|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-605 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 580.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 22 PSEVLRFYVYFLRQVWPVFLALLVVGLIVALIEVALFSYLGRIVDLAQSTPSAEFFRVhaneLIWMAVVALVLRPLFNAL 101
Cdd:COG1132 5 PRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLL----LLLLLLGLALLRALLSYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 102 HDMLVHqSINPSMTNLIRWQNHRYVLKQSLGFFQNDFAGRIAQRIMQTGNSLRDSAVQVVDALWHVLIYTVSALVLFAEA 181
Cdd:COG1132 81 QRYLLA-RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 182 DWRLMIPLVLWVFAYVGALAYFVPQVKRRSVEASDSRSKLMGRIVDGYTNITTLKLFAHTRQEEDYAREAIGDQTLKSQR 261
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 262 AGRVVTSMDVTITVMNGVLITGTTGLALWLWSQELISVGAIALATGLVIRINNMSGWIMWVVGGIFENIGQVQDGMQTIA 341
Cdd:COG1132 240 AARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 342 LPRKVVDREDAQPLRVERGEVEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILV 421
Cdd:COG1132 320 EPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 422 DGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERG 501
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPD-----GYDTVVGERG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 502 VKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAE 581
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
570 580
....*....|....*....|....
gi 15598424 582 SGTHAELLAHGGLYARLWQHQTGG 605
Cdd:COG1132 555 QGTHEELLARGGLYARLYRLQFGE 578
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-602 |
3.36e-130 |
|
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: 394.96 E-value: 3.36e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 12 PFRSASERMPPSEVLRFYVYFLRQVWPVFLALLVVGLIVALIEVALFSYLGRIVDLAQstpsaeffrvHANELIWMAVVA 91
Cdd:COG5265 11 AAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLS----------GAAALLVVPVGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 92 LV-------LRPLFNALHDML---VHQSInpsmTNLIRWQNHRYVLKQSLGFFQNdfagriaqRimQTGNSLRD--SAVQ 159
Cdd:COG5265 81 LLaygllrlLSVLFGELRDALfarVTQRA----VRRLALEVFRHLHALSLRFHLE--------R--QTGGLSRDieRGTK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 160 VVDALWHVLIYTV---------SALVLFAEADWRLMIPLVLWVFAYVgALAYFVPQ--VK-RRSVEASDSRSKlmGRIVD 227
Cdd:COG5265 147 GIEFLLRFLLFNIlptlleialVAGILLVKYDWWFALITLVTVVLYI-AFTVVVTEwrTKfRREMNEADSEAN--TRAVD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 228 GYTNITTLKLF-AHTRQEEDYareaigDQTLKSQRAGRVVTSmdVTITVMN---GVLITGTTGLALWL----WSQELISV 299
Cdd:COG5265 224 SLLNYETVKYFgNEAREARRY------DEALARYERAAVKSQ--TSLALLNfgqALIIALGLTAMMLMaaqgVVAGTMTV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 300 GAIALATGLVIRIN---NMSGWIMWVVGGIFENIGQVQDGMQTialPRKVVDREDAQPLRVERGEVEFEHIAFHYGKGSG 376
Cdd:COG5265 296 GDFVLVNAYLIQLYiplNFLGFVYREIRQALADMERMFDLLDQ---PPEVADAPDAPPLVVGGGEVRFENVSFGYDPERP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNL 456
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 457 LYGRPGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDS 536
Cdd:COG5265 453 AYGRPDASEEEVEAAARAAQIHDFIESLPD-----GYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598424 537 EVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARLWQHQ 602
Cdd:COG5265 528 RTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-603 |
2.72e-125 |
|
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: 385.73 E-value: 2.72e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 9 LIDPFRSASERMPPSEVLRFYVYFLRQVWPVFLALLVVGLIVALIEVALFSYLGRIVDLAQSTPSAEFFRVhaneLIWMA 88
Cdd:COG2274 127 LLEPTPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWV----LAIGL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 89 VVALVLRPLFNALHDMLV---HQSINpsmtnlIRWQNH--RYVLKQSLGFFQNDFAGRIAQRIMQTgNSLRDS-AVQVVD 162
Cdd:COG2274 203 LLALLFEGLLRLLRSYLLlrlGQRID------LRLSSRffRHLLRLPLSFFESRSVGDLASRFRDV-ESIREFlTGSLLT 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 163 ALWHVLIYTVSALVLFAeADWRLMIPLVLWVFAYVGALAYFVPQVKRRSVEASDSRSKLMGRIVDGYTNITTLKLFAHTR 242
Cdd:COG2274 276 ALLDLLFVLIFLIVLFF-YSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAES 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 243 QEEDYAREAIGDQTLKSQRAGRVVTSMDVTITVMNGVLITGTTGLALWLWSQELISVGAIALATGLVIRINN-----MSG 317
Cdd:COG2274 355 RFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLApvaqlIGL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 318 WIMWV-VGGIFENIGQVQDgmqtiaLPRKVVDREDAQPLRVERGEVEFEHIAFHYGKGSG-VIQGLDLKVRPGEKIGLVG 395
Cdd:COG2274 435 LQRFQdAKIALERLDDILD------LPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPpVLDNISLTIKPGERVAIVG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 396 PSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKA 475
Cdd:COG2274 509 RSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLA 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 476 RADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTV 555
Cdd:COG2274 589 GLHDFIEALPM-----GYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTV 663
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 15598424 556 IAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARLWQHQT 603
Cdd:COG2274 664 IIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
362-599 |
2.68e-113 |
|
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: 338.05 E-value: 2.68e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHY-GKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGM 440
Cdd:cd03251 1 VEFKNVTFRYpGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLK 520
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPE-----GYDTVIGERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARLW 599
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
362-602 |
3.81e-112 |
|
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: 334.97 E-value: 3.81e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMV 441
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKD 521
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPD-----GYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 522 APILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARLWQH 601
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
.
gi 15598424 602 Q 602
Cdd:cd03253 236 Q 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
149-598 |
1.34e-109 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 341.17 E-value: 1.34e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 149 TGNSLRdSAVQVVDALWHV--------LIYTVSALVLFAEA---DWRLMIPLVLWVFAYVgALAYFVpqVKR-----RSV 212
Cdd:PRK13657 112 SGRALH-TLLRGTDALFGLwlefmrehLATLVALVVLLPLAlfmNWRLSLVLVVLGIVYT-LITTLV--MRKtkdgqAAV 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 213 EASdsRSKLMGRIVDGYTNITTLKLFAHTRQEEDYAReAIGDQTLKSQRA-------GRVVTSMDVTITVMnGVLITGTt 285
Cdd:PRK13657 188 EEH--YHDLFAHVSDAIGNVSVVQSYNRIEAETQALR-DIADNLLAAQMPvlswwalASVLNRAASTITML-AILVLGA- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 286 glalWLWSQELISVGAI----ALATGLVIRINNMSGWImwvvGGIFENIGQVQDGMQTIALPRKVVDREDAQPLRVERGE 361
Cdd:PRK13657 263 ----ALVQKGQLRVGEVvafvGFATLLIGRLDQVVAFI----NQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGA 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHY-GKGSGViQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGM 440
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAV 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLK 520
Cdd:PRK13657 414 VFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPD-----GYDTVVGERGRQLSGGERQRLAIARALLK 488
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARL 598
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
32-598 |
5.33e-107 |
|
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: 333.98 E-value: 5.33e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 32 FLRQVWPVFLALLVVGLIVALIEVALFSYLGRIVDLAQSTPSAEFFrvhaNELIWMAVVALVLRPLFNALHDMLVhQSIN 111
Cdd:TIGR02204 12 FVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLL----NRYFAFLLVVALVLALGTAARFYLV-TWLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 112 PSMTNLIRWQNHRYVLKQSLGFFQNDFAGRIAQRI------MQT--GNS----LRdSAVQVVDALWHVLIYTV--SALVL 177
Cdd:TIGR02204 87 ERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLttdttlLQSviGSSlsmaLR-NALMCIGGLIMMFITSPklTSLVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 178 faeadwrLMIPLVLwvfayvGALAYFVPQVKRRSVEASDSRSKLMGRIVDGYTNITTLKLFAHtrqeEDYAREAIGDQTL 257
Cdd:TIGR02204 166 -------LAVPLVL------LPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGH----EDAERSRFGGAVE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 258 KSQRAGRVVTSMDVTITVMNGVLITGTTGLALWLWSQELISvGAIALATglvirinnMSGWIMWVV------GGIFENIG 331
Cdd:TIGR02204 229 KAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIA-GKMSAGT--------LGQFVFYAVmvagsiGTLSEVWG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 332 QVQD---GMQTIA--LPRKVVDREDAQPLRVE---RGEVEFEHIAFHYGKGSG--VIQGLDLKVRPGEKIGLVGPSGAGK 401
Cdd:TIGR02204 300 ELQRaagAAERLIelLQAEPDIKAPAHPKTLPvplRGEIEFEQVNFAYPARPDqpALDGLNLTVRPGETVALVGPSGAGK 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 402 STLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFI 481
Cdd:TIGR02204 380 STLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFI 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 482 PLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHR 561
Cdd:TIGR02204 460 SALPE-----GYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHR 534
|
570 580 590
....*....|....*....|....*....|....*..
gi 15598424 562 LSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARL 598
Cdd:TIGR02204 535 LATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
362-602 |
1.44e-104 |
|
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: 315.63 E-value: 1.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYG--KGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIG 439
Cdd:cd03249 1 IEFKNVSFRYPsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVLL 519
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPD-----GYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 520 KDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARLW 599
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
...
gi 15598424 600 QHQ 602
Cdd:cd03249 236 KAQ 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
360-593 |
6.18e-97 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 295.67 E-value: 6.18e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 360 GEVEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIG 439
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVLL 519
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPN-----GYDTVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 520 KDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGG 593
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
163-601 |
1.18e-96 |
|
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: 306.69 E-value: 1.18e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 163 ALWHVLIYTVSALVLfaeadWRLMIPLVLWVFAYVGALAYFVPQV-----KRRSVEASDSRSKLMGRIVDGYTNITTLKL 237
Cdd:COG4987 136 LLVALLVILAAVAFL-----AFFSPALALVLALGLLLAGLLLPLLaarlgRRAGRRLAAARAALRARLTDLLQGAAELAA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 238 FAHTRQEEDYAREAIGDQTLKSQRAGRVVTSMDVTITVMNGVLITGTTGLALWLWSQELISVGAIALATGLVIrinnmsg 317
Cdd:COG4987 211 YGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAAL------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 318 wimwvvgGIFENIGQVQDGMQ----TIALPRKVVDREDAQPLRVERGE---------VEFEHIAFHY-GKGSGVIQGLDL 383
Cdd:COG4987 284 -------ALFEALAPLPAAAQhlgrVRAAARRLNELLDAPPAVTEPAEpapapggpsLELEDVSFRYpGAGRPVLDGLSL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 384 KVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGA 463
Cdd:COG4987 357 TLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDA 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 464 SDAELMEAVRKARADEFIpllsdAEGRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQ 543
Cdd:COG4987 437 TDEELWAALERVGLGDWL-----AALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALL 511
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 544 ESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARLWQH 601
Cdd:COG4987 512 ADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
340-593 |
4.43e-95 |
|
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: 302.45 E-value: 4.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 340 IALPRKVVDREDAQPLRVERGEVEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRI 419
Cdd:COG4988 315 LDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 420 LVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGE 499
Cdd:COG4988 395 LINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPD-----GLDTPLGE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 500 RGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHI 579
Cdd:COG4988 470 GGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRI 549
|
250
....*....|....
gi 15598424 580 AESGTHAELLAHGG 593
Cdd:COG4988 550 VEQGTHEELLAKNG 563
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
34-602 |
1.39e-94 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 301.64 E-value: 1.39e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 34 RQVWPV---FLALLVVGLIVALIEVALFSYLGRIV-DLAQSTpsaeFFRVHANELIWM--AVVAL-VLRPLFNALHDMLV 106
Cdd:TIGR02203 3 RRLWSYvrpYKAGLVLAGVAMILVAATESTLAALLkPLLDDG----FGGRDRSVLWWVplVVIGLaVLRGICSFVSTYLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 107 HQSINPSMTNLIRWQNHRYvLKQSLGFFQNDFAGRIAQRI-----MQTGNS-------LRDSAVqvVDALWHVLIYTvsa 174
Cdd:TIGR02203 79 SWVSNKVVRDIRVRMFEKL-LGLPVSFFDRQPTGTLLSRItfdseQVASAAtdafivlVRETLT--VIGLFIVLLYY--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 175 lvlfaeaDWRLMIPLVLWVFAYVGALAYFVPQVKRRSVEASDSRSKLMGRIVDGYTNITTLKLFAHTRQEE---DYAREA 251
Cdd:TIGR02203 153 -------SWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETrrfDAVSNR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 252 IGDQTLKSQRAGRVVTSM-DVTITVMNGVLITgttgLALWLWSQELISVGAIA---LATGLVIR-------INNMSGWIM 320
Cdd:TIGR02203 226 NRRLAMKMTSAGSISSPItQLIASLALAVVLF----IALFQAQAGSLTAGDFTafiTAMIALIRplksltnVNAPMQRGL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 321 WVVGGIFENIGQ---VQDGmqTIALPRKvvdredaqplrveRGEVEFEHIAFHY-GKGSGVIQGLDLKVRPGEKIGLVGP 396
Cdd:TIGR02203 302 AAAESLFTLLDSppeKDTG--TRAIERA-------------RGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 397 SGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPG-ASDAELMEAVRKA 475
Cdd:TIGR02203 367 SGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 476 RADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTV 555
Cdd:TIGR02203 447 YAQDFVDKLPL-----GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT 521
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 15598424 556 IAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARLWQHQ 602
Cdd:TIGR02203 522 LVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
123-604 |
6.67e-89 |
|
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: 290.11 E-value: 6.67e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 123 HRYVLKQSLGFFQNDFAGRIAQRIM---QTGNSLRDSAVQVVDALWHVLIY---------TVSALVLFAeadwrLMIPLV 190
Cdd:TIGR01846 219 YRHLLGLPLGYFESRRVGDTVARVReleQIRNFLTGSALTVVLDLLFVVVFlavmffyspTLTGVVIGS-----LVCYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 191 LWVFAyvgalayfVPQVKRRSVEASDSRSKLMGRIVDGYTNITTLKLFAHTRQEEDYAREAIGDQTLKSQRAGRVVTSMD 270
Cdd:TIGR01846 294 LSVFV--------GPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAG 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 271 VTITVMNGVlitgTTGLALWlWSQELISVGAiaLATGLVIRINNMSGWimwVVGGIFENIGQVQDGMQT-IALPR--KVV 347
Cdd:TIGR01846 366 QAIELIQKL----TFAILLW-FGAHLVIGGA--LSPGQLVAFNMLAGR---VTQPVLRLAQLWQDFQQTgIALERlgDIL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 348 D------REDAQPLRVERGEVEFEHIAFHYGKGSG-VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRIL 420
Cdd:TIGR01846 436 NspteprSAGLAALPELRGAITFENIRFRYAPDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 421 VDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIpllsdAEGRRGFDAHVGER 500
Cdd:TIGR01846 516 VDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFI-----SELPQGYNTEVGEK 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 501 GVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIA 580
Cdd:TIGR01846 591 GANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIA 670
|
490 500
....*....|....*....|....
gi 15598424 581 ESGTHAELLAHGGLYARLWQHQTG 604
Cdd:TIGR01846 671 ESGRHEELLALQGLYARLWQQQSG 694
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
362-602 |
7.97e-86 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 267.43 E-value: 7.97e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHY-GKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGM 440
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIpllsdAEGRRGFDAHVGERGVKLSGGQRQRIAIARVLLK 520
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFI-----SELPEGYDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARLWQ 600
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
..
gi 15598424 601 HQ 602
Cdd:cd03252 236 LQ 237
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
332-605 |
4.29e-83 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 271.51 E-value: 4.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 332 QVQDGM---QTIAlprKVVDRE---DAQPLRVER--GEVEFEHIAFHY-GKGSGVIQGLDLKVRPGEKIGLVGPSGAGKS 402
Cdd:PRK11176 307 QFQRGMaacQTLF---AILDLEqekDEGKRVIERakGDIEFRNVTFTYpGKEVPALRNINFKIPAGKTVALVGRSGSGKS 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 403 TLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGA-SDAELMEAVRKARADEFI 481
Cdd:PRK11176 384 TIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFI 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 482 PLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHR 561
Cdd:PRK11176 464 NKMDN-----GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHR 538
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 15598424 562 LSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARLWQHQTGG 605
Cdd:PRK11176 539 LSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
362-578 |
3.73e-79 |
|
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: 247.68 E-value: 3.73e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHY-GKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGM 440
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTSLLHRSIRDNLLygrpgasdaelmeavrkaradefipllsdaegrrgfdahvgergvklSGGQRQRIAIARVLLK 520
Cdd:cd03228 81 VPQDPFLFSGTIRENIL-----------------------------------------------SGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGH 578
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
182-598 |
4.23e-76 |
|
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: 253.27 E-value: 4.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 182 DWRLMIPLVLWVFAYVGALAYFVPQVKRRSVEASDSRSKLMGRIVDGYTNITTL----KLFAHTRQEEDYAREAIGDQT- 256
Cdd:TIGR01192 155 DWRLSIVLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVhsynRIEAETSALKQFTNNLLSAQYp 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 257 -LKSQRAGRVVTSMDVTITVMnGVLITGTTglalwLWSQELISVGA----IALATGLVIRINNMSGWIMWvvggIFENIG 331
Cdd:TIGR01192 235 vLDWWALASGLNRMASTISMM-CILVIGTV-----LVIKGELSVGEviafIGFANLLIGRLDQMSGFITQ----IFEARA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 332 QVQDGMQtiaLPRKVVDRE---DAQPLRVERGEVEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLL 408
Cdd:TIGR01192 305 KLEDFFD---LEDSVFQREepaDAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 409 LRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIpllsdAE 488
Cdd:TIGR01192 382 QRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFI-----LK 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 489 GRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARM 568
Cdd:TIGR01192 457 RSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNA 536
|
410 420 430
....*....|....*....|....*....|
gi 15598424 569 DRLVVLDKGHIAESGTHAELLAHGGLYARL 598
Cdd:TIGR01192 537 DLVLFLDQGRLIEKGSFQELIQKDGRFYKL 566
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
32-598 |
8.23e-75 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 252.72 E-value: 8.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 32 FLRQVWPVFLALLVVGLIVALIEVALFSYLGRIVDLAQSTPSAEFFrvhANELIWMAVVALVlRPLFNALHDmlvhQSIN 111
Cdd:TIGR00958 155 LSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPAL---ASAIFFMCLLSIA-SSVSAGLRG----GSFN 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 112 PSMTNL---IRWQNHRYVLKQSLGFFQNDFAGRIAQRIMQTGNSLRDSAVQVVDALWHVLIYTVSALVLFAEADWRLMIP 188
Cdd:TIGR00958 227 YTMARInlrIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMV 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 189 LVLWVFAYVGALAYFVPQVKRRSVEASDSRSKLMGRIVDGYTNITTLKLFAHTRQEEDYAREAIgDQTLKSQRAGRVVTS 268
Cdd:TIGR00958 307 TLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEAL-EETLQLNKRKALAYA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 269 MDVTITVMNGVLITGTTglaLWLWSQeLISVGAIALATGLVIRINNMSgwimwvVGGIFENIGQVQDG-MQTIALPRKV- 346
Cdd:TIGR00958 386 GYLWTTSVLGMLIQVLV---LYYGGQ-LVLTGKVSSGNLVSFLLYQEQ------LGEAVRVLSYVYSGmMQAVGASEKVf 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 347 --VDREDAQPLRVE------RGEVEFEHIAFHYGKGSG--VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLES 416
Cdd:TIGR00958 456 eyLDRKPNIPLTGTlaplnlEGLIEFQDVSFSYPNRPDvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 417 GRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIpllsdAEGRRGFDAH 496
Cdd:TIGR00958 536 GQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFI-----MEFPNGYDTE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 497 VGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLEtlMQGKTVIAIAHRLSTIARMDRLVVLDK 576
Cdd:TIGR00958 611 VGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKK 688
|
570 580
....*....|....*....|..
