LTILLAVMIGAFS-LGNIG 389
Cdd:cd18550 225 RWFFAAL-GLFTAIGPA------LVYWVGGLLVIGGGLTIGTLvaFTALLGRLYGPLTqLLNIQ 281
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1115-1187 |
1.82e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.77 E-value: 1.82e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 1115 PEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIA----LLERFYNPLTGGIYADGKEISSlniNDYRS-YIALVSQEP 1187
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAaalgILPAGVRQTAGRVLLDGKPVAP---CALRGrKIATIMQNP 88
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
580-650 |
1.84e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 1.84e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVM 650
Cdd:PRK13409 213 LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLdYLADNVHIA 284
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
580-650 |
2.32e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.81 E-value: 2.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 580 LSGGQKQRIAIA-----RAIVSDPkILLLDEATSALDTKS-EGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIVVM 650
Cdd:cd03227 78 LSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
450-636 |
2.62e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 450 MNGVDLVVEAGKTTA------LVGASGSGKST---------IVGL--------VERfydpvggEVLLDGVNVQELNLH-- 504
Cdd:PLN03073 187 VGGRDLIVDASVTLAfgrhygLVGRNGTGKTTflrymamhaIDGIpkncqilhVEQ-------EVVGDDTTALQCVLNtd 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 505 -----WLRQQISLVQQEPVLFATTIFDNIKHGLIGTQYEHLEHEKVREM--------VYNAAkmSNAHDFVSALPEGYET 571
Cdd:PLN03073 260 iertqLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRLEEIykrlelidAYTAE--ARAASILAGLSFTPEM 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 572 NVGE-RGFllSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAqgRTTIVIAH 636
Cdd:PLN03073 338 QVKAtKTF--SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1116-1150 |
2.66e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.88 E-value: 2.66e-05
10 20 30
....*....|....*....|....*....|....*
gi 407923078 1116 EQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALL 1150
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL 76
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1120-1204 |
2.85e-05 |
|
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: 46.52 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1120 LRGLNLSVK---PGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEI--SSLNIN--DYRSYIALVSQEPTLY-Q 1191
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKINlpPQQRKIGLVFQQYALFpH 89
|
90
....*....|...
gi 407923078 1192 GTIRDNILLGADR 1204
Cdd:cd03297 90 LNVRENLAFGLKR 102
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
449-653 |
3.10e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 449 VMNGVDLVVEAGKTTALVGASGSGKSTIV---------GLVErfydpvgGEVLLDGV-NVQELnlhwlRQQISLVQQEPV 518
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMdvlagrktgGYIE-------GDIRISGFpKKQET-----FARISGYCEQND 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 519 LFATTIfdNIKHGLIGTQYEHL-----EHEKVR--EMVYNAAKMSNAHDFVSALPegyetnvGERGflLSGGQKQRIAIA 591
Cdd:PLN03140 963 IHSPQV--TVRESLIYSAFLRLpkevsKEEKMMfvDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIA 1031
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407923078 592 RAIVSDPKILLLDEATSALDTKSEGVVQAAL-DRAAQGRTTIVIAHRLS--TIKTADKIVVMSQG 653
Cdd:PLN03140 1032 VELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSidIFEAFDELLLMKRG 1096
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1106-1169 |
3.68e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 3.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407923078 1106 NVHFRYPTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTtiaLLERFYNPLTGGIYADGKEIS 1169
Cdd:PRK13547 3 TADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKST---LLKALAGDLTGGGAPRGARVT 63
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
454-667 |
4.29e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 454 DLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQqisLVQQEpvlfattiFDNIKHGLI 533
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK---LVSDE--------WQRNNTDML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 534 GTQYEHLEHeKVREMVYNAAKMSnahdfvsALPEGYETNVG-----ERGFL-LSGGQKQRIAIARAIVSDPKILLLDEAT 607
Cdd:PRK10938 92 SPGEDDTGR-TTAEIIQDEVKDP-------ARCEQLAQQFGitallDRRFKyLSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 608 SALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTIKT-ADKIVVMSQGRIVEQGTHNELLER 667
Cdd:PRK10938 164 DGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
580-659 |
4.52e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.10 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 LSGGQKQRIAIARAIVSDPK--ILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIVIAHRLSTIKTADKIVVMSQ---- 652
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRlRDLGNTVLVVEHDEDTIRAADHVIDIGPgagv 217
|
....*....