gi 15598424 577 GHIAESGTHAELLAHGGLYARL 598
Cdd:TIGR00958 689 GSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
323-602 |
1.34e-71 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 240.88 E-value: 1.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 323 VGGIFENIGQVqdgmqtIALPRKVVDREDAQP---------LRVERGEVEFEHIAFHY-GKGSGVIQGLDLKVRPGEKIG 392
Cdd:PRK11160 297 VAGAFQHLGQV------IASARRINEITEQKPevtfpttstAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVA 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 393 LVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDAELMEAV 472
Cdd:PRK11160 371 LLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 473 RKaradefIPLLSDAEGRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQG 552
Cdd:PRK11160 451 QQ------VGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN 524
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15598424 553 KTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARLWQHQ 602
Cdd:PRK11160 525 KTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
354-579 |
3.44e-71 |
|
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: 228.89 E-value: 3.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 354 PLRVErGEVEFEHIAFHYGK--GSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQ 431
Cdd:cd03248 5 PDHLK-GIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 432 ESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQR 511
Cdd:cd03248 84 KYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELAS-----GYDTEVGEKGSQLSGGQKQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 512 IAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHI 579
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
84-598 |
2.82e-69 |
|
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: 237.92 E-value: 2.82e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 84 LIWMAVVALVLRPLFNALHDM-LVHQSINPSMTNLIRWQNHryVLKQSLGFFQNDFAGRIAQRiMQTGNSLRDS-AVQVV 161
Cdd:TIGR03796 196 LLLGMGLTALLQGVLTWLQLYyLRRLEIKLAVGMSARFLWH--ILRLPVRFFAQRHAGDIASR-VQLNDQVAEFlSGQLA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 162 DALWHVLIYTVSALVLFAeADWRLMipLVLWVFAYVGALAYFVpqVKRRSVEASDS----RSKLMGRIVDGYTNITTLKL 237
Cdd:TIGR03796 273 TTALDAVMLVFYALLMLL-YDPVLT--LIGIAFAAINVLALQL--VSRRRVDANRRlqqdAGKLTGVAISGLQSIETLKA 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 238 fahTRQEEDYAREAIGDQT------LKSQRAGRVVTSMDVTITVMNGVLITGTTGlalWLWSQELISVGAIALATGLVIR 311
Cdd:TIGR03796 348 ---SGLESDFFSRWAGYQAkllnaqQELGVLTQILGVLPTLLTSLNSALILVVGG---LRVMEGQLTIGMLVAFQSLMSS 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 312 ----INNMSGwimwVVGGIFE---NIGQVQDGMQ---TIALPRKVVDREDAQPLRVERGEVEFEHIAFHYGK-GSGVIQG 380
Cdd:TIGR03796 422 flepVNNLVG----FGGTLQElegDLNRLDDVLRnpvDPLLEEPEGSAATSEPPRRLSGYVELRNITFGYSPlEPPLIEN 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 381 LDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGR 460
Cdd:TIGR03796 498 FSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWD 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 461 PGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVES 540
Cdd:TIGR03796 578 PTIPDADLVRACKDAAIHDVITSRPG-----GYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEK 652
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 541 AIQESLETlmQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARL 598
Cdd:TIGR03796 653 IIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
360-584 |
3.08e-69 |
|
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: 223.52 E-value: 3.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 360 GEVEFEHIAFHYGKGSG-VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQI 438
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLLHRSIRDNL-LYGRpgASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARV 517
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLdPFGE--YSDEELWQALERVGLKEFVESLPG-----GLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 518 LLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGT 584
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
360-579 |
3.09e-66 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 215.53 E-value: 3.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 360 GEVEFEHIAFHY-GKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQI 438
Cdd:cd03245 1 GRIEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVL 518
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPN-----GLDLQIGERGRGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598424 519 LKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHI 579
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
361-574 |
1.89e-62 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 215.23 E-value: 1.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 361 EVEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGM 440
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLsdaegRRGFDAHVGERGVKLSGGQRQRIAIARVLLK 520
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAAL-----PQGLDTPIGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVL 574
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
381-604 |
5.30e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 210.09 E-value: 5.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 381 LDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLEsGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGR 460
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 461 PGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVES 540
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQ-----GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 541 AIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARLWQHQTG 604
Cdd:PRK11174 523 LVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-601 |
3.73e-59 |
|
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: 3.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 23 SEVLRFYVYFLRQVWPVFLaLLVVGLIVALIEVALFSYLGRIVDLAQSTPSAEFFRVHANELIwmavVALVLRPLFNALH 102
Cdd:TIGR01193 142 NSLLKFIPLITRQKKLIVN-IVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLI----IAYIIQQILSYIQ 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 103 DMLVHQ-SINPSMTNLIRWQNHryVLKQSLGFFQNDFAGRIAQRImqtgnslrDSAVQVVDALWHV---------LIYTV 172
Cdd:TIGR01193 217 IFLLNVlGQRLSIDIILSYIKH--LFELPMSFFSTRRTGEIVSRF--------TDASSIIDALASTilslfldmwILVIV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 173 SALVLFAEADWRLMIPLVLWVFAYVGALayFVPQVKRRSVEASDSRSKLMGRIVDGYTNITTLKLF---AHTRQEEDYAR 249
Cdd:TIGR01193 287 GLFLVRQNMLLFLLSLLSIPVYAVIIIL--FKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLtseAERYSKIDSEF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 250 EAIGDQTLKSQRAGRVVTSMDVTITVMNGVLItgttglaLWLWSQELISvGAIALatGLVIRINNMSGWIMwvvgGIFEN 329
Cdd:TIGR01193 365 GDYLNKSFKYQKADQGQQAIKAVTKLILNVVI-------LWTGAYLVMR-GKLTL--GQLITFNALLSYFL----TPLEN 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 330 IGQVQDGMQT--IALPR----KVVDRE-----DAQPLRVERGEVEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSG 398
Cdd:TIGR01193 431 IINLQPKLQAarVANNRlnevYLVDSEfinkkKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSG 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 399 AGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYG-RPGASDAELMEAVRKARA 477
Cdd:TIGR01193 511 SGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEI 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 478 DEFIPLLSdaegrRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLeTLMQGKTVIA 557
Cdd:TIGR01193 591 KDDIENMP-----LGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIF 664
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 15598424 558 IAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARLWQH 601
Cdd:TIGR01193 665 VAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
127-602 |
9.34e-59 |
|
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: 208.66 E-value: 9.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 127 LKQSLGFFQNDFAGRIAQRIM---QTGNSLRDSAVQVVDALwhvlIYTVSALVLFAEADWRLM---IPLVLWVFAYVGAL 200
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASRAMgisQIRRILSGSTLTTLLSG----IFALLNLGLMFYYSWKLAlvaVALALVAIAVTLVL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 201 AYFVPQVKRRSVEASDSRSKLMGRIVDGYTNITT-----------LKLFAHTRQEEdyareaigdqtLKSQRAGRVVTSM 269
Cdd:TIGR03797 296 GLLQVRKERRLLELSGKISGLTVQLINGISKLRVagaenrafarwAKLFSRQRKLE-----------LSAQRIENLLTVF 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 270 DVTITVMNGVLITGttgLALWLWSQELISVGA-IALATGLVIRINNMSGWIMWVVGgIFENIGQVQDgMQTI--ALPRkv 346
Cdd:TIGR03797 365 NAVLPVLTSAALFA---AAISLLGGAGLSLGSfLAFNTAFGSFSGAVTQLSNTLIS-ILAVIPLWER-AKPIleALPE-- 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 347 VDREDAQPLRVeRGEVEFEHIAFHYGKGSGVI-QGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQD 425
Cdd:TIGR03797 438 VDEAKTDPGKL-SGAIEVDRVTFRYRPDGPLIlDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 426 IAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDaELMEAVRKARADEFI---PLlsdaegrrGFDAHVGERGV 502
Cdd:TIGR03797 517 LAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLD-EAWEAARMAGLAEDIramPM--------GMHTVISEGGG 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 503 KLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLmqGKTVIAIAHRLSTIARMDRLVVLDKGHIAES 582
Cdd:TIGR03797 588 TLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQ 665
|
490 500
....*....|....*....|
gi 15598424 583 GTHAELLAHGGLYARLWQHQ 602
Cdd:TIGR03797 666 GTYDELMAREGLFAQLARRQ 685
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
206-602 |
1.49e-55 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 197.63 E-value: 1.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 206 QVKRRSVEASDSRSKLMGRIVDGYTNITTLKLFA-HTRQEEDYAREAIgDQTLKSQRAGRVVTSMDVTITV---MNGVLI 281
Cdd:PRK10789 160 QLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGlEDRQSALFAADAE-DTGKKNMRVARIDARFDPTIYIaigMANLLA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 282 TGTTGLALWLWSQELISVGAIALATGLVIrinnmsgWIMWVVGGIFeNIgqVQDG-------MQTIALPRKVVDREdaQP 354
Cdd:PRK10789 239 IGGGSWMVVNGSLTLGQLTSFVMYLGLMI-------WPMLALAWMF-NI--VERGsaaysriRAMLAEAPVVKDGS--EP 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 355 LRVERGEVEFEHIAFHYGKGSG-VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQES 433
Cdd:PRK10789 307 VPEGRGELDVNIRQFTYPQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 434 LRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSdaegrRGFDAHVGERGVKLSGGQRQRIA 513
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLP-----QGYDTEVGERGVMLSGGQKQRIS 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 514 IARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGG 593
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
....*....
gi 15598424 594 LYARLWQHQ 602
Cdd:PRK10789 542 WYRDMYRYQ 550
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
358-584 |
9.68e-55 |
|
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: 184.92 E-value: 9.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 358 ERGEVEFEHIAFHYGKG-SGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRA 436
Cdd:cd03369 3 EHGEIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 437 QIGMVTQDTSLLHRSIRDNL-LYGRpgASDAELMEAVRkaradefipllsdaegrrgfdahVGERGVKLSGGQRQRIAIA 515
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR-----------------------VSEGGLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 516 RVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGT 584
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
350-605 |
3.12e-53 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 191.86 E-value: 3.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 350 EDAQPLrvERGEVEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGV 429
Cdd:PRK10790 331 NDDRPL--QSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 430 TQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPgASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQR 509
Cdd:PRK10790 409 SHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPD-----GLYTPLGEQGNNLSVGQK 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 510 QRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELL 589
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
250
....*....|....*.
gi 15598424 590 AHGGLYARLWQHQTGG 605
Cdd:PRK10790 563 AAQGRYWQMYQLQLAG 578
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
341-562 |
1.14e-51 |
|
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: 186.03 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 341 ALPRKVVDREDAQPLRVERGEVEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRIL 420
Cdd:TIGR02868 314 AGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 421 VDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGER 500
Cdd:TIGR02868 394 LDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPD-----GLDTVLGEG 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598424 501 GVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRL 562
Cdd:TIGR02868 469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
341-591 |
6.32e-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: 180.87 E-value: 6.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 341 ALPRKVVDREDAQPLRVERGEV-EFEHIAFHYGKGSG----VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLE 415
Cdd:COG1123 239 AVPRLGAARGRAAPAAAAAEPLlEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 416 SGRILVDGQDIAGVTQESLRA---QIGMVTQD--TSLLHR-SIRDNL-----LYGRPGASD-----AELMEAVRkarade 479
Cdd:COG1123 319 SGSILFDGKDLTKLSRRSLRElrrRVQMVFQDpySSLNPRmTVGDIIaeplrLHGLLSRAErrervAELLERVG------ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 480 fipLLSDAEGRRGFDahvgergvkLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIA 557
Cdd:COG1123 393 ---LPPDLADRYPHE---------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLF 460
|
250 260 270
....*....|....*....|....*....|....*
gi 15598424 558 IAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:COG1123 461 ISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
362-591 |
1.14e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 166.74 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMV 441
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQ--DTSLLHRSIRDNLLYGrP---GASDAELMEAVRKArADEFipllsDAEGRRGFDAHvgergvKLSGGQRQRIAIAR 516
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFG-PenlGLPREEIRERVEEA-LELV-----GLEHLADRPPH------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 517 VLLKDAPILILDEATSALDSEVESAIQESLETL-MQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFSD 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
362-590 |
4.49e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 165.24 E-value: 4.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGViQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEsLRAQIGMV 441
Cdd:COG1131 1 IEVRGLTKRYGDKTAL-DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSL-LHRSIRDNL-----LYGRPGasdaelmeAVRKARADEFIPL--LSDAEGRRgfdahVGergvKLSGGQRQRIA 513
Cdd:COG1131 79 PQEPALyPDLTVRENLrffarLYGLPR--------KEARERIDELLELfgLTDAADRK-----VG----TLSGGMKQRLG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 514 IARVLLKDAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLA 590
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKA 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
349-591 |
1.77e-46 |
|
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: 172.24 E-value: 1.77e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 349 REDAQPLRVERGEVEFEHIAFHY-GKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIA 427
Cdd:COG4618 318 EPERMPLPRPKGRLSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 428 GVTQESLRAQIGMVTQDTSLLHRSIRDNLlyGR-PGASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSG 506
Cdd:COG4618 398 QWDREELGRHIGYLPQDVELFDGTIAENI--ARfGDADPEKVVAAAKLAGVHEMILRLPD-----GYDTRIGEGGARLSG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 507 GQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETL-MQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTH 585
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPR 550
|
....*.
gi 15598424 586 AELLAH 591
Cdd:COG4618 551 DEVLAR 556
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
362-583 |
2.43e-46 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 161.33 E-value: 2.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHY-GKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVtQESLRAQIGM 440
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTSLLHRSIRDNLlygrpgasdaelmeavrkaradefipllsdaeGRRgfdahvgergvkLSGGQRQRIAIARVLLK 520
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------GRR------------FSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESG 583
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
126-604 |
6.89e-45 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 172.08 E-value: 6.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 126 VLKQSLGFFQNDFAGRIAQR----IMQTGNSLRDSAVQVVDALWH-----VLIYTVSALVLfaeadWRLMIPLVLWVFAY 196
Cdd:PLN03232 993 ILRAPMLFFHTNPTGRVINRfskdIGDIDRNVANLMNMFMNQLWQllstfALIGTVSTISL-----WAIMPLLILFYAAY 1067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 197 VgalaYFvpQVKRRSVEASDSRSK-----LMGRIVDGYTNITTLKLFahtrqeeDYAREAIGDQTLKSQRAGRVVTSMDV 271
Cdd:PLN03232 1068 L----YY--QSTSREVRRLDSVTRspiyaQFGEALNGLSSIRAYKAY-------DRMAKINGKSMDNNIRFTLANTSSNR 1134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 272 TITV----MNGVLITGTTGLALWLWSQELISVGaIALATGLVIrinNMSGWIMWVVGGIFENIGQVQDGMQTIALPRKVV 347
Cdd:PLN03232 1135 WLTIrletLGGVMIWLTATFAVLRNGNAENQAG-FASTMGLLL---SYTLNITTLLSGVLRQASKAENSLNSVERVGNYI 1210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 348 DREDAQPLRVE----------RGEVEFEHIAFHYGKG-SGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLES 416
Cdd:PLN03232 1211 DLPSEATAIIEnnrpvsgwpsRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEK 1290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 417 GRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLlygRPGA--SDAELMEAVRKARadefiplLSDAEGRR--G 492
Cdd:PLN03232 1291 GRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSehNDADLWEALERAH-------IKDVIDRNpfG 1360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 493 FDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLV 572
Cdd:PLN03232 1361 LDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKIL 1440
|
490 500 510
....*....|....*....|....*....|..
gi 15598424 573 VLDKGHIAESGTHAELLAHGGLYARLWQHQTG 604
Cdd:PLN03232 1441 VLSSGQVLEYDSPQELLSRDTSAFFRMVHSTG 1472
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
362-583 |
1.98e-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: 157.67 E-value: 1.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSG---VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESL---R 435
Cdd:cd03257 2 LEVKNLSVSFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 436 AQIGMVTQD--TSL-LHRSIRDNLlygrpgasdAELMEAVRKARADEFIPLLSdAEGRRGF---DAHVGERGVKLSGGQR 509
Cdd:cd03257 82 KEIQMVFQDpmSSLnPRMTIGEQI---------AEPLRIHGKLSKKEARKEAV-LLLLVGVglpEEVLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 510 QRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETL--MQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
126-595 |
4.18e-44 |
|
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: 169.74 E-value: 4.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 126 VLKQSLGFFQNDFAGRIAQRIMQTGNSLRDSAVQVVDALWHVLIYTVSALVLFAeadwrLMIPLVLWVFAYVGALAYFVP 205
Cdd:TIGR00957 1048 KLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVIL-----LATPIAAVIIPPLGLLYFFVQ 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 206 --------QVKRRSveaSDSRSKLMGRIVDGYTNITTLKLFahtRQEEDYarEAIGDQTL-KSQRA--GRVVTSMDVTIT 274
Cdd:TIGR00957 1123 rfyvassrQLKRLE---SVSRSPVYSHFNETLLGVSVIRAF---EEQERF--IHQSDLKVdENQKAyyPSIVANRWLAVR 1194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 275 ---VMNGVLITGttglALW-LWSQELISVGAIALATGLVIRINNMSGWIMWVVGGIFENIGQVQDgmqtialPRKVVDRE 350
Cdd:TIGR00957 1195 lecVGNCIVLFA----ALFaVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVER-------LKEYSETE 1263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 351 DAQPLRVE----------RGEVEFEHIAFHYGKG-SGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRI 419
Cdd:TIGR00957 1264 KEAPWQIQetappsgwppRGRVEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI 1343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 420 LVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNL-LYGRpgASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVG 498
Cdd:TIGR00957 1344 IIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQ--YSDEEVWWALELAHLKTFVSALPD-----KLDHECA 1416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 499 ERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGH 578
Cdd:TIGR00957 1417 EGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGE 1496
|
490
....*....|....*..
gi 15598424 579 IAESGTHAELLAHGGLY 595
Cdd:TIGR00957 1497 VAEFGAPSNLLQQRGIF 1513
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
362-581 |
4.28e-44 |
|
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: 156.48 E-value: 4.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSG---VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVtqeslRAQI 438
Cdd:cd03293 1 LEVRNVSKTYGGGGGavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLL-HRSIRDNLLYG--RPGASDAElmeavRKARADEFIPL--LSDAEGRRGFDahvgergvkLSGGQRQRIA 513
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNVALGleLQGVPKAE-----ARERAEELLELvgLSGFENAYPHQ---------LSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 514 IARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDK--GHIAE 581
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDEAVFLaDRVVVLSArpGRIVA 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
363-579 |
5.39e-44 |
|
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: 154.68 E-value: 5.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYGKGSG-VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMV 441
Cdd:cd03246 2 EVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLLHRSIRDNLLygrpgasdaelmeavrkaradefipllsdaegrrgfdahvgergvklSGGQRQRIAIARVLLKD 521
Cdd:cd03246 82 PQDDELFSGSIAENIL-----------------------------------------------SGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 522 APILILDEATSALDSEVESAIQESLETL-MQGKTVIAIAHRLSTIARMDRLVVLDKGHI 579
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
378-532 |
5.48e-44 |
|
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: 153.96 E-value: 5.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 378 IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLL-HRSIRDNL 456
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598424 457 LYgrpGASDAELMEAVRKARADEFIPLLSDAEGRrgfDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATS 532
Cdd:pfam00005 81 RL---GLLLKGLSKREKDARAEEALEKLGLGDLA---DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
362-591 |
7.57e-44 |
|
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: 7.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSG---VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQI 438
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQD--TSL-----LHRSIRDNL-LYGRPGASD--AELMEAVrkaradefipllsdaegrrGFDAHVGERGV-KLSGG 507
Cdd:COG1124 82 QMVFQDpyASLhprhtVDRILAEPLrIHGLPDREEriAELLEQV-------------------GLPPSFLDRYPhQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 508 QRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGT 584
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELT 222
|
....*..
gi 15598424 585 HAELLAH 591
Cdd:COG1124 223 VADLLAG 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
362-591 |
1.75e-43 |
|
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: 155.92 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMV 441
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLL-HRSIRDNL-----LYGRPgasdaelmEAVRKARADEFIPLLS-DAEGRRGFDAHvgergvKLSGGQRQRIAI 514
Cdd:cd03295 81 IQQIGLFpHMTVEENIalvpkLLKWP--------KEKIRERADELLALVGlDPAEFADRYPH------ELSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 515 ARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLaDRIAIMKNGEIVQVGTPDEILRS 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
362-581 |
4.11e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 155.25 E-value: 4.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSG---VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGvtqesLRAQI 438
Cdd:COG1116 8 LELRGVSKRFPTGGGgvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLL-HRSIRDNLLYGRP--GASDAElmeavRKARADEFIPL--LSDAEgrrgfDAHVGErgvkLSGGQRQRIA 513
Cdd:COG1116 83 GVVFQEPALLpWLTVLDNVALGLElrGVPKAE-----RRERARELLELvgLAGFE-----DAYPHQ----LSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 514 IARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAH------RLStiarmDRLVVLDK--GHIAE 581
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFLA-----DRVVVLSArpGRIVE 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
363-578 |
5.73e-43 |
|
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: 153.39 E-value: 5.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYGKGSG-VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMV 441
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQ--DTSLLHRSIRDNLLYGRP--GASDAElMEAVRKARADEFipLLSDAEGRRGFDahvgergvkLSGGQRQRIAIARV 517
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLEnlGLPEEE-IEERVEEALELV--GLEGLRDRSPFT---------LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 518 LLKDAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIAR-MDRLVVLDKGH 578
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
362-591 |
2.47e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 155.62 E-value: 2.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLD---LKVRPGEKIGLVGPSGAGKSTLV---NLLLRlYDleSGRILVDGQDIAGVTQESLR 435
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDdvsLTIEKGEIFGIIGYSGAGKSTLIrciNLLER-PT--SGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 436 A---QIGMVTQDTSLLH-RSIRDNLLYgrP----GASDAElmeavRKARADEFIPL--LSDAEgrrgfDAHVGErgvkLS 505
Cdd:COG1135 79 AarrKIGMIFQHFNLLSsRTVAENVAL--PleiaGVPKAE-----IRKRVAELLELvgLSDKA-----DAYPSQ----LS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 506 GGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIqesLETLMQ-----GKTVIAIAHRLSTIARM-DRLVVLDKGHI 579
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSI---LDLLKDinrelGLTIVLITHEMDVVRRIcDRVAVLENGRI 219
|
250
....*....|..
gi 15598424 580 AESGTHAELLAH 591
Cdd:COG1135 220 VEQGPVLDVFAN 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
363-593 |
2.75e-42 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 152.32 E-value: 2.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEsLRAQIGMVT 442
Cdd:COG4555 3 EVENLSKKYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 443 QDTSL-LHRSIRDNLLYgrpGASDAELMEAVRKARADEFIPLLsdaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKD 521
Cdd:COG4555 81 DERGLyDRLTVRENIRY---FAELYGLFDEELKKRIEELIELL-------GLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 522 APILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAHGG 593
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
363-579 |
2.90e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.12 E-value: 2.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVT 442
Cdd:COG4619 2 ELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 443 QDTSLLHRSIRDNLLYGRPGASDAELMEAVRKaradefipLLSdaegRRGFDAHVGERGVK-LSGGQRQRIAIARVLLKD 521
Cdd:COG4619 81 QEPALWGGTVRDNLPFPFQLRERKFDRERALE--------LLE----RLGLPPDILDKPVErLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 522 APILILDEATSALDSE----VESAIQESLETlmQGKTVIAIAHRLSTIARM-DRLVVLDKGHI 579
Cdd:COG4619 149 PDVLLLDEPTSALDPEntrrVEELLREYLAE--EGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
360-593 |
3.55e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 163.76 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 360 GEVEFEHIAFHYGKG-SGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQI 438
Cdd:PLN03130 1236 GSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLLHRSIRDNLlygRPGA--SDAELMEAVRKARadefiplLSDAEGR--RGFDAHVGERGVKLSGGQRQRIAI 514
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNL---DPFNehNDADLWESLERAH-------LKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSL 1385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 515 ARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGG 593
Cdd:PLN03130 1386 ARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
362-591 |
1.13e-41 |
|
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: 150.42 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSG---VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRA-- 436
Cdd:cd03258 2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 437 -QIGMVTQDTSLL-HRSIRDNLLYgrP----GASDAElmeavRKARADEFIPLLsDAEGRRgfDAHVGErgvkLSGGQRQ 510
Cdd:cd03258 82 rRIGMIFQHFNLLsSRTVFENVAL--PleiaGVPKAE-----IEERVLELLELV-GLEDKA--DAYPAQ----LSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 511 RIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAE 587
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEE 227
|
....
gi 15598424 588 LLAH 591
Cdd:cd03258 228 VFAN 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
362-583 |
3.54e-41 |
|
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: 148.44 E-value: 3.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEslRAQIGMV 441
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLL-HRSIRDNLLYgrpGASDAELMEAVRKARADEFIPLLsdaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLK 520
Cdd:cd03259 78 FQDYALFpHLTVAENIAF---GLKLRGVPKAEIRARVRELLELV-------GLEGLLNRYPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETLM--QGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQreLGITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
362-579 |
8.56e-41 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 147.64 E-value: 8.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSG---VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESL---- 434
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 435 RAQIGMVTQDTSLL-HRSIRDN-----LLYGRPGASdaelmeavRKARADEfipLLsdaeGRRGFDAHVGERGVKLSGGQ 508
Cdd:cd03255 81 RRHIGFVFQSFNLLpDLTALENvelplLLAGVPKKE--------RRERAEE---LL----ERVGLGDRLNHYPSELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 509 RQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETL--MQGKTVIAIAHRLSTIARMDRLVVLDKGHI 579
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
362-587 |
9.28e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 147.51 E-value: 9.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQES---LRAQI 438
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLL-HRSIRDNLLYgrP----GASDAELMEAVRKA--------RADEFIPllsdaegrrgfdahvgergvKLS 505
Cdd:COG2884 82 GVVFQDFRLLpDRTVYENVAL--PlrvtGKSRKEIRRRVREVldlvglsdKAKALPH--------------------ELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 506 GGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETL-MQGKTVIaIA-HRLSTIARMD-RLVVLDKGHIAES 582
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVL-IAtHDLELVDRMPkRVLELEDGRLVRD 218
|
....*
gi 15598424 583 GTHAE 587
Cdd:COG2884 219 EARGV 223
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
362-589 |
1.36e-40 |
|
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: 148.27 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMV 441
Cdd:COG1120 2 LEAENLSVGYGGRP-VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLLHR-SIRDNLLYGR---------PGASDAEL-MEAVRKARADEFipllsdAEgrRGFDAhvgergvkLSGGQRQ 510
Cdd:COG1120 81 PQEPPAPFGlTVRELVALGRyphlglfgrPSAEDREAvEEALERTGLEHL------AD--RPVDE--------LSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 511 RIAIARVLLKDAPILILDEATSALD----SEVESAIQEslETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTH 585
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRR--LARERGRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPP 222
|
....
gi 15598424 586 AELL 589
Cdd:COG1120 223 EEVL 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
362-583 |
1.62e-40 |
|
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: 146.94 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLE-----SGRILVDGQDIAG--VTQESL 434
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 435 RAQIGMVTQDTSLLHRSIRDNLLYG---RPGASDAELMEAVRKA--RADefiplLSDAEGRRgfdAHVGErgvkLSGGQR 509
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlHGIKLKEELDERVEEAlrKAA-----LWDEVKDR---LHALG----LSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598424 510 QRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFG 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
362-581 |
2.17e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.73 E-value: 2.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSG---VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESL---- 434
Cdd:COG1136 5 LELRNLTKSYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 435 RAQIGMVTQDTSLL-HRSIRDN----LLYGrpGASDAElmeavRKARADEFIPLLsdaegrrGFDAHVGERGVKLSGGQR 509
Cdd:COG1136 85 RRHIGFVFQFFNLLpELTALENvalpLLLA--GVSRKE-----RRERARELLERV-------GLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 510 QRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARMDRLVVLDKGHIAE 581
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
362-591 |
3.15e-40 |
|
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: 153.91 E-value: 3.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSG-VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLE---SGRILVDGQDIAGVTQESLRAQ 437
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 438 IGMVTQD--TSLLHRSIRDNLLYGrpgasdAELMEAVRKARADEFIPLLSDAEGRRGFDAHVGErgvkLSGGQRQRIAIA 515
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEA------LENLGLSRAEARARVLELLEAVGLERRLDRYPHQ----LSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 516 RVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILAA 233
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
255-591 |
8.90e-40 |
|
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: 152.89 E-value: 8.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 255 QTLKSQRAGRVvtsMDVTITVMNgVLITGTTGLALWLWSQELISVGAIALATGLVIRI-----NNMSGWimwvvggifEN 329
Cdd:TIGR01842 217 QSAASDRAGML---SNLSKYFRI-VLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRAlapidGAIGGW---------KQ 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 330 IGQVQDGMQTIA-LPRKVVDREDAQPLRVERGEVEFEHIAF-HYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNL 407
Cdd:TIGR01842 284 FSGARQAYKRLNeLLANYPSRDPAMPLPEPEGHLSVENVTIvPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 408 LLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDa 487
Cdd:TIGR01842 364 IVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPD- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 488 egrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETL-MQGKTVIAIAHRLSTIA 566
Cdd:TIGR01842 443 ----GYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLG 518
|
330 340
....*....|....*....|....*
gi 15598424 567 RMDRLVVLDKGHIAESGTHAELLAH 591
Cdd:TIGR01842 519 CVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
362-601 |
1.05e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.62 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVtqeslRAQIGMV 441
Cdd:COG1121 7 IELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTS-------------LLHRSIRDNLLyGRPGASDAEL-MEAVRKARADEFIpllsdaegrrgfDAHVGErgvkLSGG 507
Cdd:COG1121 81 PQRAEvdwdfpitvrdvvLMGRYGRRGLF-RRPSRADREAvDEALERVGLEDLA------------DRPIGE----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 508 QRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETL-MQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAeSGTH 585
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYfDRVLLLNRGLVA-HGPP 222
|
250
....*....|....*.
gi 15598424 586 AELLAHGGLyARLWQH 601
Cdd:COG1121 223 EEVLTPENL-SRAYGG 237
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
370-591 |
2.93e-39 |
|
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: 146.35 E-value: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 370 HYGKGSGVIQ---GLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYD---LESGRILVDGQDIAGVTQESLRA----QIG 439
Cdd:COG0444 10 YFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKirgrEIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQD--TSL---------LHRSIRDNLLYGRPGASD--AELMEAVRkaradefiplLSDAEGRrgFDAHVGErgvkLSG 506
Cdd:COG0444 90 MIFQDpmTSLnpvmtvgdqIAEPLRIHGGLSKAEAREraIELLERVG----------LPDPERR--LDRYPHE----LSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 507 GQRQRIAIARVLLKDAPILILDEATSALDSEVESAIqesLETLMQ-----GKTVIAIAHRLSTIARM-DRLVVLDKGHIA 580
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQI---LNLLKDlqrelGLAILFITHDLGVVAEIaDRVAVMYAGRIV 230
|
250
....*....|.
gi 15598424 581 ESGTHAELLAH 591
Cdd:COG0444 231 EEGPVEELFEN 241
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
362-577 |
8.11e-39 |
|
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: 141.84 E-value: 8.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSG----VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQdIAGVTQESLraq 437
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IAYVSQEPW--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 438 igmvtqdtsLLHRSIRDNLLYGRPgaSDAELMEAVRKA---RADefIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAI 514
Cdd:cd03250 77 ---------IQNGTIRENILFGKP--FDEERYEKVIKAcalEPD--LEILPD-----GDLTEIGEKGINLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598424 515 ARVLLKDAPILILDEATSALDSEVESAIQES--LETLMQGKTVIAIAHRLSTIARMDRLVVLDKG 577
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
362-579 |
9.25e-39 |
|
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: 140.23 E-value: 9.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGvTQESLRAQIGMV 441
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLLHR-SIRDNLlygrpgasdaelmeavrkaradefipllsdaegrrgfdahvgergvKLSGGQRQRIAIARVLLK 520
Cdd:cd03230 79 PEEPSLYENlTVRENL----------------------------------------------KLSGGMKQRLALAQALLH 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARM-DRLVVLDKGHI 579
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
362-578 |
2.00e-38 |
|
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: 139.63 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQES--LRAQIG 439
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQDTSLL-HRSIRDNLLYGrpgasdaelmeavrkaradefipllsdaegrrgfdahvgergvkLSGGQRQRIAIARVL 518
Cdd:cd03229 80 MVFQDFALFpHLTVLENIALG--------------------------------------------LSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 519 LKDAPILILDEATSALDSEVESAIQESLETL--MQGKTVIAIAHRLSTIARM-DRLVVLDKGH 578
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
363-578 |
3.45e-38 |
|
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: 138.15 E-value: 3.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVT 442
Cdd:cd00267 1 EIENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 443 QdtsllhrsirdnllygrpgasdaelmeavrkaradefipllsdaegrrgfdahvgergvkLSGGQRQRIAIARVLLKDA 522
Cdd:cd00267 80 Q------------------------------------------------------------LSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 523 PILILDEATSALDSEVESAIQESLETLMQ-GKTVIAIAHRLSTIAR-MDRLVVLDKGH 578
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
362-591 |
7.26e-38 |
|
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: 7.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEslRAQIGMV 441
Cdd:COG3842 6 LELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLL-HRSIRDNLLYG--RPGASDAElmeavRKARADEFIPL--LSDAEGRRgfdahVGErgvkLSGGQRQRIAIAR 516
Cdd:COG3842 83 FQDYALFpHLTVAENVAFGlrMRGVPKAE-----IRARVAELLELvgLEGLADRY-----PHQ----LSGGQQQRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 517 VLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLS---TIArmDRLVVLDKGHIAESGTHAELLAH 591
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHDQEealALA--DRIAVMNDGRIEQVGTPEEIYER 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
344-597 |
2.10e-37 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 149.41 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 344 RKVVDREDAQPLRVE-----RGEVEFEHIAFHYGKGSGV--IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLE- 415
Cdd:PTZ00265 1143 KSNIDVRDNGGIRIKnkndiKGKIEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKn 1222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 416 -----------------------------------------------------SGRILVDGQDIAGVTQESLRAQIGMVT 442
Cdd:PTZ00265 1223 dhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVS 1302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 443 QDTSLLHRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDAegrrgFDAHVGERGVKLSGGQRQRIAIARVLLKDA 522
Cdd:PTZ00265 1303 QEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNK-----YDTNVGPYGKSLSGGQKQRIAIARALLREP 1377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 523 PILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARMDRLVVLDK----GHIAES-GTHAELL-AHGGL 594
Cdd:PTZ00265 1378 KILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLsVQDGV 1457
|
...
gi 15598424 595 YAR 597
Cdd:PTZ00265 1458 YKK 1460
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
123-588 |
3.17e-37 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 148.77 E-value: 3.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 123 HRYVLKQ----SLGFFQNDFAGRIAQR----IMQTGNSLRDSAVQVVDALWHVLiytVSALVLFAEAdwrlmiPLVLWVF 194
Cdd:PTZ00243 1034 HRDLLRSvsrgTMSFFDTTPLGRILNRfsrdIDILDNTLPMSYLYLLQCLFSIC---SSILVTSASQ------PFVLVAL 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 195 AYVGALAYFVPQ--------VKRRSVEASDSRSKLMGRIVDGYTNITTLKLfAHTRQEEDYAREAIGDQTLKSQRAG--- 263
Cdd:PTZ00243 1105 VPCGYLYYRLMQfynsanreIRRIKSVAKSPVFTLLEEALQGSATITAYGK-AHLVMQEALRRLDVVYSCSYLENVAnrw 1183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 264 ---RVVTSMDVTITVmngVLITGTTGLALWLWSQElisVGAIALATGLVIRINNMSGWIMWVVGGIFENIGQVQDGMQTI 340
Cdd:PTZ00243 1184 lgvRVEFLSNIVVTV---IALIGVIGTMLRATSQE---IGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYT 1257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 341 ------------ALPRKVVDRE------------------DAQPLRVERGEVEFEHIAFHYGKG-SGVIQGLDLKVRPGE 389
Cdd:PTZ00243 1258 devphedmpeldEEVDALERRTgmaadvtgtvviepasptSAAPHPVQAGSLVFEGVQMRYREGlPLVLRGVSFRIAPRE 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 390 KIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLlygRP--GASDAE 467
Cdd:PTZ00243 1338 KVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPflEASSAE 1414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 468 LMEAVRKARADEFIPllSDAEgrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILIL-DEATSALDSEVESAIQESL 546
Cdd:PTZ00243 1415 VWAALELVGLRERVA--SESE---GIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATV 1489
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15598424 547 ETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAEL 588
Cdd:PTZ00243 1490 MSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
362-591 |
4.60e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 137.82 E-value: 4.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQE--SLRAQIG 439
Cdd:COG1126 2 IEIENLHKSFGDLE-VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQDTSLL-HRSIRDNLLYGrP----GASDAelmEAVRKARAdefipLLSdaegRRGFDAHVGERGVKLSGGQRQRIAI 514
Cdd:COG1126 81 MVFQQFNLFpHLTVLENVTLA-PikvkKMSKA---EAEERAME-----LLE----RVGLADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 515 ARVLLKDAPILILDEATSALDSEVesaIQESLETLMQ----GKTVIAIAHRLS---TIArmDRLVVLDKGHIAESGTHAE 587
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPEL---VGEVLDVMRDlakeGMTMVVVTHEMGfarEVA--DRVVFMDGGRIVEEGPPEE 222
|
....
gi 15598424 588 LLAH 591
Cdd:COG1126 223 FFEN 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
362-591 |
1.01e-36 |
|
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: 136.86 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQE---SLRAQI 438
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQD----TSLlhrSIRDNL---LYGRPGASDAELMEAVRkaradEFIPL--LSDAEgrrgfDAHVGErgvkLSGGQR 509
Cdd:cd03261 80 GMLFQSgalfDSL---TVFENVafpLREHTRLSEEEIREIVL-----EKLEAvgLRGAE-----DLYPAE----LSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 510 QRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETL--MQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHA 586
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPE 222
|
....*
gi 15598424 587 ELLAH 591
Cdd:cd03261 223 ELRAS 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
362-591 |
1.44e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 136.76 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKgSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAG--VTQESLRAQIG 439
Cdd:PRK09493 2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQDTSLL-HRSIRDNLLYGrP----GASDAelmEAVRKARAdefipLLsdaeGRRGFDAHVGERGVKLSGGQRQRIAI 514
Cdd:PRK09493 81 MVFQQFYLFpHLTALENVMFG-PlrvrGASKE---EAEKQARE-----LL----AKVGLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 515 ARVLLKDAPILILDEATSALDSEVEsaiQESLeTLMQ-----GKTVIAIAHRLStIARM--DRLVVLDKGHIAESGTHAE 587
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELR---HEVL-KVMQdlaeeGMTMVIVTHEIG-FAEKvaSRLIFIDKGRIAEDGDPQV 222
|
....
gi 15598424 588 LLAH 591
Cdd:PRK09493 223 LIKN 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
360-598 |
2.07e-36 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 136.96 E-value: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 360 GEVEFEHIAFHYGKG-SGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQI 438
Cdd:cd03288 18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLLHRSIRDNLLYGRPgASDAELMEAVRKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVL 518
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPG-----GLDAVVTEGGENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 519 LKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAH-GGLYAR 597
Cdd:cd03288 172 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGVFAS 251
|
.
gi 15598424 598 L 598
Cdd:cd03288 252 L 252
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
362-579 |
2.29e-36 |
|
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: 135.35 E-value: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQE--SLRAQIG 439
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQDTSLL-HRSIRDNLLYG---RPGASDAelmEAVRKARAdefipLLsdaeGRRGFDAHVGERGVKLSGGQRQRIAIA 515
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLApikVKGMSKA---EAEERALE-----LL----EKVGLADKADAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 516 RVLLKDAPILILDEATSALDSEVesaIQESLETLMQ----GKTVIAIAHRLStIAR--MDRLVVLDKGHI 579
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPEL---VGEVLDVMKDlaeeGMTMVVVTHEMG-FARevADRVIFMDDGRI 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
382-591 |
4.14e-36 |
|
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: 136.23 E-value: 4.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 382 DLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRA----QIGMVTQDTSLL-HRSIRDNL 456
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 457 LYGrpgASDAELMEAVRKARADEFIPLLsdaeGRRGF-DAHVGErgvkLSGGQRQRIAIARVLLKDAPILILDEATSALD 535
Cdd:cd03294 124 AFG---LEVQGVPRAEREERAAEALELV----GLEGWeHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 536 SEVESAIQESLETL--MQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:cd03294 193 PLIRREMQDELLRLqaELQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
363-588 |
4.22e-36 |
|
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: 135.39 E-value: 4.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESL---RAQIG 439
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQDTSLLHR-SIRDNLLYGRPGAsdaelMEAVRKaradeFIPLLSDAEGRRGFDA--HVG------ERGVKLSGGQRQ 510
Cdd:cd03256 82 MIFQQFNLIERlSVLENVLSGRLGR-----RSTWRS-----LFGLFPKEEKQRALAAleRVGlldkayQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 511 RIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLStIAR--MDRLVVLDKGHIAESGTHA 586
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVD-LAReyADRIVGLKDGRIVFDGPPA 230
|
..
gi 15598424 587 EL 588
Cdd:cd03256 231 EL 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
362-591 |
8.66e-36 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 137.62 E-value: 8.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLD---LKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRA-- 436
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNnvsLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 437 -QIGMVTQDTSLLH-RSIRDNL-----LYGRPgasdaelmEAVRKARADEFIPLLSDAEGRRGFDAhvgergvKLSGGQR 509
Cdd:PRK11153 82 rQIGMIFQHFNLLSsRTVFDNValpleLAGTP--------KAEIKARVTELLELVGLSDKADRYPA-------QLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 510 QRIAIARVLLKDAPILILDEATSALDSEVESAIqesLETLMQ-----GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSI---LELLKDinrelGLTIVLITHEMDVVKRIcDRVAVIDAGRLVEQG 223
|
....*...
gi 15598424 584 THAELLAH 591
Cdd:PRK11153 224 TVSEVFSH 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
362-590 |
8.86e-36 |
|
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: 134.34 E-value: 8.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQE---SLRAQI 438
Cdd:COG1127 6 IEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQD----TSLlhrSIRDNLLYG---RPGASDAELMEAVRKAradefipLlsdaegrrgfdAHVGERGVK------LS 505
Cdd:COG1127 85 GMLFQGgalfDSL---TVFENVAFPlreHTDLSEAEIRELVLEK-------L-----------ELVGLPGAAdkmpseLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 506 GGQRQRIAIARVLLKDAPILILDEATSALD----SEVESAIQESLETLmqGKTVIAIAHRLSTIARM-DRLVVLDKGHIA 580
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDpitsAVIDELIRELRDEL--GLTSVVVTHDLDSAFAIaDRVAVLADGKII 221
|
250
....*....|
gi 15598424 581 ESGTHAELLA 590
Cdd:COG1127 222 AEGTPEELLA 231
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
362-588 |
1.18e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 134.41 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESL---RAQI 438
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLLHR-SIRDNLLYGRPGAsdaelmeaVRKARAdeFIPLLSDAEGRRGFDA--------HVGERGVKLSGGQR 509
Cdd:COG3638 83 GMIFQQFNLVPRlSVLTNVLAGRLGR--------TSTWRS--LLGLFPPEDRERALEAlervgladKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 510 QRIAIARVLLKDAPILILDEATSALDseVESAiQESLETLMQ-----GKTVIAIAHRLStIARM--DRLVVLDKGHIAES 582
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLD--PKTA-RQVMDLLRRiaredGITVVVNLHQVD-LARRyaDRIIGLRDGRVVFD 228
|
....*.