gi 407923078 653 --GRIVEQG 659
Cdd:cd03270 218 hgGEIVAQG 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1119-1187 |
4.63e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 4.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407923078 1119 VLRGLNLSVKPGQYVALVGASGCGKSTT-IALLeRFYNPlTGGIYADGKEISSLNIND---YRSYIALVSQEP 1187
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTgLALL-RLINS-QGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDP 371
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
580-650 |
5.33e-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: 47.47 E-value: 5.33e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSE-GVVQAALDRAAQGRTTIVIAHRLSTI-KTADKIVVM 650
Cdd:COG1245 213 LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRlNVARLIRELAEEGKYVLVVEHDLAILdYLADYVHIL 285
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
569-649 |
5.51e-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: 47.47 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 569 YETNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAA--QGRTTIVIAHRLSTIKT-AD 645
Cdd:COG1245 449 LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAenRGKTAMVVDHDIYLIDYiSD 524
|
....
gi 407923078 646 KIVV 649
Cdd:COG1245 525 RLMV 528
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1122-1171 |
5.94e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.14 E-value: 5.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 407923078 1122 GLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSL 1171
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL 72
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
565-649 |
6.00e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 565 LPEGYETNVGErgflLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGR--TTIVIAHRLSTIK 642
Cdd:PRK13409 443 LERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMID 518
|
....*...
gi 407923078 643 T-ADKIVV 649
Cdd:PRK13409 519 YiSDRLMV 526
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1099-1175 |
6.14e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 46.12 E-value: 6.14e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407923078 1099 EGHIEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIND 1175
Cdd:PRK10619 3 ENKLNVIDLHKRYG---EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKD 76
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1102-1210 |
7.23e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 46.27 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYptRPEQP----VLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN----I 1173
Cdd:PRK13643 2 IKFEKVNYTY--QPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeI 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 407923078 1174 NDYRSYIALVSQEP--TLYQGTIRDNILLGADRENVPEE 1210
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKE 118
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1096-1171 |
7.66e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.91 E-value: 7.66e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 1096 NNMEGHIEFRNVHFrypTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSL 1171
Cdd:PRK11831 2 QSVANLVDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM 74
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1120-1185 |
8.66e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 46.23 E-value: 8.66e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407923078 1120 LRGLNLSVKPGQYVALVGASGCGKSTTIALlerfynpLTGGIYADGKEISSLNINDYRSYIALVSQ 1185
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKM-------LTGILVPTSGEVRVLGYVPFKRRKEFARR 96
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1119-1215 |
8.75e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 46.23 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1119 VLRGLNLSVKPGQYVALVGASGCGKST---TIALLErfyNPLTGGIYADGKEISSLNINDYRsyIALVSQEPTLYQG-TI 1194
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTllrIIAGLE---HQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRHmTV 91
|
90 100
....*....|....*....|....
gi 407923078 1195 RDNILLGAD---RENVPEEAIIKA 1215
Cdd:PRK10851 92 FDNIAFGLTvlpRRERPNAAAIKA 115
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
844-1060 |
9.81e-05 |
|
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: 45.65 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 844 FAICSEKLIHRVRDTAFRTMLRQDISFFdqEENSAGALTSFLSTETTSLAGLSGATLGTIFTVLTTLIGALVLGIaIGWK 923
Cdd:cd18566 66 LAWIGARFDHRLSNAAFEHLLSLPLSFF--EREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWY-LGGK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 924 LGLVCASTIPVLLACGFLRFWILAR-FEQRSKkAYEKSASYACEATSAIRTVASLTREEDVYASYHQQLVDQGAKNLRSI 1002
Cdd:cd18566 143 LVLVPLVLLGLFVLVAILLGPILRRaLKERSR-ADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVA 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 1003 LKSSTLYALSQSGMFLCTALGFWYGGTLISKGEyslfqffvcfsaITFGAQSAGTIFS 1060
Cdd:cd18566 222 KINAVAQTLGQLFSQVSMVAVVAFGALLVINGD------------LTVGALIACTMLS 267
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
463-644 |
1.00e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 463 TALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELnlhwlrqqislvqQEPvlFATTIFDNIKHGLIGTQYEHL-- 540
Cdd:PRK13541 29 TYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------------AKP--YCTYIGHNLGLKLEMTVFENLkf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 541 --EHEKVREMVYNAAKMSNAHDFVSalpegyetnvgERGFLLSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVV 618
Cdd:PRK13541 94 wsEIYNSAETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170 180
....*....|....*....|....*..
gi 407923078 619 QAALD-RAAQGRTTIVIAHRLSTIKTA 644
Cdd:PRK13541 163 NNLIVmKANSGGIVLLSSHLESSIKSA 189
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1098-1201 |
1.09e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 45.22 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1098 MEGHIEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERF--YNP---LTGGIYADGKEISSLN 1172
Cdd:PRK14267 1 MKFAIETVNLRVYYG---SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEearVEGEVRLFGRNIYSPD 77
|
90 100 110
....*....|....*....|....*....|..
gi 407923078 1173 IN--DYRSYIALVSQEPTLY-QGTIRDNILLG 1201
Cdd:PRK14267 78 VDpiEVRREVGMVFQYPNPFpHLTIYDNVAIG 109
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1102-1199 |
1.28e-04 |
|
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: 44.67 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRY-PTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSlNINDYRSYI 1180
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100
....*....|....*....|
gi 407923078 1181 ALVSQEPTLYQG-TIRDNIL 1199
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLE 100
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
441-655 |
1.41e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 441 YPSRPevTVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDG-VNVQELNLHWLrQQISLvQQEPVL 519
Cdd:PLN03073 518 YPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAkVRMAVFSQHHV-DGLDL-SSNPLL 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 520 FATTIFDNIKHgligtqyehlehEKVREMVYNAAKMSNAhdfvsALPEGYEtnvgergflLSGGQKQRIAIARAIVSDPK 599
Cdd:PLN03073 594 YMMRCFPGVPE------------QKLRAHLGSFGVTGNL-----ALQPMYT---------LSGGQKSRVAFAKITFKKPH 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 407923078 600 ILLLDEATSALDTKS-EGVVQAALdrAAQGRTTIViAHRLSTIK-TADKIVVMSQGRI 655
Cdd:PLN03073 648 ILLLDEPSNHLDLDAvEALIQGLV--LFQGGVLMV-SHDEHLISgSVDELWVVSEGKV 702
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1120-1207 |
1.47e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.48 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1120 LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIND---YRSYIALVSQE-PTLYQGTIR 1195
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDhHLLMDRTVY 97
|
90
....*....|....*..
gi 407923078 1196 DN-----ILLGADRENV 1207
Cdd:PRK10908 98 DNvaiplIIAGASGDDI 114
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1120-1201 |
1.64e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1120 LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIND-YRSYIALVSQEPTLY-QGTIRDN 1197
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVlQRSVMDN 93
|
....
gi 407923078 1198 ILLG 1201
Cdd:PRK10982 94 MWLG 97
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
450-673 |
1.65e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.65 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 450 MNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVLLDGVNVQELNLHWLRQQISLVQqepvlfattifdNIK 529
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIE------------NIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 530 -HGLIgtqyEHLEHEKVREMVYNAAKMSNAHDFVSALPEGYetnvgergfllSGGQKQRIAIARAIVSDPKILLLDEATS 608
Cdd:PRK13545 108 lKGLM----MGLTKEKIKEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 609 ALD-TKSEGVVQAALDRAAQGRTTIVIAHRLSTIKT-ADKIVVMSQGRIVEQGTHNELLERKQAY---YN 673
Cdd:PRK13545 173 VGDqTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFlkkYN 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1083-1187 |
1.72e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.00 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1083 PEIDTWSSDGEKINNMEGH--IEFRNVHFRYPTRP--------EQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLER 1152
Cdd:PRK10261 293 EHPAKQEPPIEQDTVVDGEpiLQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLR 372
|
90 100 110
....*....|....*....|....*....|....*...