gi 15598424 583 GTHAEL 588
Cdd:COG3638 229 GPPAEL 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
362-588 |
1.72e-35 |
|
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: 133.52 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEslRAQIGMV 441
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLL-HRSIRDNLLYgrpGASDAELMEAVRKARADEFIPLLsdaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLK 520
Cdd:cd03300 78 FQNYALFpHLTVFENIAF---GLRLKKLPKAEIKERVAEALDLV-------QLEGYANRKPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAEL 588
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTMsDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
363-583 |
5.99e-35 |
|
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: 130.25 E-value: 5.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVT 442
Cdd:cd03214 1 EVENLSVGYGGRT-VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 443 QdtsllhrsirdnllygrpgasdaelmeAVRKARADEFIpllsdaegRRGFDAhvgergvkLSGGQRQRIAIARVLLKDA 522
Cdd:cd03214 80 Q---------------------------ALELLGLAHLA--------DRPFNE--------LSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 523 PILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
370-590 |
1.03e-34 |
|
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: 131.02 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 370 HYGKgSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGV-TQESLRAQIGMVTQDTSLL 448
Cdd:cd03224 9 GYGK-SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERARAGIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 449 HR-SIRDNLL---YGRPGASDAELMEAVrkarADEFiPLLSDAEGRRGFDahvgergvkLSGGQRQRIAIARVLLKDAPI 524
Cdd:cd03224 88 PElTVEENLLlgaYARRRAKRKARLERV----YELF-PRLKERRKQLAGT---------LSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 525 LILDEATSALDSEVESAIQESLETL-MQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLA 590
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELrDEGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
355-590 |
2.55e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 130.26 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 355 LRVERGEVEFEHIAFHYgkgsgviqglDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGvTQESL 434
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF----------DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 435 RAqIGMVTQDTSLL-HRSIRDNLLYG-RPGASdaeLMEAVRKAradefiplLSDAEGRRGFDAHVGERGVKLSGGQRQRI 512
Cdd:COG3840 71 RP-VSMLFQENNLFpHLTVAQNIGLGlRPGLK---LTAEQRAQ--------VEQALERVGLAGLLDRLPGQLSGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 513 AIARVLLKDAPILILDEATSALD--------SEVESAIQEsletlmQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDpalrqemlDLVDELCRE------RGLTVLMVTHDPEDAARIaDRVLLVADGRIAADG 212
|
....*..
gi 15598424 584 THAELLA 590
Cdd:COG3840 213 PTAALLD 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
362-592 |
7.42e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.14 E-value: 7.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHY-GKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGM 440
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQ--DTSLLHRSIRDNLLYG--RPGASDAELME----AVRKARADEFIpllsDAEGRRgfdahvgergvkLSGGQRQRI 512
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGleNIGVPREEMVErvdqALRQVGMEDFL----NREPHR------------LSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 513 AIARVLLKDAPILILDEATSALDSEvesAIQESLETLMQGK-----TVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAE 587
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPR---GRREVLETVRQLKeqkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
....*
gi 15598424 588 LLAHG 592
Cdd:PRK13635 227 IFKSG 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
363-580 |
1.59e-33 |
|
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: 127.26 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVtqeslRAQIGMVT 442
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 443 QDTSLLHR---SIRDNLLYGR---------PGASD-AELMEAVRKARADEFIpllsdaegrrgfDAHVGErgvkLSGGQR 509
Cdd:cd03235 75 QRRSIDRDfpiSVRDVVLMGLyghkglfrrLSKADkAKVDEALERVGLSELA------------DRQIGE----LSGGQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 510 QRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETL-MQGKTVIAIAHRLSTIAR-MDRLVVLDKGHIA 580
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
351-591 |
2.66e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 130.24 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 351 DAQPLrvergeVEFEHIAFHYGKGSGVIQ----------GLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRIL 420
Cdd:COG4608 3 MAEPL------LEVRDLKKHFPVRGGLFGrtvgvvkavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 421 VDGQDIAGVTQESLRA---QIGMVTQD--TSLLHR-SIRD--------NLLYGRPGASD--AELMEAVRkaradefipLL 484
Cdd:COG4608 77 FDGQDITGLSGRELRPlrrRMQMVFQDpyASLNPRmTVGDiiaeplriHGLASKAERRErvAELLELVG---------LR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 485 SDAEGRRgfdAHvgergvKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRL 562
Cdd:COG4608 148 PEHADRY---PH------EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDelGLTYLFISHDL 218
|
250 260 270
....*....|....*....|....*....|
gi 15598424 563 STIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:COG4608 219 SVVRHIsDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
365-579 |
5.52e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 125.45 E-value: 5.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 365 EHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAgvtQESLRAQIGMVTQD 444
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 445 TS--LLHRSIRDNLLYGRPGASDaelmeavRKARADEFIPL--LSDAEGRRGFDahvgergvkLSGGQRQRIAIARVLLK 520
Cdd:cd03226 80 VDyqLFTDSVREELLLGLKELDA-------GNEQAETVLKDldLYALKERHPLS---------LSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARM-DRLVVLDKGHI 579
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
362-583 |
1.77e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.92 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKgSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLE-----SGRILVDGQDI--AGVTQESL 434
Cdd:COG1117 12 IEVRNLNVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIydPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 435 RAQIGMVTQDTSLLHRSIRDNLLYG---RPGASDAELMEAVRKA--RA---DEfiplLSDaegrrgfdaHVGERGVKLSG 506
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVAYGlrlHGIKSKSELDEIVEESlrKAalwDE----VKD---------RLKKSALGLSG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 507 GQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVsDYTAFFYLGELVEFG 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
143-596 |
3.26e-32 |
|
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: 133.53 E-value: 3.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 143 AQRIMQTG---NSLRDSAVQVVDALWhVLIYTVSALVLFAEADWRLMIPLVLWVfaYVGALAYFVPQVKRRsveasDSRS 219
Cdd:TIGR00957 425 AQRFMDLAtyiNMIWSAPLQVILALY-FLWLNLGPSVLAGVAVMVLMVPLNAVM--AMKTKTYQVAHMKSK-----DNRI 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 220 KLMGRIVDGytnITTLKLFAHTRQEEDYArEAIGDQTLKSQRAGRVVTSMDVTITVMNGVLITGTTgLALWLWSQELISV 299
Cdd:TIGR00957 497 KLMNEILNG---IKVLKLYAWELAFLDKV-EGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALIT-FAVYVTVDENNIL 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 300 GA----IALATGLVIRINnmsgwiMWVVGGIFENIGQVQDGMQTIalpRKVVDREDAQPLRVERGEVE--------FEHI 367
Cdd:TIGR00957 572 DAekafVSLALFNILRFP------LNILPMVISSIVQASVSLKRL---RIFLSHEELEPDSIERRTIKpgegnsitVHNA 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 368 AFHYGKG-SGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRIlvdgqdiagvtqeSLRAQIGMVTQDTS 446
Cdd:TIGR00957 643 TFTWARDlPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAW 709
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 447 LLHRSIRDNLLYGRPgasdaelMEAVRKARADEFIPLLSDAEGRRGFD-AHVGERGVKLSGGQRQRIAIARVLLKDAPIL 525
Cdd:TIGR00957 710 IQNDSLRENILFGKA-------LNEKYYQQVLEACALLPDLEILPSGDrTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 526 ILDEATSALDSEVESAIQESL---ETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYA 596
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFA 856
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
360-591 |
9.39e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 126.34 E-value: 9.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 360 GEVEFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVtqESLRAQIG 439
Cdd:COG3839 2 ASLELENVSKSYGGVE-ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL--PPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQDTSLL-HRSIRDNLLYG---RpGASDAELMEAVRKArAD--EFIPLLsdaegrrgfDAHVGErgvkLSGGQRQRIA 513
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlklR-KVPKAEIDRRVREA-AEllGLEDLL---------DRKPKQ----LSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 514 IARVLLKDAPILILDEATSALD--------SEVeSAIQESLetlmqGKTVIAIAHRLS---TIArmDRLVVLDKGHIAES 582
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrvemrAEI-KRLHRRL-----GTTTIYVTHDQVeamTLA--DRIAVMNDGRIQQV 215
|
....*....
gi 15598424 583 GTHAELLAH 591
Cdd:COG3839 216 GTPEELYDR 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
362-583 |
3.13e-31 |
|
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: 120.94 E-value: 3.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQ---GLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESlRAQI 438
Cdd:cd03266 2 ITADALTKRFRDVKKTVQavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA-RRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLLHR-SIRDNLLY--GRPGASDAELmeavrKARADEFIPLLsdaegrrGFDAHVGERGVKLSGGQRQRIAIA 515
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYfaGLYGLKGDEL-----TARLEELADRL-------GMEELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 516 RVLLKDAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
381-583 |
3.95e-31 |
|
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: 120.68 E-value: 3.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 381 LDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAgvTQESLRAQIGMVTQDTSLL-HRSIRDNLLYG 459
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFaHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 460 R-PGAsdaELMEAVRKAradefiplLSDAEGRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEV 538
Cdd:cd03298 95 LsPGL---KLTAEDRQA--------IEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598424 539 ESAIQESLETL--MQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:cd03298 164 RAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
362-588 |
4.23e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.06 E-value: 4.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVT-QESLRAQIGM 440
Cdd:COG1129 5 LEMRGISKSFG-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTSLL-HRSIRDNLLYGR----PGASDAELMEavRKARAdefipLLSdaegRRGFDAHVGERGVKLSGGQRQRIAIA 515
Cdd:COG1129 84 IHQELNLVpNLSVAENIFLGReprrGGLIDWRAMR--RRARE-----LLA----RLGLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 516 RVLLKDAPILILDEATSAL-DSEVesaiqESLETLM-----QGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAEL 588
Cdd:COG1129 153 RALSRDARVLILDEPTASLtEREV-----ERLFRIIrrlkaQGVAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVAEL 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
379-591 |
1.21e-30 |
|
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: 126.34 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 379 QGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLydLES-GRILVDGQDIAGVTQE---SLRAQIGMVTQD--TSL----- 447
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRL--IPSeGEIRFDGQDLDGLSRRalrPLRRRMQVVFQDpfGSLsprmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 448 LHRSIRDNLLYGRPGASDAElmeavRKARADEfipLLSDAegrrGFDAHVGERGV-KLSGGQRQRIAIARVLLKDAPILI 526
Cdd:COG4172 381 VGQIIAEGLRVHGPGLSAAE-----RRARVAE---ALEEV----GLDPAARHRYPhEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 527 LDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLAVVRALaHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
362-593 |
1.35e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 122.63 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQeSLRAQIGMV 441
Cdd:PRK13536 42 IDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR-LARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQ-DTSLLHRSIRDNLL-YGRPGASDAELMEAVrkaradefIP-LLSDAEGRRGFDAHVGErgvkLSGGQRQRIAIARVL 518
Cdd:PRK13536 120 PQfDNLDLEFTVRENLLvFGRYFGMSTREIEAV--------IPsLLEFARLESKADARVSD----LSGGMKRRLTLARAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 519 LKDAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARM-DRLVVLDKGH-IAESGTHAELLAHGG 593
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVLEAGRkIAEGRPHALIDEHIG 265
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
361-574 |
3.83e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 127.07 E-value: 3.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 361 EVEFEHIAFHYG--KGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILV-DGQDIAGVTQESLRAQ 437
Cdd:PTZ00265 382 KIQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 438 IGMVTQDTSLLHRSIRDNLLYGRPGASDAELME----------------------------------------------- 470
Cdd:PTZ00265 462 IGVVSQDPLLFSNSIKNNIKYSLYSLKDLEALSnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrkny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 471 ----------AVRKARADEFIPLLSDAegrrgFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVES 540
Cdd:PTZ00265 542 qtikdsevvdVSKKVLIHDFVSALPDK-----YETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260 270
....*....|....*....|....*....|....*.
gi 15598424 541 AIQESLETLM--QGKTVIAIAHRLSTIARMDRLVVL 574
Cdd:PTZ00265 617 LVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
362-591 |
4.04e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 120.30 E-value: 4.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESlRAQIGMV 441
Cdd:PRK13537 8 IDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSL-LHRSIRDNLL-YGRP-GASDAELMEAVRkaradefiPLLSDAEGRRGFDAHVGErgvkLSGGQRQRIAIARVL 518
Cdd:PRK13537 86 PQFDNLdPDFTVRENLLvFGRYfGLSAAAARALVP--------PLLEFAKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598424 519 LKDAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARM-DRLVVLDKGH-IAESGTHaELLAH 591
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERLcDRLCVIEEGRkIAEGAPH-ALIES 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
362-580 |
6.83e-30 |
|
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: 115.22 E-value: 6.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVT-QESLRAQIGM 440
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQdtsllhrsirdnllygrpgasdaelmeavrkaradefipllsdaegrrgfdahvgergvkLSGGQRQRIAIARVLLK 520
Cdd:cd03216 80 VYQ------------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 521 DAPILILDEATSAL-DSEVESAIqESLETLM-QGKTVIAIAHRLSTIARM-DRLVVLDKGHIA 580
Cdd:cd03216 100 NARLLILDEPTAALtPAEVERLF-KVIRRLRaQGVAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
377-591 |
1.31e-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: 117.15 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVtQESLRAQIGMV-T-QDTSLLHR-SIR 453
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL-PPHEIARLGIGrTfQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 454 DNLLYGRPGASDAELMEAVRKARADEFIPLLSDAEGRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSA 533
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 534 LDSEVESAIQESLETL-MQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:cd03219 174 LNPEETEELAELIRELrERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
362-584 |
1.32e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 120.44 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEslRAQIGMV 441
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLL-HRSIRDNLLYG-----RPGASDAE-LMEAVRKARADEFipllsdaegrrgfdahvGERGVK-LSGGQRQRIA 513
Cdd:PRK09452 92 FQSYALFpHMTVFENVAFGlrmqkTPAAEITPrVMEALRMVQLEEF-----------------AQRKPHqLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 514 IARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAH-RLSTIARMDRLVVLDKGHIAESGT 584
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
361-591 |
2.00e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 119.48 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 361 EVEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDiAGVTQESLRAQIGM 440
Cdd:COG1118 2 SIEVRNISKRFG-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD-LFTNLPPRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTSLL-HRSIRDNLLYGrpgASDAELMEAVRKARADEFIPL--LSDAEGRRgfdahVGErgvkLSGGQRQRIAIARV 517
Cdd:COG1118 80 VFQHYALFpHMTVAENIAFG---LRVRPPSKAEIRARVEELLELvqLEGLADRY-----PSQ----LSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 518 LLKDAPILILDEATSALDSEVESAIQESLETL---MQGKTVIaIAH------RLStiarmDRLVVLDKGHIAESGTHAEL 588
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhdeLGGTTVF-VTHdqeealELA-----DRVVVMNQGRIEQVGTPDEV 221
|
...
gi 15598424 589 LAH 591
Cdd:COG1118 222 YDR 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
365-589 |
3.43e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 116.27 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 365 EHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQd 444
Cdd:PRK11231 6 ENLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 445 tslLHR-----SIRD---------NLLYGRPGASDAELME-AVRKARADEFipllsdAEgRRGFDahvgergvkLSGGQR 509
Cdd:PRK11231 84 ---HHLtpegiTVRElvaygrspwLSLWGRLSAEDNARVNqAMEQTRINHL------AD-RRLTD---------LSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 510 QRIAIARVLLKDAPILILDEATSALD--SEVEsaiqesLETLM-----QGKTVIAIAHRLSTIARM-DRLVVLDKGHIAE 581
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDinHQVE------LMRLMrelntQGKTVVTVLHDLNQASRYcDHLVVLANGHVMA 218
|
....*...
gi 15598424 582 SGTHAELL 589
Cdd:PRK11231 219 QGTPEEVM 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
363-591 |
4.46e-29 |
|
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: 115.46 E-value: 4.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYGKgSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGV-TQESLRAQIGMV 441
Cdd:COG0410 5 EVENLHAGYGG-IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLpPHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQD----TSLlhrSIRDNLLYGRPGASDAELMEAvRKARADEFIPLLsdAEgRRgfdahvGERGVKLSGGQRQRIAIARV 517
Cdd:COG0410 84 PEGrrifPSL---TVEENLLLGAYARRDRAEVRA-DLERVYELFPRL--KE-RR------RQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 518 LLKDAPILILDEATSALD----SEVESAIQESLEtlmQGKTVIAI---AHRLSTIArmDRLVVLDKGHIAESGTHAELLA 590
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAplivEEIFEIIRRLNR---EGVTILLVeqnARFALEIA--DRAYVLERGRIVLEGTAAELLA 225
|
.
gi 15598424 591 H 591
Cdd:COG0410 226 D 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
380-591 |
5.25e-29 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 115.13 E-value: 5.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 380 GLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEslRAQIGMVTQDTSLL-HRSIRDNLLY 458
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 459 GrpgASDAELMEAVRKARADEFIPLLsdaegrrGFDaHVGERGVK-LSGGQRQRIAIARVLLKDAPILILDEATSALDSE 537
Cdd:cd03299 95 G---LKKRKVDKKEIERKVLEIAEML-------GID-HLLNRKPEtLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 538 VESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:cd03299 164 TKEKLREELKKIRKefGVTVLHVTHDFEEAWALaDKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
362-577 |
1.11e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 120.13 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkgsGVI--QGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQ--DIAGvTQESLRAQ 437
Cdd:COG3845 6 LELRGITKRFG---GVVanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRS-PRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 438 IGMVTQDTSLLHR-SIRDNLLYGRPGASDAEL-MEAVRKaRADEfiplLSDaegRRGF----DAHVGErgvkLSGGQRQR 511
Cdd:COG3845 82 IGMVHQHFMLVPNlTVAENIVLGLEPTKGGRLdRKAARA-RIRE----LSE---RYGLdvdpDAKVED----LSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598424 512 IAIARVLLKDAPILILDEATSAL-DSEVEsaiqESLETLM----QGKTVIAIAHRLSTIARM-DRLVVLDKG 577
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLtPQEAD----ELFEILRrlaaEGKSIIFITHKLREVMAIaDRVTVLRRG 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
373-591 |
1.41e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 114.46 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 373 KGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAG---VTQE-----SLRAQIGMVTQD 444
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarsLSQQkglirQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 445 TSLL-HRSIRDNLLYGRPGASDAELMEAVRKARAdefipLLsdaegrrgfdAHVGERGV------KLSGGQRQRIAIARV 517
Cdd:PRK11264 94 FNLFpHRTVLENIIEGPVIVKGEPKEEATARARE-----LL----------AKVGLAGKetsyprRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 518 LLKDAPILILDEATSALDSEVESAIQESLETLMQGK-TVIAIAHRLStIAR--MDRLVVLDKGHIAESGTHAELLAH 591
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMS-FARdvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
387-583 |
1.63e-28 |
|
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: 113.16 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 387 PGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQdIAGVTQESL-----RAQIGMVTQDTSLL-HRSIRDNLLYGR 460
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKInlppqQRKIGLVFQQYALFpHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 461 PGASDAElmeavRKARADEFIPLLsdaegrrGFDaHVGERGV-KLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVE 539
Cdd:cd03297 101 KRKRNRE-----DRISVDELLDLL-------GLD-HLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598424 540 SAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:cd03297 168 LQLLPELKQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
362-589 |
2.01e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 114.70 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSG-VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGM 440
Cdd:PRK13632 8 IKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQ--DTSLLHRSIRDNLLYGrpgasdaelMEAvRKARADEFIPLLSDAEGRRGFDAHVGERGVKLSGGQRQRIAIARVL 518
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFG---------LEN-KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 519 LKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELL 589
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
362-588 |
2.02e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 116.74 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKgSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDiagVTQESLRAQ-IGM 440
Cdd:PRK11432 7 VVLKNITKRFGS-NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED---VTHRSIQQRdICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTSLL-HRSIRDNLLYGRP--GASDAELMEAVRKARAdefiplLSDAEGrrgfdahVGERGV-KLSGGQRQRIAIAR 516
Cdd:PRK11432 83 VFQSYALFpHMSLGENVGYGLKmlGVPKEERKQRVKEALE------LVDLAG-------FEDRYVdQISGGQQQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598424 517 VLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLS-TIARMDRLVVLDKGHIAESGTHAEL 588
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
381-594 |
2.49e-28 |
|
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: 116.36 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 381 LDLKVR-PGEKI-GLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDI----AGVTQESLRAQIGMVTQDTSLL-HRSIR 453
Cdd:TIGR02142 14 LDADFTlPGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFpHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 454 DNLLYGRPGASDAElmeavRKARADEFIPLLsdaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSA 533
Cdd:TIGR02142 94 GNLRYGMKRARPSE-----RRISFERVIELL-------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 534 LDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAHGGL 594
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
355-596 |
3.26e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 117.25 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 355 LRVERGEVEfehiafhygkgsgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESL 434
Cdd:PRK09536 9 LSVEFGDTT-------------VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 435 RAQIGMVTQDTSL-LHRSIRDNLLYGR-PGASDAELMEAVRKARADEfipllsdAEGRRGFDAHVGERGVKLSGGQRQRI 512
Cdd:PRK09536 76 SRRVASVPQDTSLsFEFDVRQVVEMGRtPHRSRFDTWTETDRAAVER-------AMERTGVAQFADRPVTSLSGGERQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 513 AIARVLLKDAPILILDEATSALDseVESAIQ--ESLETLMQ-GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAEL 588
Cdd:PRK09536 149 LLARALAQATPVLLLDEPTASLD--INHQVRtlELVRRLVDdGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPADV 226
|
....*...
gi 15598424 589 LAHGGLYA 596
Cdd:PRK09536 227 LTADTLRA 234
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
362-579 |
3.77e-28 |
|
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: 112.12 E-value: 3.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQES---LRAQI 438
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLL-HRSIRDNLLYGrpgasdaelMEAVRKARADefIP-LLSDAEGRRGFDAHVGERGVKLSGGQRQRIAIAR 516
Cdd:cd03292 81 GVVFQDFRLLpDRNVYENVAFA---------LEVTGVPPRE--IRkRVPAALELVGLSHKHRALPAELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598424 517 VLLKDAPILILDEATSALDSEVESAIQESLETLMQ-GKTVIAIAHRLSTIARMD-RLVVLDKGHI 579
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
380-604 |
3.79e-28 |
|
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: 115.97 E-value: 3.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 380 GLDLKVR---PGEKI-GLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQdiagVTQESLRAQ--------IGMVTQDTSL 447
Cdd:COG4148 13 GFTLDVDftlPGRGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE----VLQDSARGIflpphrrrIGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 448 L-HRSIRDNLLYGRPGASDAElmeavRKARADEFIPLLsdaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILI 526
Cdd:COG4148 89 FpHLSVRGNLLYGRKRAPRAE-----RRISFDEVVELL-------GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 527 LDEATSALDSEVESAIQESLETLmQGKT---VIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAHGGLYARLWQHQ 602
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERL-RDELdipILYVSHSLDEVARLaDHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEE 235
|
..
gi 15598424 603 TG 604
Cdd:COG4148 236 AG 237
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
371-583 |
6.25e-28 |
|
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: 111.54 E-value: 6.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 371 YGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIagVTQESLRAQIGMVTQDTSL-LH 449
Cdd:cd03268 10 YGKKR-VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALIEAPGFyPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 450 RSIRDNLLYGRpgasdaeLMEAVRKARADEFIPLLsdaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDE 529
Cdd:cd03268 87 LTARENLRLLA-------RLLGIRKKRIDEVLDVV-------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 530 ATSALDSEvesAIQESLETLM----QGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:cd03268 153 PTNGLDPD---GIKELRELILslrdQGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
382-590 |
7.55e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 111.98 E-value: 7.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 382 DLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAgVTQESLRAqIGMVTQDTSLL-HRSIRDNLLYG- 459
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT-TTPPSRRP-VSMLFQENNLFsHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 460 RPGAsdaELMEAVRKaradefipLLSDAEGRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVE 539
Cdd:PRK10771 97 NPGL---KLNAAQRE--------KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 540 saiQESLETLMQ-----GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLA 590
Cdd:PRK10771 166 ---QEMLTLVSQvcqerQLTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
362-583 |
1.41e-27 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 110.42 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVtqESLRAQIGMV 441
Cdd:cd03301 1 VELENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLL-HRSIRDNLLYGRpgasdaelmeAVRKARADEFIPLLSDAEGRRGFDAHVGERGVKLSGGQRQRIAIARVLLK 520
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGL----------KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAH---RLSTIArmDRLVVLDKGHIAESG 583
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdqvEAMTMA--DRIAVMNDGQIQQIG 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
361-586 |
1.48e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 111.26 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 361 EVEFEHIAFHYGKgSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDG------QDIAGVTQESL 434
Cdd:COG4161 2 SIQLKNINCFYGS-HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 435 RAQIGMVTQDTSLL-HRSIRDNLLYGrP----GASDAELMEavrkaRADEFIPLLSDAEGRRGFDAHvgergvkLSGGQR 509
Cdd:COG4161 81 RQKVGMVFQQYNLWpHLTVMENLIEA-PckvlGLSKEQARE-----KAMKLLARLRLTDKADRFPLH-------LSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 510 QRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ-GKTVIAIAHRLStIAR--MDRLVVLDKGHIAESGTHA 586
Cdd:COG4161 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVE-FARkvASQVVYMEKGRIIEQGDAS 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
362-593 |
1.65e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 112.13 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSG--VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIG 439
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQ--DTSLLHRSIRDNLLYG--RPGASDAELMEavrkaRADEFIPLLsdaegrrGFDAHVGERGVKLSGGQRQRIAIA 515
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGleNKGIPHEEMKE-----RVNEALELV-------GMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 516 RVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGG 593
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
362-583 |
1.98e-27 |
|
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: 109.98 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSgVIQGLDLKVRPGeKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEsLRAQIGMV 441
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLLHR-SIRDNLLYGrpgASDAELMEAVRKARADEFIPL--LSDAEGRRgfdahVGergvKLSGGQRQRIAIARVL 518
Cdd:cd03264 78 PQEFGVYPNfTVREFLDYI---AWLKGIPSKEVKARVDEVLELvnLGDRAKKK-----IG----SLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598424 519 LKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
362-589 |
2.25e-27 |
|
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: 111.44 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGS--------GVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQES 433
Cdd:TIGR02769 3 LEVRDVTHTYRTGGlfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 434 LRA---QIGMVTQDTSLL---HRSIRDNLlyGRPGASDAELMEAVRKARADEfiplLSDAEGRRgfDAHVGERGVKLSGG 507
Cdd:TIGR02769 83 RRAfrrDVQLVFQDSPSAvnpRMTVRQII--GEPLRHLTSLDESEQKARIAE----LLDMVGLR--SEDADKLPRQLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 508 QRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGT 584
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSFcQRVAVMDKGQIVEECD 234
|
....*
gi 15598424 585 HAELL 589
Cdd:TIGR02769 235 VAQLL 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
361-583 |
2.29e-27 |
|
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: 109.18 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 361 EVEFEHIAFHYGKGSG-----VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLL--LRLYDLESGRILVDGQDIagvTQES 433
Cdd:cd03213 3 TLSFRNLTVTVKSSPSksgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 434 LRAQIGMVTQDTSLL-HRSIRDNLLYGrpgasdAELmeavrkaradefipllsdaegrrgfdahvgeRGvkLSGGQRQRI 512
Cdd:cd03213 80 FRKIIGYVPQDDILHpTLTVRETLMFA------AKL-------------------------------RG--LSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 513 AIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ-GKTVIAIAHRLST--IARMDRLVVLDKGHIAESG 583
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
362-588 |
2.75e-27 |
|
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: 109.77 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGViQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEsLRAQIGMV 441
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLLHR-SIRDNL-----LYGRPGasdaelmeAVRKARADEFIPLLSDAEGRrgfDAHVGergvKLSGGQRQRIAIA 515
Cdd:cd03265 79 FQDLSVDDElTGWENLyiharLYGVPG--------AERRERIDELLDFVGLLEAA---DRLVK----TYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598424 516 RVLLKDAPILILDEATSALDSEVESAIQESLETLM--QGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAEL 588
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
361-591 |
3.73e-27 |
|
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: 110.12 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 361 EVEFEHIAFHYGKGSGViQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEslRAQIGM 440
Cdd:cd03296 2 SIEVRNVSKRFGDFVAL-DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTSLL-HRSIRDNLLYG---RPGASDAElmEAVRKARADEFIPL--LSDAEGRrgFDAhvgergvKLSGGQRQRIAI 514
Cdd:cd03296 79 VFQHYALFrHMTVFDNVAFGlrvKPRSERPP--EAEIRAKVHELLKLvqLDWLADR--YPA-------QLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 515 ARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
377-591 |
7.76e-27 |
|
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: 109.74 E-value: 7.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQeSLRAQIGMV-T-QDTSLLHR-SIR 453
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIArTfQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 454 DNLL---YGRPGASDAELMEAVRKARADEfIPLLSDAE---GRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILIL 527
Cdd:COG0411 98 ENVLvaaHARLGRGLLAALLRLPRARREE-REARERAEellERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 528 DEATSAL-DSEVEsAIQESLETL--MQGKTVIAIAHRLSTIARM-DRLVVLDKGH-IAEsGTHAELLAH 591
Cdd:COG0411 177 DEPAAGLnPEETE-ELAELIRRLrdERGITILLIEHDMDLVMGLaDRIVVLDFGRvIAE-GTPAEVRAD 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
366-591 |
8.40e-27 |
|
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: 8.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 366 HIAFHYGKGSG-VIQGLDLKVRPGEKIGLVGPSGAGKS----TLVNLLLRLYDLESGRILVDGQDIAGVTQESLRA---- 436
Cdd:COG4172 13 SVAFGQGGGTVeAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 437 QIGMVTQD--TSL--LH---RSIRDNL-LYGRPGASDA-----ELMEAVRkaradefIPllsDAEGRRGFDAHvgergvK 503
Cdd:COG4172 93 RIAMIFQEpmTSLnpLHtigKQIAEVLrLHRGLSGAAAraralELLERVG-------IP---DPERRLDAYPH------Q 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 504 LSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIA 580
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRelGMALLLITHDLGVVRRFaDRVAVMRQGEIV 236
|
250
....*....|.
gi 15598424 581 ESGTHAELLAH 591
Cdd:COG4172 237 EQGPTAELFAA 247
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-589 |
1.58e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 108.85 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 351 DAQPLRVERGEVEfehiafhygkgsgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLE-----SGRILVDGQD 425
Cdd:PRK14247 5 EIRDLKVSFGQVE-------------VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 426 IAGVTQESLRAQIGMVTQ-DTSLLHRSIRDNLLYG----RPGASDAELMEAVRKARadEFIPLLSDAEGRrgFDAHVGer 500
Cdd:PRK14247 72 IFKMDVIELRRRVQMVFQiPNPIPNLSIFENVALGlklnRLVKSKKELQERVRWAL--EKAQLWDEVKDR--LDAPAG-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 501 gvKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHI 579
Cdd:PRK14247 146 --KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARIsDYVAFLYKGQI 223
|
250
....*....|
gi 15598424 580 AESGTHAELL 589
Cdd:PRK14247 224 VEWGPTREVF 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
362-590 |
2.98e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 108.54 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQ-ESLRAQIGM 440
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQ--DTSLLHRSIRDNLLYGRPGASdaelmeavrkaradefiplLSDAEGRRGFDAHVGERGVK---------LSGGQR 509
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLC-------------------LPPIEIRKRVDRALAEIGLEkyrhrspktLSGGQG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 510 QRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ-GKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAEL 588
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
|
..
gi 15598424 589 LA 590
Cdd:PRK13644 223 LS 224
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
362-588 |
3.40e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.73 E-value: 3.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGS-GVIQGLDLKVRPGEKIGLVGPSGAGKST---LVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQ 437
Cdd:PRK13640 6 VEFKHVSFTYPDSKkPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 438 IGMVTQ--DTSLLHRSIRDNLLYG--RPGASDAELMEAVRKARADEFIPLLSDAEGRrgfdahvgergvKLSGGQRQRIA 513
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGleNRAVPRPEMIKIVRDVLADVGMLDYIDSEPA------------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 514 IARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGK--TVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAEL 588
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
393-591 |
3.67e-26 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 109.51 E-value: 3.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 393 LVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEslRAQIGMVTQDTSLL-HRSIRDNLLYG--RPGASDAElm 469
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFpHMTVEENVAFGlkMRKVPRAE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 470 eavRKARADEFIPLLsdaegrrgfdaHVGERG----VKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQES 545
Cdd:TIGR01187 77 ---IKPRVLEALRLV-----------QLEEFAdrkpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598424 546 LETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:TIGR01187 143 LKTIQEqlGITFVFVTHDQEEAMTMsDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
362-589 |
3.87e-26 |
|
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: 107.48 E-value: 3.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLR-LYDLESGRILVDGQDIAGVTQESLRAQIGM 440
Cdd:COG1119 4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDtslLHRSIRDNL---------------LYGRPGASDaelmeavrKARADEFIPLLsdaegrrGFDAHVGERGVKLS 505
Cdd:COG1119 83 VSPA---LQLRFPRDEtvldvvlsgffdsigLYREPTDEQ--------RERARELLELL-------GLAHLADRPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 506 GGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTI-ARMDRLVVLDKGHIAES 582
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIpPGITHVLLLKDGRVVAA 224
|
....*..
gi 15598424 583 GTHAELL 589
Cdd:COG1119 225 GPKEEVL 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
362-585 |
5.72e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 106.64 E-value: 5.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKgSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQ--DIAGVTQE----SLR 435
Cdd:PRK11124 3 IQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkairELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 436 AQIGMVTQDTSLL-HRSIRDNLLYGrP----GASDAElmeavRKARADEFIPLLSDAEGRRGFDAHvgergvkLSGGQRQ 510
Cdd:PRK11124 82 RNVGMVFQQYNLWpHLTVQQNLIEA-PcrvlGLSKDQ-----ALARAEKLLERLRLKPYADRFPLH-------LSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 511 RIAIARVLLKDAPILILDEATSALDSE----VESAIQESLETlmqGKTVIAIAHRLStIAR--MDRLVVLDKGHIAESGT 584
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEitaqIVSIIRELAET---GITQVIVTHEVE-VARktASRVVYMENGHIVEQGD 224
|
.
gi 15598424 585 H 585
Cdd:PRK11124 225 A 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
362-575 |
5.89e-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: 105.64 E-value: 5.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTqESLRAQIGMV 441
Cdd:COG4133 3 LEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSL-LHRSIRDNL-----LYGRPGASDA--ELMEAVRkaradefiplLSDAEGRRgfdahVGergvKLSGGQRQRIA 513
Cdd:COG4133 81 GHADGLkPELTVRENLrfwaaLYGLRADREAidEALEAVG----------LAGLADLP-----VR----QLSAGQKRRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598424 514 IARVLLKDAPILILDEATSALDSE----VESAIQESLEtlmQGKTVIAIAHRLSTIARMDRLVVLD 575
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAgvalLAELIAAHLA---RGGAVLLTTHQPLELAAARVLDLGD 204
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
367-583 |
7.84e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.78 E-value: 7.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 367 IAFHYGKGSGvIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLE-----SGRILVDGQDIAGVTQES--LRAQIG 439
Cdd:PRK14239 11 LSVYYNKKKA-LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTvdLRKEIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQDTSLLHRSIRDNLLYGR--PGASDAELM-EAVRKARADEFIpllSDAEGRRGFDAHVGergvkLSGGQRQRIAIAR 516
Cdd:PRK14239 90 MVFQQPNPFPMSIYENVVYGLrlKGIKDKQVLdEAVEKSLKGASI---WDEVKDRLHDSALG-----LSGGQQQRVCIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 517 VLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYN 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
331-577 |
7.85e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 111.82 E-value: 7.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 331 GQVQDGM-------QTIALPRKVVDR--------EDAQPL--------RVERGEVEFEHIAFHYGKGSGVIQGLDLKVRP 387
Cdd:COG4178 309 GQVQGALswfvdnyQSLAEWRATVDRlagfeealEAADALpeaasrieTSEDGALALEDLTLRTPDGRPLLEDLSLSLKP 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 388 GEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILV-DGQDIAgvtqeslraqigMVTQDTSLLHRSIRDNLLYGRPGA--S 464
Cdd:COG4178 389 GERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL------------FLPQRPYLPLGTLREALLYPATAEafS 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 465 DAELMEAVRKARADEFIPLLsDAEGRRGfdaHVgergvkLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQE 544
Cdd:COG4178 457 DAELREALEAVGLGHLAERL-DEEADWD---QV------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
250 260 270
....*....|....*....|....*....|...
gi 15598424 545 SLETLMQGKTVIAIAHRLSTIARMDRLVVLDKG 577
Cdd:COG4178 527 LLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
362-587 |
8.65e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.44 E-value: 8.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGS----GVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIA--GVTQESLR 435
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 436 AQIGMVTQ--DTSLLHRSIRDNLLYG--RPGASDAELMEAVRKARadEFIPL-LSDAEGRRGFDahvgergvkLSGGQRQ 510
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAM--NIVGLdYEDYKDKSPFE---------LSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 511 RIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGK--TVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAE 587
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPRE 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
363-581 |
1.27e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.48 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYGKGSG---VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTqeslrAQIG 439
Cdd:COG4525 5 TVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----ADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQDTSLLH-RSIRDNLLYGR--PGASDAElmeavRKARADEFIPL--LSDAEGRRGFdahvgergvKLSGGQRQRIAI 514
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVAFGLrlRGVPKAE-----RRARAEELLALvgLADFARRRIW---------QLSGGMRQRVGI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 515 ARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHR------LSTiarmdRLVVLDK--GHIAE 581
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITHSveealfLAT-----RLVVMSPgpGRIVE 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
362-587 |
1.57e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 104.96 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQES---LRAQI 438
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLL-HRSIRDNLLYGR--PGASDAELMEavRKARADEFIPLLSDAegrRGFDahvgergVKLSGGQRQRIAIA 515
Cdd:PRK10908 82 GMIFQDHHLLmDRTVYDNVAIPLiiAGASGDDIRR--RVSAALDKVGLLDKA---KNFP-------IQLSGGEQQRVGIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 516 RVLLKDAPILILDEATSALDSEVESAIQESLETLMQ-GKTVIAIAHRLSTIARMD-RLVVLDKGHIAEsGTHAE 587
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSyRMLTLSDGHLHG-GVGGE 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
362-581 |
1.92e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.15 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRIlvdgqdIAGVTqeslrAQIGMV 441
Cdd:COG0488 316 LELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV------KLGET-----VKIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLLH--RSIRDNLLYGRPGASDAElmeavrkARAdefipLLsdaeGRRGF---DAH--VGergvKLSGGQRQRIAI 514
Cdd:COG0488 384 DQHQEELDpdKTVLDELRDGAPGGTEQE-------VRG-----YL----GRFLFsgdDAFkpVG----VLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 515 ARVLLKDAPILILDEATSALDseVESaiQESLETLMQ---GkTVIAIAH-R--LSTIArmDRLVVLDKGHIAE 581
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLD--IET--LEALEEALDdfpG-TVLLVSHdRyfLDRVA--TRILEFEDGGVRE 509
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
382-583 |
3.43e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 103.79 E-value: 3.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 382 DLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTqeSLRAQIGMVTQDTSLL-HRSIRDNLLYG- 459
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA--PYQRPVSMLFQENNLFaHLTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 460 RPGASdaelMEAVRKARadefiplLSDAEGRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVE 539
Cdd:TIGR01277 96 HPGLK----LNAEQQEK-------VVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598424 540 SAIQESLETLMQGK--TVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:TIGR01277 165 EEMLALVKQLCSERqrTLLMVTHHLSDARAIaSQIAVVSQGKIKVVS 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
350-591 |
7.98e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.64 E-value: 7.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 350 EDAQP-LRVERGEVEFE--------HIAFHYgkgsgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLEsGRIL 420
Cdd:PRK15134 270 EPASPlLDVEQLQVAFPirkgilkrTVDHNV-----VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 421 VDGQDIAGVTQESL---RAQIGMVTQD--TSLLHR-----SIRDNLLYGRPGASDAELMEAVRKARADEFIpllsDAEGR 490
Cdd:PRK15134 344 FDGQPLHNLNRRQLlpvRHRIQVVFQDpnSSLNPRlnvlqIIEEGLRVHQPTLSAAQREQQVIAVMEEVGL----DPETR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 491 RGFDAhvgergvKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTV--IAIAHRLSTIARM 568
Cdd:PRK15134 420 HRYPA-------EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAL 492
|
250 260
....*....|....*....|....
gi 15598424 569 -DRLVVLDKGHIAESGTHAELLAH 591
Cdd:PRK15134 493 cHQVIVLRQGEVVEQGDCERVFAA 516
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
365-589 |
8.56e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 103.70 E-value: 8.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 365 EHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLL---LRLYdleSGRILVDGQDIAGVTQESLRAQIGMV 441
Cdd:PRK13548 6 RNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsgeLSPD---SGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLLHR-SIRDNLLYGR-PGA-SDAELMEAVRKARAdefiplLSDAEGRRGFDAHvgergvKLSGGQRQRIAIARVL 518
Cdd:PRK13548 82 PQHSSLSFPfTVEEVVAMGRaPHGlSRAEDDALVAAALA------QVDLAHLAGRDYP------QLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 519 L------KDAPILILDEATSALDsevesaIQESLETLM--------QGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALD------LAHQHHVLRlarqlaheRGLAVIVVLHDLNLAARYaDRIVLLHQGRLVADG 223
|
....*.
gi 15598424 584 THAELL 589
Cdd:PRK13548 224 TPAEVL 229
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
363-588 |
1.15e-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: 102.60 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGV-TQESLRAQIGMV 441
Cdd:TIGR03410 2 EVSNLNVYYG-QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLpPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLLHR-SIRDNLLYGRPGASDAElmeAVRKARADEFIPLLSDAEGRRGFDahvgergvkLSGGQRQRIAIARVLLK 520
Cdd:TIGR03410 81 PQGREIFPRlTVEENLLTGLAALPRRS---RKIPDEIYELFPVLKEMLGRRGGD---------LSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETL--MQGKTVIAIAHRLS-TIARMDRLVVLDKGHIAESGTHAEL 588
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
365-590 |
2.76e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 102.84 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 365 EHIAFHYGKGS--------GVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRA 436
Cdd:PRK10419 7 SGLSHHYAHGGlsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 437 ---QIGMVTQDT-SLLH--RSIRDNLlyGRPGASDAELMEAVRKARADEfiplLSDAEGRRgfDAHVGERGVKLSGGQRQ 510
Cdd:PRK10419 87 frrDIQMVFQDSiSAVNprKTVREII--REPLRHLLSLDKAERLARASE----MLRAVDLD--DSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 511 RIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAE 587
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFcQRVMVMDNGQIVETQPVGD 238
|
...