gi 407923078 1153 FYNPLTGGIYADGKEISSLN---INDYRSYIALVSQEP 1187
Cdd:PRK10261 373 LVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDP 410
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1102-1174 |
1.73e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 45.10 E-value: 1.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407923078 1102 IEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIN 1174
Cdd:COG4152 2 LELKGLTKRFGDKT---AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR 71
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1119-1172 |
2.28e-04 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.00 E-value: 2.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 407923078 1119 VLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN 1172
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD 78
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1105-1187 |
2.64e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.57 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1105 RNVHFRYPTR-----PEQPV--LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEI---SSLNIN 1174
Cdd:PRK11308 9 IDLKKHYPVKrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQK 88
|
90
....*....|...
gi 407923078 1175 DYRSYIALVSQEP 1187
Cdd:PRK11308 89 LLRQKIQIVFQNP 101
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
580-639 |
2.67e-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: 44.28 E-value: 2.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSE-GVVQAALDRAAQGRTTIVIAHRLS 639
Cdd:cd03236 140 LSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1117-1201 |
2.73e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 43.97 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1117 QPVLRGLNLSVKPGQYVALVGASGCGKST---TIALLERfynPLTGGIYADGKEIS---SLN-----INDYRSYIALVSQ 1185
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQ---PEAGTIRVGDITIDtarSLSqqkglIRQLRQHVGFVFQ 92
|
90
....*....|....*..
gi 407923078 1186 EPTLY-QGTIRDNILLG 1201
Cdd:PRK11264 93 NFNLFpHRTVLENIIEG 109
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1119-1172 |
2.75e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 44.04 E-value: 2.75e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 407923078 1119 VLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLN 1172
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLS 77
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1097-1201 |
2.81e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.16 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1097 NMEGHIEFRNVHFRYPtrpeqPV--LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNIN 1174
Cdd:PRK09700 1 MATPYISMAGIGKSFG-----PVhaLKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK 75
|
90 100
....*....|....*....|....*....
gi 407923078 1175 D-YRSYIALVSQEPTLY-QGTIRDNILLG 1201
Cdd:PRK09700 76 LaAQLGIGIIYQELSVIdELTVLENLYIG 104
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1110-1199 |
3.02e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.15 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1110 RYPTRPEQpVLRGLNLSVKPGQYVALVGASGCGKSTTI-ALLERFynpltggiyadgkEISSLNINDYRSyIALVSQEPT 1188
Cdd:PTZ00243 667 FFELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLqSLLSQF-------------EISEGRVWAERS-IAYVPQQAW 731
|
90
....*....|.
gi 407923078 1189 LYQGTIRDNIL 1199
Cdd:PTZ00243 732 IMNATVRGNIL 742
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
429-645 |
3.12e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 429 QGRVELRQVKHIYPSRPevtVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYdPVG--GEVLLDGvnvqelnlhwl 506
Cdd:PRK10938 258 EPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQGysNDLTLFG----------- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 507 RQQISlvqqepvlfATTIFDNIKH-GLIGTQYeHLEHE---KVREM----------VYNA---AKMSNAHDFVSALpeGY 569
Cdd:PRK10938 323 RRRGS---------GETIWDIKKHiGYVSSSL-HLDYRvstSVRNVilsgffdsigIYQAvsdRQQKLAQQWLDIL--GI 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 570 ETNVGERGFL-LSGGQkQRIA-IARAIVSDPKILLLDEATSALDTKSEGVVQAALDR-AAQGRTTIV------------I 634
Cdd:PRK10938 391 DKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacI 469
|
250
....*....|.