gi 15598424 588 LLA 590
Cdd:PRK10419 239 KLT 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
381-601 |
5.34e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 107.75 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 381 LDLKVRPGEKIGLVGPSGAGKSTLVNLLL-RLYDLESGRILVdgqdiagvtqeslRAQIGMVTQDTSLLHRSIRDNLLYG 459
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLgELSHAETSSVVI-------------RGSVAYVPQVSWIFNATVRENILFG 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 460 rpgaSDaelMEAVRKARADEFIPLLSDAEGRRGFD-AHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEV 538
Cdd:PLN03232 703 ----SD---FESERYWRAIDVTALQHDLDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 539 ESAIQES-LETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARLWQH 601
Cdd:PLN03232 776 AHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMEN 839
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
362-581 |
1.28e-23 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 99.82 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSG---VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQES---LR 435
Cdd:COG4181 9 IELRGLTKTVGTGAGeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDArarLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 436 AQ-IGMVTQDTSLL-HRSIRDN-----LLYGRPGASD--AELMEAVrkaradefipllsdaegrrGFDAHVGERGVKLSG 506
Cdd:COG4181 89 ARhVGFVFQSFQLLpTLTALENvmlplELAGRRDARAraRALLERV-------------------GLGHRLDHYPAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 507 GQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLM--QGKTVIAIAHRLSTIARMDRLVVLDKGHIAE 581
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNreRGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
378-591 |
1.45e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 102.09 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 378 IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRA---QIGMVTQD--TSLLHRS- 451
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsDIQMIFQDplASLNPRMt 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 452 ----IRDNLLYGRPGASDAELMEAVRKARADefIPLLSDAEGRRgfdAHvgergvKLSGGQRQRIAIARVLLKDAPILIL 527
Cdd:PRK15079 117 igeiIAEPLRTYHPKLSRQEVKDRVKAMMLK--VGLLPNLINRY---PH------EFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 528 DEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:PRK15079 186 DEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHIsDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
364-595 |
2.35e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.99 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 364 FEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGqdiagvtqeslRAQIGMVTQ 443
Cdd:COG0488 1 LENLSKSFGGRP-LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 444 DTSLL-HRSIRDNLLygrpgASDAELMEAVRKARADEFIPLLSDAEGRR---------------------------GFDA 495
Cdd:COG0488 69 EPPLDdDLTVLDTVL-----DGDAELRALEAELEELEAKLAEPDEDLERlaelqeefealggweaearaeeilsglGFPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 496 HVGERGVK-LSGGQRQRIAIARVLLKDAPILILDEATSALDSEvesAIqESLETLMQG--KTVIAIAHrlstiarmDRlV 572
Cdd:COG0488 144 EDLDRPVSeLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE---SI-EWLEEFLKNypGTVLVVSH--------DR-Y 210
|
250 260
....*....|....*....|....*
gi 15598424 573 VLDK--GHIAEsgthaelLAHGGLY 595
Cdd:COG0488 211 FLDRvaTRILE-------LDRGKLT 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
378-589 |
2.39e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.80 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 378 IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESL----RAQIGMVTQDTSLL-HRSI 452
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 453 RDNLLYGrpgasdAELMEAVRKARADEFIpllsDAEGRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATS 532
Cdd:PRK10070 124 LDNTAFG------MELAGINAEERREKAL----DALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 533 ALDSEVESAIQESLETLM--QGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELL 589
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQakHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
377-579 |
2.64e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.78 E-value: 2.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESlRAQ-IGMVTQD------TSLlh 449
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAKyIGRVFQDpmmgtaPSM-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 450 rSIRDNLL--YGRpGASdAELMEAVRKARADEFIPLLSDA----EGRrgFDAHVGergvKLSGGQRQRIAIARVLLKDAP 523
Cdd:COG1101 98 -TIEENLAlaYRR-GKR-RGLRRGLTKKRRELFRELLATLglglENR--LDTKVG----LLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598424 524 ILILDEATSALD---SEV-----ESAIQE-SLETLMqgktviaIAHRLSTIARM-DRLVVLDKGHI 579
Cdd:COG1101 169 LLLLDEHTAALDpktAALvleltEKIVEEnNLTTLM-------VTHNMEQALDYgNRLIMMHEGRI 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
381-598 |
2.98e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 105.21 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 381 LDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVdgqdiagvtqesLRAQIGMVTQDTSLLHRSIRDNLLYGR 460
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGS 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 461 PgasdaelMEAVRKARADEFIPLLSDAEGRRGFD-AHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEV- 538
Cdd:PLN03130 704 P-------FDPERYERAIDVTALQHDLDLLPGGDlTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVg 776
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 539 ----ESAIQESLetlmQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHGGLYARL 598
Cdd:PLN03130 777 rqvfDKCIKDEL----RGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
362-592 |
2.98e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.83 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHY-GKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGM 440
Cdd:PRK13648 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTsllhrsirDNLLYGRPGASDAEL-ME--AVRKARADEFIP-LLSDAE--GRRGFDAHvgergvKLSGGQRQRIAI 514
Cdd:PRK13648 88 VFQNP--------DNQFVGSIVKYDVAFgLEnhAVPYDEMHRRVSeALKQVDmlERADYEPN------ALSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 515 ARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGK--TVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLAHG 592
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
362-577 |
3.33e-23 |
|
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: 97.74 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIagvtQESLRAQIGMV 441
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSL-LHRSIRDNLLYgrpGASDAELMEAVRKARADEFIPllsdaegRRGFDAHVGERGVKLSGGQRQRIAIARVLLK 520
Cdd:cd03269 76 PEERGLyPKMKVIDQLVY---LAQLKGLKKEEARRRIDEWLE-------RLELSEYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 521 DAPILILDEATSALDS-EVESAIQESLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKG 577
Cdd:cd03269 146 DPELLILDEPFSGLDPvNVELLKDVIRELARAGKTVILSTHQMELVEELcDRVLLLNKG 204
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
365-589 |
3.35e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 99.03 E-value: 3.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 365 EHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQD 444
Cdd:COG4559 5 ENLSVRLG-GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 445 TSL-----------LHRSIrdnllYGRPGASDAELMEAVRkARADefiplLSDAEGRrgfdaHVGErgvkLSGGQRQRIA 513
Cdd:COG4559 84 SSLafpftveevvaLGRAP-----HGSSAAQDRQIVREAL-ALVG-----LAHLAGR-----SYQT----LSGGEQQRVQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 514 IARVLL-----KDAP--ILILDEATSALDsevesaIQESLETL-------MQGKTVIAIAHRLSTIARM-DRLVVLDKGH 578
Cdd:COG4559 144 LARVLAqlwepVDGGprWLFLDEPTSALD------LAHQHAVLrlarqlaRRGGGVVAVLHDLNLAAQYaDRILLLHQGR 217
|
250
....*....|.
gi 15598424 579 IAESGTHAELL 589
Cdd:COG4559 218 LVAQGTPEEVL 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
377-583 |
3.54e-23 |
|
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: 98.11 E-value: 3.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLL---LRLYDLESGRILVDGQDI-AGVTQESlraqIGMVTQDTSLL-HRS 451
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRkPDQFQKC----VAYVRQDDILLpGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 452 IRDNLLYGRPGASDAELMEAVRKARADEFipLLSDAEgrrgfDAHVGERGVK-LSGGQRQRIAIARVLLKDAPILILDEA 530
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDAIRKKRVEDV--LLRDLA-----LTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598424 531 TSALDSEVESAIQESLETLMQ-GKTVIAIAHR-LSTIARM-DRLVVLDKGHIAESG 583
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARrNRIVILTIHQpRSDLFRLfDRILLLSSGEIVYSG 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
363-574 |
6.16e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.48 E-value: 6.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVT 442
Cdd:PRK10247 9 QLQNVGYLAG-DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 443 QDTSLLHRSIRDNLLYgrPgasdaelmEAVRKARADEFIpLLSDAEgRRGFDAHVGERGV-KLSGGQRQRIAIARVLLKD 521
Cdd:PRK10247 88 QTPTLFGDTVYDNLIF--P--------WQIRNQQPDPAI-FLDDLE-RFALPDTILTKNIaELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598424 522 APILILDEATSALDSEVESAIQESLETLM--QGKTVIAIAHRLSTIARMDRLVVL 574
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITL 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
363-560 |
1.39e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.46 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESlraqiGMVT 442
Cdd:PRK11248 3 QISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 443 QDTSLLH-RSIRDNLLYGR--PGASDAElmeavRKARADEFIPLLsdaeGRRGFDAHvgeRGVKLSGGQRQRIAIARVLL 519
Cdd:PRK11248 77 QNEGLLPwRNVQDNVAFGLqlAGVEKMQ-----RLEIAHQMLKKV----GLEGAEKR---YIWQLSGGQRQRVGIARALA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598424 520 KDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAH 560
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH 187
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
362-590 |
1.44e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.86 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQ--GLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIG 439
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQlnGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQ--DTSLLHRSIRDNLLYG--RPGASDAELMEavrkaRADEFIPLLSDAEGRRgfdahvgERGVKLSGGQRQRIAIA 515
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGmeNQGIPREEMIK-----RVDEALLAVNMLDFKT-------REPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 516 RVLLKDAPILILDEATSALDSEVESAIQESLETLMQGK--TVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELLA 590
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
362-590 |
1.59e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.84 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAgVTQESL---RAQI 438
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQ--DTSLLHRSIRDNLLYGrP---GASDAELMEAVRKARAdefipllsdAEGRRGFDAHVGERgvkLSGGQRQRIA 513
Cdd:PRK13639 81 GIVFQnpDDQLFAPTVEEDVAFG-PlnlGLSKEEVEKRVKEALK---------AVGMEGFENKPPHH---LSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 514 IARVLLKDAPILILDEATSALDSEVESAIQESLETL-MQGKTVIAIAHRLSTIAR-MDRLVVLDKGHIAESGTHAELLA 590
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
377-583 |
1.60e-22 |
|
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: 96.45 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQdIAGVtqesLRAQIGMvtqDTSLlhrSIRDN- 455
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSL----LGLGGGF---NPEL---TGRENi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 456 ----LLYGRPGASDAELMeavrkaradEFIPLLSDAEGRrgFDAHVGErgvkLSGGQRQRIAIARVLLKDAPILILDEAT 531
Cdd:cd03220 106 ylngRLLGLSRKEIDEKI---------DEIIEFSELGDF--IDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598424 532 SALDSE-VESAIQESLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:cd03220 171 AVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
362-590 |
1.62e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.00 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQ--DIAGVTQESLRAQIG 439
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQ--DTSLLHRSIRDNLLYG--RPGASDAELMEAVRKARADEFIPLLSDAEgrrgfdAHVgergvkLSGGQRQRIAIA 515
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKDKP------THC------LSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 516 RVLLKDAPILILDEATSALD----SEVESAIQESLETLmqGKTVIAIAHRLSTIA-RMDRLVVLDKGHIAESGTHAELLA 590
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
381-588 |
2.01e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 99.33 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 381 LDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVtqESLRAQIGMVTQDTSLL-HRSIRDNLLYG 459
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGVGMVFQSYALYpHLSVAENMSFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 460 R--PGASDAELMEAVRKARadEFIPLlsdaegrrgfdAHVGERGVK-LSGGQRQRIAIARVLLKDAPILILDEATSALDS 536
Cdd:PRK11000 100 LklAGAKKEEINQRVNQVA--EVLQL-----------AHLLDRKPKaLSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 537 EVESAIQESLETLMQ--GKTVIAIAH---RLSTIArmDRLVVLDKGHIAESGTHAEL 588
Cdd:PRK11000 167 ALRVQMRIEISRLHKrlGRTMIYVTHdqvEAMTLA--DKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
365-591 |
2.15e-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: 96.07 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 365 EHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIagvTQESL--RAQIGM-- 440
Cdd:cd03218 4 ENLSKRYGKRK-VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI---TKLPMhkRARLGIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTSLLHR-SIRDNLLygrpgaSDAELMEAVRKARADEFIPLLSDaegrrgFD-AHVGER-GVKLSGGQRQRIAIARV 517
Cdd:cd03218 80 LPQEASIFRKlTVEENIL------AVLEIRGLSKKEREEKLEELLEE------FHiTHLRKSkASSLSGGERRRVEIARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598424 518 LLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIA-HRLS-TIARMDRLVVLDKGHIAESGTHAELLAH 591
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
378-535 |
3.00e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 95.24 E-value: 3.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 378 IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLE---SGRILVDGQDIAGVTQEslRAQIGMVTQDtSLL--HRSI 452
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQD-DLLfpHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 453 RDNLLYGRPgasdAELMEAVRKARADEfipLLSDAEGrrgfdAHVGERGVK-LSGGQRQRIAIARVLLKDAPILILDEAT 531
Cdd:COG4136 94 GENLAFALP----PTIGRAQRRARVEQ---ALEEAGL-----AGFADRDPAtLSGGQRARVALLRALLAEPRALLLDEPF 161
|
....
gi 15598424 532 SALD 535
Cdd:COG4136 162 SKLD 165
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
370-588 |
3.13e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 98.38 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 370 HYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDiagVTQESLRAQ-IGMVTQDTSLL 448
Cdd:PRK11650 12 SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV---VNELEPADRdIAMVFQNYALY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 449 -HRSIRDNLLYG---RpGASDAELMEAVRK-ARADEFIPLLsDAEGRrgfdahvgergvKLSGGQRQRIAIARVLLKDAP 523
Cdd:PRK11650 89 pHMSVRENMAYGlkiR-GMPKAEIEERVAEaARILELEPLL-DRKPR------------ELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 524 ILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAH---RLSTIArmDRLVVLDKGHIAESGTHAEL 588
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMRLEIQRLHRrlKTTSLYVTHdqvEAMTLA--DRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
377-606 |
4.16e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.95 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESL----RAQIGMVTQDTSLL-HRS 451
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLsHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 452 IRDNLlygRPGASDAELMEAVRKARADEFIpllsdaeGRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEAT 531
Cdd:PRK10535 103 AAQNV---EVPAVYAGLERKQRLLRAQELL-------QRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 532 SALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARMDRLVVLDKGHI-AESGTHAELLAHGGLYARL-----WQHQTG 604
Cdd:PRK10535 173 GALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIvRNPPAQEKVNVAGGTEPVVntasgWRQFVS 252
|
..
gi 15598424 605 GF 606
Cdd:PRK10535 253 GF 254
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
362-588 |
4.71e-22 |
|
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: 94.88 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSG-VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIagVTQ-ESLRAQIG 439
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDrKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQDTSLLHR-SIRDNL-----LYGRPGASDAELMEAVRKARadefipllsdaegrrGFDAHVGERGVKLSGGQRQRIA 513
Cdd:cd03263 79 YCPQFDALFDElTVREHLrfyarLKGLPKSEIKEEVELLLRVL---------------GLTDKANKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598424 514 IARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAEL 588
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALcDRIAIMSDGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
362-583 |
5.55e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.96 E-value: 5.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMV 441
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQD--TSLLHRSIRDNLLYG--RPGASDAELMEAVRKARAdefiplLSDAEGRRGFDAHvgergvKLSGGQRQRIAIARV 517
Cdd:PRK13647 85 FQDpdDQVFSSTVWDDVAFGpvNMGLDKDEVERRVEEALK------AVRMWDFRDKPPY------HLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 518 LLKDAPILILDEATSALDSEVESAIQESLETL-MQGKTVIAIAHRLSTIAR-MDRLVVLDKGHIAESG 583
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEG 220
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
362-589 |
8.71e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.76 E-value: 8.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMV 441
Cdd:COG4604 2 IEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLLHR-SIRDNLLYGR-------PGASDAELMEavrkaRADEFIPlLSDAEGRrgfdaHVGErgvkLSGGQRQRIA 513
Cdd:COG4604 81 RQENHINSRlTVRELVAFGRfpyskgrLTAEDREIID-----EAIAYLD-LEDLADR-----YLDE----LSGGQRQRAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 514 IARVLLKDAPILILDEATSALDsevesaIQESLEtLMQ---------GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLD------MKHSVQ-MMKllrrladelGKTVVIVLHDINFASCYaDHIVAMKDGRVVAQG 218
|
....*.
gi 15598424 584 THAELL 589
Cdd:COG4604 219 TPEEII 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
369-589 |
1.65e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.34 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 369 FHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQ------DIAGVTQESLRAQIGMVT 442
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 443 QDTSLL-HRSIRDNLLYgrPGASdaelmEAVRKARadEFIPLLSDAEGRRGFDAHVGER----GVKLSGGQRQRIAIARV 517
Cdd:PRK14246 97 QQPNPFpHLSIYDNIAY--PLKS-----HGIKEKR--EIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 518 LLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELL 589
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
361-567 |
3.20e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 93.69 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 361 EVEFEHIAFHYGKGSGViQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDL-----ESGRILVDGQDI--AGVTQES 433
Cdd:PRK14243 10 VLRTENLNVYYGSFLAV-KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 434 LRAQIGMVTQDTSLLHRSIRDNLLYGR-----PGASDaELME-AVRKARA-DEFIPLLSDAegrrgfdahvgerGVKLSG 506
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYGAringyKGDMD-ELVErSLRQAALwDEVKDKLKQS-------------GLSLSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598424 507 GQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIAR 567
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAAR 215
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
378-583 |
3.33e-21 |
|
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: 92.91 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 378 IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLraqigMVTQDTSLLH-RSIRDNL 456
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 457 lYGRPGASDAELMEAVRKARADEFIPLLsdaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDS 536
Cdd:TIGR01184 76 -ALAVDRVLPDLSKSERRAIVEEHIALV-------GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598424 537 EVESAIQESLETLMQ--GKTVIAIAHRL-STIARMDRLVVLDKGHIAESG 583
Cdd:TIGR01184 148 LTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
361-592 |
3.68e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 93.93 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 361 EVEFEHIAFHYGKGSG----VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQE---- 432
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 433 SLRAQIGMVTQ--DTSLLHRSIRDNLLYGrP---GASDAElmeavRKARADEFIPLLsdaegrrGFDAHVGERG-VKLSG 506
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFG-PmnfGVSEED-----AKQKAREMIELV-------GLPEELLARSpFELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 507 GQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIAR-MDRLVVLDKGHIAESG 583
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQG 228
|
....*....
gi 15598424 584 THAELLAHG 592
Cdd:PRK13634 229 TPREIFADP 237
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
365-590 |
4.54e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.65 E-value: 4.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 365 EHIAFHYgKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVT-QESLRAQIGMVTQ 443
Cdd:PRK10895 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 444 DTSLLHR-SIRDNLLYGRPGASDaeLMEAVRKARADEFIPLLSDAEGRRGFdahvgerGVKLSGGQRQRIAIARVLLKDA 522
Cdd:PRK10895 86 EASIFRRlSVYDNLMAVLQIRDD--LSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 523 PILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRL-STIARMDRLVVLDKGHIAESGTHAELLA 590
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
27-590 |
5.45e-21 |
|
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: 96.79 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 27 RFYVYFLRQVWPVFLALLVVGLIVALIEVALFSYLGRIVDLAQSTPSAeffrvhaneLIWMAVVALVLRPLFNALHDMLV 106
Cdd:COG4615 2 NLLRLLLRESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALAR---------LLLLFAGLLVLLLLSRLASQLLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 107 HQSINPSMTNLiRWQNHRYVLKQSLGFFQNDFAGRIAQRIMQTGNSLRDSAVQVVDALWHVLIyTVSALVLFAEADWRLM 186
Cdd:COG4615 73 TRLGQHAVARL-RLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVAL-VLGCLAYLAWLSPPLF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 187 IPLVLWVFAYVGALAYFVPQVKRRSVEASDSRSKLMGR---IVDGytnITTLKLFAHTRQE--EDYAREAIGDQTLKSQR 261
Cdd:COG4615 151 LLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHfraLLEG---FKELKLNRRRRRAffDEDLQPTAERYRDLRIR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 262 AGRVVTSMDVTITVMNGVLItgttGLALWLWSQelISVGAIALATGLVIRINNMSGWIMWVVGGI---------FENIGQ 332
Cdd:COG4615 228 ADTIFALANNWGNLLFFALI----GLILFLLPA--LGWADPAVLSGFVLVLLFLRGPLSQLVGALptlsranvaLRKIEE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 333 VQDGMQTialPRKVVDREDAQPLRVERGEVEFEHIAFHY----GKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLL 408
Cdd:COG4615 302 LELALAA---AEPAAADAAAPPAPADFQTLELRGVTYRYpgedGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 409 LRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRsirdnlLYGRPGASDAElmeavrkaRADEFIPLLsdae 488
Cdd:COG4615 379 TGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGEADPA--------RARELLERL---- 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 489 grrGFDAHVGERG-----VKLSGGQRQRIAIARVLLKDAPILILDE-AtsaldsevesAIQ----------ESLETLM-Q 551
Cdd:COG4615 441 ---ELDHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDEwA----------ADQdpefrrvfytELLPELKaR 507
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 15598424 552 GKTVIAIAH--RLSTIArmDRLVVLDKGHIAESGTHAELLA 590
Cdd:COG4615 508 GKTVIAISHddRYFDLA--DRVLKMDYGKLVELTGPAALAA 546
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
377-593 |
6.69e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.25 E-value: 6.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIagvtQESLRAQIG-----------Mvtqdt 445
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIGylpeerglypkM----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 446 sllhrSIRDNLLY-GR-PGASDAELmeavrKARADEFIPLLsDAEGRRgfDAHVGErgvkLSGGQRQRIAIARVLLKDAP 523
Cdd:COG4152 87 -----KVGEQLVYlARlKGLSKAEA-----KRRADEWLERL-GLGDRA--NKKVEE----LSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598424 524 ILILDEATSALD----SEVESAIQESLEtlmQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAHGG 593
Cdd:COG4152 150 LLILDEPFSGLDpvnvELLKDVIRELAA---KGTTVIFSSHQMELVEELcDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
373-591 |
6.99e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 93.88 E-value: 6.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 373 KGSGVIQGLD---LKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAG---VTQESLRAQIGMVTQD-- 444
Cdd:PRK11308 23 KPERLVKALDgvsFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNpy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 445 TSLLHR-SIRDNLlyGRPGASDAELMEAVRKARADEFIpllsdaegrrgfdAHVGERGVK-------LSGGQRQRIAIAR 516
Cdd:PRK11308 103 GSLNPRkKVGQIL--EEPLLINTSLSAAERREKALAMM-------------AKVGLRPEHydryphmFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 517 VLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLST---IArmDRLVVLDKGHIAESGTHAELLAH 591
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQelGLSYVFISHDLSVvehIA--DEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
377-577 |
7.64e-21 |
|
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: 91.73 E-value: 7.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQ----DIAGVTQE---SLRAQ-IGMVTQ----- 443
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPReilALRRRtIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 444 ------DT---SLLHRsirdnllygrpGASDAelmEAVRKARAdefipLLsdaegRRgfdAHVGERGVKL-----SGGQR 509
Cdd:COG4778 106 prvsalDVvaePLLER-----------GVDRE---EARARARE-----LL-----AR---LNLPERLWDLppatfSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 510 QRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARM-DRLVVLDKG 577
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKaRGTAIIGIFHDEEVREAVaDRVVDVTPF 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
360-589 |
1.35e-20 |
|
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: 92.22 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 360 GEVEFEHIAFHYGK-GSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLEsGRILVDGQDIAGVTQESLRAQI 438
Cdd:cd03289 1 GQMTVKDLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLLHRSIRDNL-LYGRpgASDAELMEAvrkarADEfIPLLSDAEGRRG-FDAHVGERGVKLSGGQRQRIAIAR 516
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLdPYGK--WSDEEIWKV-----AEE-VGLKSVIEQFPGqLDFVLVDGGCVLSHGHKQLMCLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 517 VLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAELL 589
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
355-584 |
1.35e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 91.61 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 355 LRVERGEVEFEHiafhygkgSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLES---------GRILVDGQD 425
Cdd:PRK09984 5 IRVEKLAKTFNQ--------HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 426 IAGVTQESlRAQIGMVTQDTSLLHR-SIRDNLLYGRPGASD-----AELMEAVRKARADEfipllsdAEGRRGFDAHVGE 499
Cdd:PRK09984 77 LARDIRKS-RANTGYIFQQFNLVNRlSVLENVLIGALGSTPfwrtcFSWFTREQKQRALQ-------ALTRVGMVHFAHQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 500 RGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDK 576
Cdd:PRK09984 149 RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRYcERIVALRQ 228
|
....*...