gi 407923078 635 AHRLSTIKTAD 645
Cdd:PRK10938 470 THRLEFVPDGD 480
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1102-1202 |
3.69e-04 |
|
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: 43.00 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPT-RPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALL--ERFYNPLTGGIYADGKEISSlninDYRS 1178
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagRKTAGVITGEILINGRPLDK----NFQR 79
|
90 100
....*....|....*....|....*
gi 407923078 1179 YIALVSQEPTLYQG-TIRDNILLGA 1202
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALRFSA 104
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
580-648 |
4.12e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 4.12e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407923078 580 LSGGQKQRIAIAR---AIVSDPKILLLDEATSALDTKS-EGVVQAALDRAAQGRTTIVIAHRLSTIKTADKIV 648
Cdd:PRK00635 810 LSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
580-669 |
4.48e-04 |
|
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: 44.62 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 LSGGQKQRIAIARAIVSDPK--ILLLDEATSALDTKSEGVVQAALDRAA-QGRTTIVIAHRLSTIKTADKIVVMSQ---- 652
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRdLGNTLIVVEHDEDTIRAADYVIDIGPgage 568
|
90
....*....|....*....
gi 407923078 653 --GRIVEQGTHNELLERKQ 669
Cdd:TIGR00630 569 hgGEVVASGTPEEILANPD 587
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
580-660 |
4.71e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 LSGGQKQRIAIAR--AIVSDPKIL-LLDEATSAL---DtksegvVQ---AALDR-AAQGRTTIVIAHRLSTIKTADKIVV 649
Cdd:COG0178 827 LSGGEAQRVKLASelSKRSTGKTLyILDEPTTGLhfhD------IRkllEVLHRlVDKGNTVVVIEHNLDVIKTADWIID 900
|
90
....*....|....*..
gi 407923078 650 M-----SQ-GRIVEQGT 660
Cdd:COG0178 901 LgpeggDGgGEIVAEGT 917
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
581-664 |
4.83e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 581 SGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQGRTTIVIAHRL--STIKTADKIVVMSQGRIVEQ 658
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVIDRGRVIAD 225
|
....*.
gi 407923078 659 GTHNEL 664
Cdd:NF000106 226 GKVDEL 231
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
580-671 |
8.48e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.91 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 580 LSGGQKQRIAIA-----RaivSDPKIL-LLDEATSALDT----KSEGVVQAALDraaQGRTTIVIAHRLSTIKTADKIVV 649
Cdd:PRK00349 831 LSGGEAQRVKLAkelskR---STGKTLyILDEPTTGLHFedirKLLEVLHRLVD---KGNTVVVIEHNLDVIKTADWIID 904
|
90 100
....*....|....*....|....*...
gi 407923078 650 M------SQGRIVEQGTHNELLERKQAY 671
Cdd:PRK00349 905 LgpeggdGGGEIVATGTPEEVAKVEASY 932
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
580-649 |
8.66e-04 |
|
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: 41.79 E-value: 8.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407923078 580 LSGGQKQRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRAAQ--GRTTIVIAHRLSTIK-TADKIVV 649
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDyLSDRIHV 144
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1104-1198 |
8.92e-04 |
|
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: 41.86 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1104 FRNVHFRYP-TRPEQPVLRGLNLSVKPGQYVALVGASGCGKST---TIALLERFYNPLTGGIYADGKEISSlNINDYRSY 1179
Cdd:cd03233 6 WRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKE-FAEKYPGE 84
|
90 100
....*....|....*....|...
gi 407923078 1180 IALVSQE----PTLyqgTIRDNI 1198
Cdd:cd03233 85 IIYVSEEdvhfPTL---TVRETL 104
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1116-1175 |
9.14e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 9.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 1116 EQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALL--ERFYNPLTGGIYADGKEISSLNIND 1175
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPED 74
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1117-1202 |
9.52e-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: 43.85 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1117 QPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSlNINDYRSYIALVSQEPTLYQG-TIR 1195
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVA 1021
|
....*..
gi 407923078 1196 DNILLGA 1202
Cdd:TIGR01257 1022 EHILFYA 1028
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1129-1208 |
9.76e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1129 PGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSLNINDYRSYIALVSQEPTLYQGTIRDNILLGADRENVP 1208
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
154-267 |
1.10e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 42.49 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 154 FVLYFVYLFIGEFFTCYIATVGWIYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVG-L 232
Cdd:cd18580 41 LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLdF 120
|
90 100 110
....*....|....*....|....*....|....*
gi 407923078 233 VQQSLATFITAFVIGFVKYWkltLILCSTIFAIVF 267
Cdd:cd18580 121 LQSLFSVLGSLIVIAIVSPY---FLIVLPPLLVVY 152
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
583-670 |
1.14e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 583 GQKQRIAIARAIVSDPKILLLDEATSaldtkseGVVQAALDR--------AAQGRTTIVI-------AHRlstiktADKI 647
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTS-------GVDPVARDMfwrllielSREDGVTIFIsthfmneAER------CDRI 467
|
90 100
....*....|....*....|...
gi 407923078 648 VVMSQGRIVEQGTHNELLERKQA 670
Cdd:NF033858 468 SLMHAGRVLASDTPAALVAARGA 490
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1101-1150 |
1.40e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 1.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 407923078 1101 HIEFRNVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALL 1150
Cdd:PRK10938 260 RIVLNNGVVSYN---DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI 306
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1102-1220 |
1.40e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1102 IEFRNVHFRYPTRPeqpVLRGLNLSVKPGQYVALVGASGCGKSTTIALLErfynpltGGIYADGKEISSLNindyRSYIA 1181
Cdd:PRK10636 2 IVFSSLQIRRGVRV---LLDNATATINPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSYTFPG----NWQLA 67
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 407923078 1182 LVSQE-PTLYQGTIrdNILLGADRENVPEEAIIKACKDAN 1220
Cdd:PRK10636 68 WVNQEtPALPQPAL--EYVIDGDREYRQLEAQLHDANERN 105
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
432-670 |
1.97e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 432 VELRQVKHIYPSRPevtVMNGVDLVVEAGKTTALVGASGSGKSTIVGLVERFYDPVGGEVlldgvnvqelnlHWLRQ-QI 510
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSENaNI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 511 SLVQQEPVL-FAT--TIFDNIkhgligTQYEHLEHEK--VREMVynaAKMSNAHDfvsalpegyetNVGERGFLLSGGQK 585
Cdd:PRK15064 385 GYYAQDHAYdFENdlTLFDWM------SQWRQEGDDEqaVRGTL---GRLLFSQD-----------DIKKSVKVLSGGEK 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 586 QRIAIARAIVSDPKILLLDEATSALDTKSEGVVQAALDRaAQGrTTIVIAH-R--LSTIKTadKIVVMSQGRIVE-QGTH 661
Cdd:PRK15064 445 GRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEK-YEG-TLIFVSHdRefVSSLAT--RIIEITPDGVVDfSGTY 520
|
....*....
gi 407923078 662 NELLERKQA 670
Cdd:PRK15064 521 EEYLRSQGI 529
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
107-267 |
2.56e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 41.40 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 107 VVSSICAIAAGAVLPLM------TVVFGSLSGTFQgmFQGTMSNGEFNDELVKFVLYFVYLFIGEFFTCYIATVGWIYVG 180
Cdd:cd18565 5 LLASILNRLFDLAPPLLigvaidAVFNGEASFLPL--VPASLGPADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 181 ERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEKVGLVQQSLATFITAFVIGFVKYWKLTLILCS 260
Cdd:cd18565 83 QRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALL 162
|
....*..