gi 15598424 577 GHIAESGT 584
Cdd:PRK09984 229 GHVFYDGS 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
362-592 |
2.62e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.38 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGS----GVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQES---- 433
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 434 LRAQIGMVTQ--DTSLLHRSIRDNLLYGrPGASDAELMEAvrKARADEfipLLSDAegrrGFDAHVGERG-VKLSGGQRQ 510
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFG-PKNFKMNLDEV--KNYAHR---LLMDL----GFSRDVMSQSpFQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 511 RIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLM--QGKTVIAIAHRLSTIAR-MDRLVVLDKGHIAESGTHAE 587
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKE 232
|
....*
gi 15598424 588 LLAHG 592
Cdd:PRK13646 233 LFKDK 237
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
386-589 |
2.76e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.11 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 386 RPGEKIGLVGPSGAGKSTLVNLL--LRLYDLE-SGRILVDGQDIagvTQESLRAQIGMVTQDTSLL-HRSIRDNLLYGRP 461
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALafRSPKGVKgSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIpTLTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 462 GASDAELMEAVRKARADEFIP---LLSDAEGRRGfdahVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEV 538
Cdd:TIGR00955 126 LRMPRRVTKKEKRERVDEVLQalgLRKCANTRIG----VPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFM 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598424 539 ESAIQESLETLMQ-GKTVIAIAHR-LSTIARM-DRLVVLDKGHIAESGTHAELL 589
Cdd:TIGR00955 202 AYSVVQVLKGLAQkGKTIICTIHQpSSELFELfDKIILMAEGRVAYLGSPDQAV 255
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
393-598 |
3.99e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 95.23 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 393 LVGPSGAGKSTLVNLLLRLYDLESGRILVDgqdiagvtqeslrAQIGMVTQDTSLLHRSIRDNLLYGRPgASDAELMEAV 472
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNILFFDE-EDAARLADAV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 473 RKARADEFIPLLSDaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEV-ESAIQESLETLMQ 551
Cdd:PTZ00243 757 RVSQLEADLAQLGG-----GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVEECFLGALA 831
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598424 552 GKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAElLAHGGLYARL 598
Cdd:PTZ00243 832 GKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATL 877
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
361-591 |
4.08e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 94.27 E-value: 4.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 361 EVEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGM 440
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTSLLHRsirdnLLYGRPGASDAELMEA-------VRKARADEFipLLSDaegrrgfdahvgergVKLSGGQRQRIA 513
Cdd:PRK10522 402 VFTDFHLFDQ-----LLGPEGKPANPALVEKwlerlkmAHKLELEDG--RISN---------------LKLSKGQKKRLA 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 514 IARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARMDRLVVLDKGHIAE-SGTHAELLA 590
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAAS 539
|
.
gi 15598424 591 H 591
Cdd:PRK10522 540 R 540
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
370-604 |
5.53e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.03 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 370 HYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQ-------------ESLRA 436
Cdd:PRK10619 14 RYGEHE-VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqlRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 437 QIGMVTQDTSLL-HRSIRDNLLYGrP----GASDAELMEavrkaRADEFIPLLSDAEGRRGfdahvgERGVKLSGGQRQR 511
Cdd:PRK10619 93 RLTMVFQHFNLWsHMTVLENVMEA-PiqvlGLSKQEARE-----RAVKYLAKVGIDERAQG------KYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 512 IAIARVLLKDAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLStIAR--MDRLVVLDKGHIAESGTHAEL 588
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMG-FARhvSSHVIFLHQGKIEEEGAPEQL 239
|
250
....*....|....*.
gi 15598424 589 LAHGGlYARLWQHQTG 604
Cdd:PRK10619 240 FGNPQ-SPRLQQFLKG 254
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
378-598 |
6.46e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 90.92 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 378 IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDG----QDiagvtQESLRAQIGMV----TQ------ 443
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfKR-----RKEFARRIGVVfgqrSQlwwdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 444 --DTSLLHRSIrdnllYGRPgasdaelmEAVRKARADEFIPLLSdaegrrgfdahVGE------RgvKLSGGQRQRIAIA 515
Cdd:COG4586 113 aiDSFRLLKAI-----YRIP--------DAEYKKRLDELVELLD-----------LGElldtpvR--QLSLGQRMRCELA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 516 RVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAHG 592
Cdd:COG4586 167 AALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRerGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKERF 246
|
....*.
gi 15598424 593 GLYARL 598
Cdd:COG4586 247 GPYKTI 252
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
362-584 |
6.88e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 91.68 E-value: 6.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKgSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESlrAQIGMV 441
Cdd:PRK10851 3 IEIANIKKSFGR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDTSLL-HRSIRDNLLYG--------RPGAsdAELMEAVrkARADEFIPLlsdaegrrgfdAHVGER-GVKLSGGQRQR 511
Cdd:PRK10851 80 FQHYALFrHMTVFDNIAFGltvlprreRPNA--AAIKAKV--TQLLEMVQL-----------AHLADRyPAQLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598424 512 IAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAH-RLSTIARMDRLVVLDKGHIAESGT 584
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
362-583 |
7.13e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.31 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIafhyGKGSGVIQGL---DLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEsLRAQ- 437
Cdd:PRK09700 6 ISMAGI----GKSFGPVHALksvNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 438 -IGMVTQDTSLLHR-SIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDAEG-RRGFDAHVGErgvkLSGGQRQRIAI 514
Cdd:PRK09700 81 gIGIIYQELSVIDElTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGlKVDLDEKVAN----LSISHKQMLEI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 515 ARVLLKDAPILILDEATSAL-DSEVES--AIQESLETlmQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLtNKEVDYlfLIMNQLRK--EGTAIVYISHKLAEIRRIcDRYTVMKDGSSVCSG 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
346-591 |
9.57e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.44 E-value: 9.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 346 VVDREDAQPLRVERGEVEFEHIAFHYgKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQD 425
Cdd:PRK11607 4 AIPRPQAKTRKALTPLLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 426 IAGVTqeSLRAQIGMVTQDTSLL-HRSIRDNLLYGrpgASDAELMEAVRKARADEFIPLLSDAEgrrgfdaHVGERGVKL 504
Cdd:PRK11607 83 LSHVP--PYQRPINMMFQSYALFpHMTVEQNIAFG---LKQDKLPKAEIASRVNEMLGLVHMQE-------FAKRKPHQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 505 SGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAE 581
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTMaGRIAIMNRGKFVQ 230
|
250
....*....|
gi 15598424 582 SGTHAELLAH 591
Cdd:PRK11607 231 IGEPEEIYEH 240
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
362-588 |
1.11e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.38 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDiagvTQE-----SLRA 436
Cdd:PRK13633 10 VSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD----TSDeenlwDIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 437 QIGMVTQ--DTSLLHRSIRDNLLYGrP---GASDAELmeavrKARADEFIPLLSDAEGRRgFDAHVgergvkLSGGQRQR 511
Cdd:PRK13633 86 KAGMVFQnpDNQIVATIVEEDVAFG-PenlGIPPEEI-----RERVDESLKKVGMYEYRR-HAPHL------LSGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 512 IAIARVLLKDAPILILDEATSALD----SEVESAIQESLETlmQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAE 587
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKK--YGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
.
gi 15598424 588 L 588
Cdd:PRK13633 231 I 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
362-578 |
1.11e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.94 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKgSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLES-----GRILVDGQDI--AGVTQESL 434
Cdd:PRK14258 8 IKVNNLSFYYDT-QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 435 RAQIGMVTQDTSLLHRSIRDNLLYG------RPgasDAELMEAVRKAradefiplLSDAEGRRGFDAHVGERGVKLSGGQ 508
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRP---KLEIDDIVESA--------LKDADLWDEIKHKIHKSALDLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 509 RQRIAIARVLLKDAPILILDEATSALDS----EVESAIQESleTLMQGKTVIAIAHRLSTIARMDRLVVLDKGH 578
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSL--RLRSELTMVIVSHNLHQVSRLSDFTAFFKGN 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
377-589 |
1.33e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.59 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLL--RLYDLESGRILVDGQDIAGV-TQESLRAQIGMVTQD--------- 444
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELsPDERARAGIFLAFQYpveipgvsv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 445 TSLLHRSirdnllygrpgasdaelMEAVRKARAD--EFIPLLSDAEGRRGFDAHVGERGV--KLSGGQRQRIAIARVLLK 520
Cdd:COG0396 95 SNFLRTA-----------------LNARRGEELSarEFLKLLKEKMKELGLDEDFLDRYVneGFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAH--RLSTIARMDRLVVLDKGHIAESGThAELL 589
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KELA 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
355-560 |
1.63e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 355 LRVERGEVEfehiafhygkgsgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIagvTQESL 434
Cdd:PRK13539 8 LACVRGGRV-------------LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 435 RAQIgmvtqdTSLLHR-------SIRDNL-----LYGRPGASDAELMEAVRkaradefiplLSDAEGRRGFDahvgergv 502
Cdd:PRK13539 72 AEAC------HYLGHRnamkpalTVAENLefwaaFLGGEELDIAAALEAVG----------LAPLAHLPFGY-------- 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 503 kLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLET-LMQGKTVIAIAH 560
Cdd:PRK13539 128 -LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIAATH 185
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
364-588 |
2.56e-19 |
|
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: 88.37 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 364 FEHIAFHygkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQdiagvtqeslraqIGMVTQ 443
Cdd:cd03291 42 FSNLCLV---GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 444 DTSLLHRSIRDNLLYGRpgASDAELMEAVRKA-RADEFIPLLSDAEgrrgfDAHVGERGVKLSGGQRQRIAIARVLLKDA 522
Cdd:cd03291 106 FSWIMPGTIKENIIFGV--SYDEYRYKSVVKAcQLEEDITKFPEKD-----NTVLGEGGITLSGGQRARISLARAVYKDA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 523 PILILDEATSALDSEVESAIQES-LETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAEL 588
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
352-579 |
2.86e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.81 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 352 AQPLRVERG-EVEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILvdgqdiAGVT 430
Cdd:PRK11247 2 MNTARLNQGtPLLLNAVSKRYG-ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL------AGTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 431 Q-ESLRAQIGMVTQDTSLLH-RSIRDNLLYG-----RPGASDAelMEAVrkaradefipllsdaegrrGFDAHVGERGVK 503
Cdd:PRK11247 75 PlAEAREDTRLMFQDARLLPwKKVIDNVGLGlkgqwRDAALQA--LAAV-------------------GLADRANEWPAA 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 504 LSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLS-TIARMDRLVVLDKGHI 579
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
374-579 |
3.28e-19 |
|
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: 85.56 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 374 GSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAG-VTQESLRAQIGMVTQDTS----LL 448
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrSPRDAIRAGIAYVPEDRKreglVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 449 HRSIRDNLLygrpgasdaelmeavrkaradefIPLLsdaegrrgfdahvgergvkLSGGQRQRIAIARVLLKDAPILILD 528
Cdd:cd03215 92 DLSVAENIA-----------------------LSSL-------------------LSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598424 529 EATSALDseVEsAIQESLETLM----QGKTVIAIAHRLSTIARM-DRLVVLDKGHI 579
Cdd:cd03215 130 EPTRGVD--VG-AKAEIYRLIReladAGKAVLLISSELDELLGLcDRILVMYEGRI 182
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
369-577 |
3.99e-19 |
|
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: 86.23 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 369 FHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRIL----VDGQDIAGVTQESLRAQIGMVTQD 444
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 445 TSLLHRSIRDNLLYGRPgaSDAELMEAVRKA---RAD-EFIPLlsdaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLK 520
Cdd:cd03290 88 PWLLNATVEENITFGSP--FNKQRYKAVTDAcslQPDiDLLPF--------GDQTEIGERGINLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 521 DAPILILDEATSALDSEV-ESAIQESLETLMQG--KTVIAIAHRLSTIARMDRLVVLDKG 577
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLsDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
346-601 |
4.41e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 91.90 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 346 VVDREDAQPLRVERGEVEFEHIAFHYGK-GSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLEsGRILVDGQ 424
Cdd:TIGR01271 1202 VIENPHAQKCWPSGGQMDVQGLTAKYTEaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGV 1280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 425 DIAGVTQESLRAQIGMVTQDTSLLHRSIRDNLlygRPGA--SDAELMEAVRKARADEFIPLLSDAegrrgFDAHVGERGV 502
Cdd:TIGR01271 1281 SWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQFPDK-----LDFVLVDGGY 1352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 503 KLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAES 582
Cdd:TIGR01271 1353 VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQY 1432
|
250
....*....|....*....
gi 15598424 583 GTHAELLAHGGLYARLWQH 601
Cdd:TIGR01271 1433 DSIQKLLNETSLFKQAMSA 1451
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
377-579 |
4.47e-19 |
|
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: 86.62 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQdIAGVTQESLRAQIGMV----TQ--------D 444
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVfgqkTQlwwdlpviD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 445 TSLLHRSIRDnllygrpgasdaeLMEAVRKARADEFIPLLSDAEgrrgfDAHVGERgvKLSGGQRQRIAIARVLLKDAPI 524
Cdd:cd03267 115 SFYLLAAIYD-------------LPPARFKKRLDELSELLDLEE-----LLDTPVR--QLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 525 LILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHI 579
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRerGTTVLLTSHYMKDIEALaRRVLVIDKGRL 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
362-597 |
5.15e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.55 E-value: 5.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMV 441
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQ--DTSLLHRSIRDNLLYGrpgASDAELMEAVRKARADEFIPLLSDAEGRRGFDAHvgergvkLSGGQRQRIAIARVLL 519
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFG---PINLGLDEETVAHRVSSALHMLGLEELRDRVPHH-------LSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 520 KDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAHGGLYA 596
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQPDLLA 233
|
.
gi 15598424 597 R 597
Cdd:PRK13652 234 R 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
365-591 |
7.69e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 86.24 E-value: 7.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 365 EHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIagvTQESL--RAQ--IGM 440
Cdd:COG1137 7 ENLVKSYGKRT-VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI---THLPMhkRARlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 VTQDTSLLHR-SIRDNLLygrpgaSDAELME---AVRKARADEfipLLSDaegrrgFD-AHVGE-RGVKLSGGQRQRIAI 514
Cdd:COG1137 83 LPQEASIFRKlTVEDNIL------AVLELRKlskKEREERLEE---LLEE------FGiTHLRKsKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 515 ARVLLKDAPILILDEATSALD----SEvesaIQESLETL-MQGktvIAIahrL-------STIARMDRLVVLDKGHIAES 582
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDpiavAD----IQKIIRHLkERG---IGV---LitdhnvrETLGICDRAYIISEGKVLAE 217
|
....*....
gi 15598424 583 GTHAELLAH 591
Cdd:COG1137 218 GTPEEILNN 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
362-583 |
8.42e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.43 E-value: 8.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLE-----SGRILVDGQDIAG--VTQESL 434
Cdd:PRK14267 5 IETVNLRVYYGSNH-VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSpdVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 435 RAQIGMVTQ-DTSLLHRSIRDNLLYG----RPGASDAELMEAVR-----KARADEFIPLLSDAEGrrgfdahvgergvKL 504
Cdd:PRK14267 84 RREVGMVFQyPNPFPHLTIYDNVAIGvklnGLVKSKKELDERVEwalkkAALWDEVKDRLNDYPS-------------NL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 505 SGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESG 583
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVG 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
374-588 |
8.81e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 91.13 E-value: 8.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 374 GSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQdiagvtqeslraqIGMVTQDTSLLHRSIR 453
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 454 DNLLYGRpgASDAELMEAVRKA-RADEFIPLLSDAEgrrgfDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATS 532
Cdd:TIGR01271 505 DNIIFGL--SYDEYRYTSVIKAcQLEEDIALFPEKD-----KTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 533 ALDSEVESAIQES-LETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGTHAEL 588
Cdd:TIGR01271 578 HLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
381-600 |
1.05e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.01 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 381 LDLKVR---PGEKI-GLVGPSGAGKSTLVNLLLRLYDLESGRI------LVDGQDIAGVTQESLRaqIGMVTQDTSLL-H 449
Cdd:PRK11144 13 LCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvLFDAEKGICLPPEKRR--IGYVFQDARLFpH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 450 RSIRDNLLYGrpgasdaelMEAVRKARADEFIPLLsdaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDE 529
Cdd:PRK11144 91 YKVRGNLRYG---------MAKSMVAQFDKIVALL-------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 530 ATSALDSEVESAIQESLETLMQG-KT-VIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAHGGLyaRLWQ 600
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREiNIpILYVSHSLDEILRLaDRVVVLEQGKVKAFGPLEEVWASSAM--RPWL 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
360-598 |
1.50e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.22 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 360 GEVEFEHIAFHYGKGS----GVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDI-AGVTQ--- 431
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKike 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 432 -ESLRAQIGMVTQ--DTSLLHRSIRDNLLYGrPGASDAELMEAVRKAraDEFIPLLSDAEgrrgfdAHVGERGVKLSGGQ 508
Cdd:PRK13645 85 vKRLRKEIGLVFQfpEYQLFQETIEKDIAFG-PVNLGENKQEAYKKV--PELLKLVQLPE------DYVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 509 RQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETL--MQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTH 585
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVLRIaDEVIVMHEGKVISIGSP 235
|
250
....*....|...