gi 407923078 261 TIFAIVF 267
Cdd:cd18565 163 PVPLIIA 169
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1104-1151 |
2.58e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 41.55 E-value: 2.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 407923078 1104 FRNVhfrYPTRPEQPVLRGLNLSVKPGQYVALVGASGCGKST---TIALLE 1151
Cdd:PRK11000 6 LRNV---TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTllrMIAGLE 53
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
178-368 |
2.64e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 41.42 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 178 YVGERISSRIREYYLSAILRQ----NVGYFDKLGAGEITTRItADANLVQDgisekvGLVQQSLATFI-TAFVIGFVKY- 251
Cdd:cd18782 64 YLFTDTANRIDLELGGTIIDHllrlPLGFFDKRPVGELSTRI-SELDTIRG------FLTGTALTTLLdVLFSVIYIAVl 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 252 ----WKLTLILCSTIFAIVFTMGGGSTFIMKYNKQSLASYALGGTVVEEVFSSIRNAVAFGTQDKLARQYNEHLviAEYW 327
Cdd:cd18782 137 fsysPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRY--ARSL 214
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 407923078 328 GKKMKTVLASMLGAMM--TIVYLNYGLAFWMGSRYLVKGEMSL 368
Cdd:cd18782 215 GEGFKLTVLGTTSGSLsqFLNKLSSLLVLWVGAYLVLRGELTL 257
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1119-1185 |
2.71e-03 |
|
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: 40.72 E-value: 2.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407923078 1119 VLRGLNLSVKPGQYVALVGASGCGKSTTIAL----LERFYNpLTGGIYADGKEissLNINDYRSYIALVSQ 1185
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAisgrVEGGGT-TSGQILFNGQP---RKPDQFQKCVAYVRQ 88
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1106-1199 |
2.74e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 40.32 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1106 NVHFRYPtrpEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYNPLTGGIYADGKEISSlNINDYRSYIALVSQ 1185
Cdd:PRK13540 6 ELDFDYH---DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGH 81
|
90
....*....|....*...
gi 407923078 1186 E----PTLyqgTIRDNIL 1199
Cdd:PRK13540 82 RsginPYL---TLRENCL 96
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
170-320 |
4.18e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 40.55 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 170 YIATVGWIyvGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITAD----ANLVQDGISEKVglvqQSLATFITAFV 245
Cdd:cd18546 59 QTRLTGRT--GERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDidalSELLQTGLVQLV----VSLLTLVGIAV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 246 IGFVKYWKLTLILCSTIFAIVFTmgggsTFImkYNKQSLASYALGGTVVEEV-------FSSIRNAVAFGTQDKLARQYN 318
Cdd:cd18546 133 VLLVLDPRLALVALAALPPLALA-----TRW--FRRRSSRAYRRARERIAAVnadlqetLAGIRVVQAFRRERRNAERFA 205
|
..
gi 407923078 319 EH 320
Cdd:cd18546 206 EL 207
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1120-1201 |
5.67e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 1120 LRGLNLSVKPGQYVALVGASGCGKSTTIALLERFYnP---LTGGIYADGKEISSLNINDY-RSYIALVSQE----PTLyq 1191
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKDIRDSeALGIVIIHQElaliPYL-- 93
|
90
....*....|
gi 407923078 1192 gTIRDNILLG 1201
Cdd:NF040905 94 -SIAENIFLG 102
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
104-269 |
5.95e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 40.16 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 104 IIIVVSSICAIAAGAVLPLMT-------VVFGSLSGtfqgmfqgtmsngefndeLVKFVLYFVYLF----IGEFFTCYIA 172
Cdd:cd18540 5 ILLIILMLLVALLDAVFPLLTkyaidhfITPGTLDG------------------LTGFILLYLGLIliqaLSVFLFIRLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407923078 173 tvgwIYVGERISSRIREYYLSAILRQNVGYFDKLGAGEITTRITADANLVQDGISEkvGLVQQSLATF--ITAFVIGFVK 250
Cdd:cd18540 67 ----GKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISW--GLVDLVWGITymIGILIVMLIL 140
|
170 180
....*....|....*....|
gi 407923078 251 YWKLTLILCSTI-FAIVFTM 269
Cdd:cd18540 141 NWKLALIVLAVVpVLAVVSI 160
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1102-1171 |
9.05e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.24 E-value: 9.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407923078 1102 IEFRNVHfryPTRPEQPVLRGLNLSVKPGQYVALVGASGCGKSTTIALLERF--YNPLTGGIYADGKEISSL 1171
Cdd:CHL00131 8 LEIKNLH---ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDL 76
|
|
| |