gi 15598424 586 AELLAHGGLYARL 598
Cdd:PRK13645 236 FEIFSNQELLTKI 248
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
377-591 |
1.62e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.13 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQdIAgvtqeslraqigmvtqdtSLL------HR 450
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VS------------------ALLelgagfHP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 451 SI--RDN-----LLYGRPGASDAELMEAVRkaradEFipllsdAEGRRGFDAHVGergvKLSGGQRQRIAIARVLLKDAP 523
Cdd:COG1134 102 ELtgRENiylngRLLGLSRKEIDEKFDEIV-----EF------AELGDFIDQPVK----TYSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 524 ILILDEATSALDSE----VESAIQESLEtlmQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:COG1134 167 ILLVDEVLAVGDAAfqkkCLARIRELRE---SGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
374-589 |
2.02e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.61 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 374 GSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQI-----------GMVT 442
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVaylpqqlpaaeGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 443 QDTSLLHRSIRDNLLyGRPGASDAElmeavrkaRADEFIPLLsdaeGRRGFdAHvgeRGV-KLSGGQRQRIAIARVLLKD 521
Cdd:PRK10575 103 RELVAIGRYPWHGAL-GRFGAADRE--------KVEEAISLV----GLKPL-AH---RLVdSLSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598424 522 APILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELL 589
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQerGLTVIAVLHDINMAARYcDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
380-580 |
2.17e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.45 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 380 GLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLES--GRILVDGQDI-AGVTQESLRAQIGMVTQDTSLL-HRSIRDN 455
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELqASNIRDTERAGIAIIHQELALVkELSVLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 456 LLYG----RPGASDAELMeavrKARADEfipLLSdaegRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEAT 531
Cdd:PRK13549 103 IFLGneitPGGIMDYDAM----YLRAQK---LLA----QLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598424 532 SAL-DSEVES--AIQESLETlmQGKTVIAIAHRLSTIARM-DRLVVLDKG-HIA 580
Cdd:PRK13549 172 ASLtESETAVllDIIRDLKA--HGIACIYISHKLNEVKAIsDTICVIRDGrHIG 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
393-596 |
3.02e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.06 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 393 LVGPSGAGKSTLVN----LLLRLYDLESGRILVDGQDIAGVTQ------------ESLRAQIGMVTQ--DTSLLHRSIRD 454
Cdd:PRK13631 57 IIGNSGSGKSTLVThfngLIKSKYGTIQVGDIYIGDKKNNHELitnpyskkiknfKELRRRVSMVFQfpEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 455 NLLYGrPGASDAELMEAVRKARAdefipLLSdaegRRGFDAHVGERG-VKLSGGQRQRIAIARVLLKDAPILILDEATSA 533
Cdd:PRK13631 137 DIMFG-PVALGVKKSEAKKLAKF-----YLN----KMGLDDSYLERSpFGLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598424 534 LDSEVESAIQE-SLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAHGGLYA 596
Cdd:PRK13631 207 LDPKGEHEMMQlILDAKANNKTVFVITHTMEHVLEVaDEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
344-580 |
3.32e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 344 RKVVDREDAQPlrVERGEV--EFEHIAfhygkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILV 421
Cdd:COG1129 239 RELEDLFPKRA--AAPGEVvlEVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 422 DGQDIA-GVTQESLRAQIGMVTQD---TSL-LHRSIRDNLLYGRpgasdaelMEAVRKARadefipLLSDAEGRRGFDAH 496
Cdd:COG1129 312 DGKPVRiRSPRDAIRAGIAYVPEDrkgEGLvLDLSIRENITLAS--------LDRLSRGG------LLDRRRERALAEEY 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 497 VGERGVK----------LSGGQRQRIAIARVLLKDAPILILDEATSALD----SEVESAIQESLEtlmQGKTVIAIAHRL 562
Cdd:COG1129 378 IKRLRIKtpspeqpvgnLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgakAEIYRLIRELAA---EGKAVIVISSEL 454
|
250
....*....|....*....
gi 15598424 563 STIARM-DRLVVLDKGHIA 580
Cdd:COG1129 455 PELLGLsDRILVMREGRIV 473
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
362-579 |
3.58e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.27 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGV-IQGLD---LKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQ----ES 433
Cdd:PRK13641 3 IKFENVDYIYSPGTPMeKKGLDnisFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 434 LRAQIGMVTQ--DTSLLHRSIRDNLLYGrP---GASDAElmeavRKARADEFIPllsdaegRRGFDAHVGERG-VKLSGG 507
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFG-PknfGFSEDE-----AKEKALKWLK-------KVGLSEDLISKSpFELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 508 QRQRIAIARVLLKDAPILILDEATSALDSEV-ESAIQESLETLMQGKTVIAIAHRLSTIAR-MDRLVVLDKGHI 579
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
362-589 |
4.62e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.79 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGK----GSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQES---- 433
Cdd:PRK13643 2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 434 LRAQIGMVTQ--DTSLLHRSIRDNLLYGrPGASDAELMEAVR-KARADEFIPLLSDAEGRRGFDahvgergvkLSGGQRQ 510
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFG-PQNFGIPKEKAEKiAAEKLEMVGLADEFWEKSPFE---------LSGGQMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 511 RIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ-GKTVIAIAHRLSTIAR-MDRLVVLDKGHIAESGTHAEL 588
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDV 231
|
.
gi 15598424 589 L 589
Cdd:PRK13643 232 F 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
362-581 |
4.92e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.29 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGS---GVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQE---SLR 435
Cdd:PRK10584 7 VEVHHLKKSVGQGEhelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 436 AQ-IGMVTQDTSLLHR-SIRDN-----LLYgrpGASDAElmeavRKARADEFIPLLSDAEGRRGFDAhvgergvKLSGGQ 508
Cdd:PRK10584 87 AKhVGFVFQSFMLIPTlNALENvelpaLLR---GESSRQ-----SRNGAKALLEQLGLGKRLDHLPA-------QLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598424 509 RQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARMDRLVVLDKGHIAE 581
Cdd:PRK10584 152 QQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
393-590 |
5.09e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.38 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 393 LVGPSGAGKSTLVNLLLRLYD-----LESGRILVDGQDIAGVTQE-SLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDA 466
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRSIFNYRDVlEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 467 ELME--AVRKARADEFipLLSDAEGRRgfdahVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQE 544
Cdd:PRK14271 132 PRKEfrGVAQARLTEV--GLWDAVKDR-----LSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEE 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598424 545 SLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLA 590
Cdd:PRK14271 205 FIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFS 251
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
377-574 |
5.24e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.28 E-value: 5.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILV-DGQDIAGVTQES-LRAQIGMVTQDTSLLHRSIRD 454
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaGGARVAYVPQRSeVPDSLPLTVRDLVAMGRWARR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 455 NLLyGRPGASD----AELMEAVRkaradefiplLSDAEGRRgfdahVGErgvkLSGGQRQRIAIARVLLKDAPILILDEA 530
Cdd:NF040873 87 GLW-RRLTRDDraavDDALERVG----------LADLAGRQ-----LGE----LSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598424 531 TSALDSEVESAIQESL-ETLMQGKTVIAIAHRLSTIARMDRLVVL 574
Cdd:NF040873 147 TTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
362-584 |
7.33e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.03 E-value: 7.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGS----GVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQ----ES 433
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 434 LRAQIGMVTQ--DTSLLHRSIRDNLLYGrPGASDAELMEAVRKARadEFIPLLSDAE---GRRGFDahvgergvkLSGGQ 508
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG-PQNFGVSQEEAEALAR--EKLALVGISEslfEKNPFE---------LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 509 RQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ-GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGT 584
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGK 228
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
357-591 |
7.85e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.00 E-value: 7.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 357 VERGEVEFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAG-VTQESLR 435
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 436 AQIGMVTQDTSLLHR-SIRDNLLYGRPGASDAELMEavRKARADEFIPLLSDaegRRGfdahvgERGVKLSGGQRQRIAI 514
Cdd:PRK11614 80 EAVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQE--RIKWVYELFPRLHE---RRI------QRAGTMSGGEQQMLAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 515 ARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ-GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREqGMTIFLVEQNANQALKLaDRGYVLENGHVVLEDTGDALLAN 227
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
375-589 |
8.61e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.35 E-value: 8.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 375 SGVIQGLDLKVRPGEKIGLVGPSGAGKSTlvnLLLRLYDLES--GRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHrsi 452
Cdd:COG4138 9 AGRLGPISAQVNAGELIHLIGPNGAGKST---LLARMAGLLPgqGEILLNGRPLSDWSAAELARHRAYLSQQQSPPF--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 453 rdNL-------LYGRPGASDAELMEAVRK-ARADEFIPLLSdaegrrgfdahvgeRGV-KLSGGQRQRIAIARVLLK--- 520
Cdd:COG4138 83 --AMpvfqylaLHQPAGASSEAVEQLLAQlAEALGLEDKLS--------------RPLtQLSGGEWQRVRLAAVLLQvwp 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 521 ----DAPILILDEATSALDseveSAIQESLETLM-----QGKTVIAIAHRLS-TIARMDRLVVLDKGHIAESGTHAELL 589
Cdd:COG4138 147 tinpEGQLLLLDEPMNSLD----VAQQAALDRLLrelcqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
362-578 |
9.48e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 80.19 E-value: 9.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGqdiagvtqeslRAQIGMV 441
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQdtsllhrsirdnllygrpgasdaelmeavrkaradefipllsdaegrrgfdahvgergvkLSGGQRQRIAIARVLLKD 521
Cdd:cd03221 69 EQ------------------------------------------------------------LSGGEKMRLALAKLLLEN 88
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598424 522 APILILDEATSALDseVESaiQESLETLMQG--KTVIAIAH-R--LSTIArmDRLVVLDKGH 578
Cdd:cd03221 89 PNLLLLDEPTNHLD--LES--IEALEEALKEypGTVILVSHdRyfLDQVA--TKIIELEDGK 144
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
383-582 |
1.59e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 383 LKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIA--GvTQESLRAQIGMVTQDTSLL-HRSIRDNLLYG 459
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnG-PKSSQEAGIGIIHQELNLIpQLTIAENIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 460 RP-----GASDAELMeavrKARADEfipLLSDAEGRRGFDAHVGErgvkLSGGQRQRIAIARVLLKDAPILILDEATSAL 534
Cdd:PRK10762 104 REfvnrfGRIDWKKM----YAEADK---LLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598424 535 -DSEVESAIQESLETLMQGKTVIAIAHRLSTIARM-DRLVVL-DKGHIAES 582
Cdd:PRK10762 173 tDTETESLFRVIRELKSQGRGIVYISHRLKEIFEIcDDVTVFrDGQFIAER 223
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
362-576 |
1.62e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 80.28 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRIlvdgqdiagvtqeslraqigmv 441
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 tqdtsllHRSIRDNLLY--GRPGASDAELMEAVRKARADEfipllsdaegrrgfdahvgergvkLSGGQRQRIAIARVLL 519
Cdd:cd03223 59 -------GMPEGEDLLFlpQRPYLPLGTLREQLIYPWDDV------------------------LSGGEQQRLAFARLLL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 520 KDAPILILDEATSALDSEVESAIQESLETLmqGKTVIAIAHRLSTIARMDRLVVLDK 576
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
355-583 |
1.65e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 81.03 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 355 LRVERGEVEfehiafhygkgsgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLE--SGRILVDGQDIAGV-TQ 431
Cdd:cd03217 6 LHVSVGGKE-------------ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLpPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 432 ESLRAQIGMVTQDTSLLhrsirdnllygrPGASDAELMEAVrkaradefipllsdaegrrgfdahvgerGVKLSGGQRQR 511
Cdd:cd03217 73 ERARLGIFLAFQYPPEI------------PGVKNADFLRYV----------------------------NEGFSGGEKKR 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598424 512 IAIARVLLKDAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAH--RLSTIARMDRLVVLDKGHIAESG 583
Cdd:cd03217 113 NEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
365-589 |
1.99e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.73 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 365 EHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQD 444
Cdd:PRK10253 11 EQLTLGYGKYT-VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 445 TSllhrsirdnllygRPGasDAELMEAVRKARADEfIPLLS-----DAEG-----RRGFDAHVGERGV-KLSGGQRQRIA 513
Cdd:PRK10253 90 AT-------------TPG--DITVQELVARGRYPH-QPLFTrwrkeDEEAvtkamQATGITHLADQSVdTLSGGQRQRAW 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 514 IARVLLKDAPILILDEATSALDSEVESAIQESLETL--MQGKTVIAIAHRLSTIAR-MDRLVVLDKGHIAESGTHAELL 589
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIV 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
378-590 |
2.05e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.44 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 378 IQGLDLKVRPGEKIGLVGPSGAGKS----TLVNLLLRLYDLESGRILVDGQDIAGvtqESLRAQ-IGMVTQDT------- 445
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP---CALRGRkIATIMQNPrsafnpl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 446 -SLLHRSIRDNLLYGRPgASDAELMEAVRKARadefiplLSDAEgrRGFDAHVGErgvkLSGGQRQRIAIARVLLKDAPI 524
Cdd:PRK10418 96 hTMHTHARETCLALGKP-ADDATLTAALEAVG-------LENAA--RVLKLYPFE----MSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 525 LILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLA 590
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQkrALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFN 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
337-590 |
2.16e-17 |
|
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: 85.62 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 337 MQTIALPRKVVDREDAQPLrvergeVEFEHIAFHY-GKGSGVIQ---GLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLY 412
Cdd:TIGR03269 261 MEGVSEVEKECEVEVGEPI------IKVRNVSKRYiSVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 413 DLESGRILVD-GQDIAGVTQESL----RAQ--IGMVTQDTSLL-HRSIRDNLlygrpgaSDAELME-----AVRKARADE 479
Cdd:TIGR03269 335 EPTSGEVNVRvGDEWVDMTKPGPdgrgRAKryIGILHQEYDLYpHRTVLDNL-------TEAIGLElpdelARMKAVITL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 480 FIPLLSDAEGRRGFDAHVGErgvkLSGGQRQRIAIARVLLKDAPILILDEATSALDS----EVESAIQESLETLmqGKTV 555
Cdd:TIGR03269 408 KMVGFDEEKAEEILDKYPDE----LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPitkvDVTHSILKAREEM--EQTF 481
|
250 260 270
....*....|....*....|....*....|....*.
gi 15598424 556 IAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLA 590
Cdd:TIGR03269 482 IIVSHDMDFVLDVcDRAALMRDGKIVKIGDPEEIVE 517
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
378-591 |
3.55e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 82.85 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 378 IQGLDLKVRPGEKIGLVGPSGAGKS----TLVNLLLRlydleSGRI----LVDGQDIAGVTQESL---RA-QIGMVTQD- 444
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRIggsaTFNGREILNLPEKELnklRAeQISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 445 -TSLlhrsirdNLlYGRPGAsdaELME------AVRKARA-DEFIPLLsDA----EGRRGFDAHVGErgvkLSGGQRQRI 512
Cdd:PRK09473 107 mTSL-------NP-YMRVGE---QLMEvlmlhkGMSKAEAfEESVRML-DAvkmpEARKRMKMYPHE----FSGGMRQRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 513 AIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELL 589
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGIcDKVLVMYAGRTMEYGNARDVF 250
|
..
gi 15598424 590 AH 591
Cdd:PRK09473 251 YQ 252
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
385-577 |
5.38e-17 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 85.16 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 385 VRPGEKIGLVGPSGAGKSTLVNLLLRLYD---LESGRILVDGQDIagvtQESLRAQIGMVTQ-DTSLLHRSIRDNLLYG- 459
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPL----DSSFQRSIGYVQQqDLHLPTSTVRESLRFSa 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 460 ---RPGA-SDAELMEAVrkaraDEFIPLLsdaEGRRGFDAHVGERGVKLSGGQRQRIAIARVLL-KDAPILILDEATSAL 534
Cdd:TIGR00956 862 ylrQPKSvSKSEKMEYV-----EEVIKLL---EMESYADAVVGVPGEGLNVEQRKRLTIGVELVaKPKLLLFLDEPTSGL 933
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598424 535 DSEVESAIQESLETLMQ-GKTVIAIAHRLSTI--ARMDRLVVLDKG 577
Cdd:TIGR00956 934 DSQTAWSICKLMRKLADhGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
377-588 |
5.45e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.33 E-value: 5.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTqESLRAQIG--MVTQDTSLL-HRSIR 453
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGiyLVPQEPLLFpNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 454 DNLLYGRPGASDAElmeavRKARAdefipLLSDAEGRRGFDAHVGergvKLSGGQRQRIAIARVLLKDAPILILDEATSA 533
Cdd:PRK15439 105 ENILFGLPKRQASM-----QKMKQ-----LLAALGCQLDLDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 534 LD-SEVESAIQESLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAEL 588
Cdd:PRK15439 171 LTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQLaDRISVMRDGTIALSGKTADL 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
382-577 |
8.17e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 83.63 E-value: 8.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 382 DLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIA-GVTQESLRAQIGMVTQDTSL-LHRSIRDNLLYG 459
Cdd:PRK10982 18 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLvLQRSVMDNMWLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 460 R-PGAS---DAELMEAVRKARADEFipllsdaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSAL- 534
Cdd:PRK10982 98 RyPTKGmfvDQDKMYRDTKAIFDEL-----------DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLt 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598424 535 DSEVES--AIQESLETlmQGKTVIAIAHRLSTIARM-DRLVVLDKG 577
Cdd:PRK10982 167 EKEVNHlfTIIRKLKE--RGCGIVYISHKMEEIFQLcDEITILRDG 210
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
374-560 |
1.18e-16 |
|
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: 78.69 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 374 GSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSIR 453
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 454 DNLLYGRPGASDAELMEAVrkaradefipllsDAEGRRGF-DAHVGErgvkLSGGQRQRIAIARVLLKDAPILILDEATS 532
Cdd:cd03231 92 ENLRFWHADHSDEQVEEAL-------------ARVGLNGFeDRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180
....*....|....*....|....*....
gi 15598424 533 ALDSEVESAIQESLET-LMQGKTVIAIAH 560
Cdd:cd03231 155 ALDKAGVARFAEAMAGhCARGGMVVLTTH 183
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
361-590 |
1.47e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.90 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 361 EVEFEHIAFHYGKGS----GVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRI----------------- 419
Cdd:PRK13651 2 QIKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 420 LVDGQDIAGVTQ-------ESLRAQIGMVTQ--DTSLLHRSIRDNLLYGrPGASDAELMEAvrKARADEFIPLLsdaegr 490
Cdd:PRK13651 82 KVLEKLVIQKTRfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG-PVSMGVSKEEA--KKRAAKYIELV------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 491 rGFDAHVGERG-VKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETL-MQGKTVIAIAHRL-STIAR 567
Cdd:PRK13651 153 -GLDESYLQRSpFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEW 231
|
250 260
....*....|....*....|...
gi 15598424 568 MDRLVVLDKGHIAESGTHAELLA 590
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDTYDILS 254
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
377-577 |
3.10e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 82.23 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLL-RLYDLE-SGRILVDGQDIagvTQESLRaQIGMVTQDTSLL-HRSIR 453
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKP---TKQILK-RTGFVTQDDILYpHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 454 DNLLYGRPGASDAELMEAVRKARADEFIPLLSDAEGRRGFDAHVGERGVklSGGQRQRIAIARVLLKDAPILILDEATSA 533
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGI--SGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598424 534 LDSEVESAIQESLETLMQ-GKTVIAIAHRLST-IARM-DRLVVLDKG 577
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQkGKTIVTSMHQPSSrVYQMfDSVLVLSEG 283
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
367-590 |
5.18e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 367 IAF-HYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLY-----DLESGRILVDGQDIAGVTQESLRA---- 436
Cdd:PRK15134 13 VAFrQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvVYPSGDIRFHGESLLHASEQTLRGvrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 437 QIGMVTQD--TSL---------------LHRSIRdnllygrpgasdaelmeavRKARADEFIPLLsDAEGRRGFDAHVGE 499
Cdd:PRK15134 93 KIAMIFQEpmVSLnplhtlekqlyevlsLHRGMR-------------------REAARGEILNCL-DRVGIRQAAKRLTD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 500 RGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDK 576
Cdd:PRK15134 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLaDRVAVMQN 232
|
250
....*....|....
gi 15598424 577 GHIAESGTHAELLA 590
Cdd:PRK15134 233 GRCVEQNRAATLFS 246
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
377-588 |
5.28e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 78.14 E-value: 5.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLL--RLYDLESGRILVDGQDIAGVTQEsLRAQIGMVtqdtsllhrsird 454
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPE-ERAHLGIF------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 455 nLLYGRP----GASDAELME----AVRKARAD------EFIPLLSDAEGRRGFDAHVGERGVK--LSGGQRQRIAIARVL 518
Cdd:CHL00131 88 -LAFQYPieipGVSNADFLRlaynSKRKFQGLpeldplEFLEIINEKLKLVGMDPSFLSRNVNegFSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 519 LKDAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAH--RLSTIARMDRLVVLDKGHIAESGThAEL 588
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD-AEL 238
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
362-580 |
6.11e-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: 80.64 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLES--GRILVDGQDI-AGVTQESLRAQI 438
Cdd:TIGR02633 2 LEMKGIVKTFG-GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLLHR-SIRDNLLYGRPGASDAELME-AVRKARADEFIPLLSdaegrrgFDAHVGERGV-KLSGGQRQRIAIA 515
Cdd:TIGR02633 81 VIIHQELTLVPElSVAENIFLGNEITLPGGRMAyNAMYLRAKNLLRELQ-------LDADNVTRPVgDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 516 RVLLKDAPILILDEATSALDSEVESAIQESLETLMQ-GKTVIAIAHRLSTIARM-DRLVVLDKG-HIA 580
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAVcDTICVIRDGqHVA 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
377-584 |
6.44e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.55 E-value: 6.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVT---QESLRAQ-IGMVTQDTSLLH--- 449
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQkLGFIYQFHHLLPdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 450 --RSIRDNLLYGrpGASDAELMEavrkaRADEFIPLLsdaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILIL 527
Cdd:PRK11629 104 alENVAMPLLIG--KKKPAEINS-----RALEMLAAV-------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 528 DEATSALDSEVESAIQESLETL--MQGKTVIAIAHRLSTIARMDRLVVLDKGHIAESGT 584
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
387-583 |
9.42e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.67 E-value: 9.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 387 PGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDI---AGVTQESLRAQIGMVTQD--TSLLHR-----SIRDNL 456
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDpyASLDPRqtvgdSIMEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 457 LYGRPGASDAelmEAVRKARADEFIPLLSDaegrrgfdaHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDS 536
Cdd:PRK10261 429 RVHGLLPGKA---AAARVAWLLERVGLLPE---------HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598424 537 EVESAIQESLETLMQ--GKTVIAIAHRLSTIARMD-RLVVLDKGHIAESG 583
Cdd:PRK10261 497 SIRGQIINLLLDLQRdfGIAYLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
362-593 |
1.21e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKgSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQdiagvtqesLRaqIGMV 441
Cdd:PRK09544 5 VSLENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQ----DTSLLHRSIRDNLLygRPGASDAELMEAVRKARAdefipllsdaegrrgfdAHVGERGV-KLSGGQRQRIAIAR 516
Cdd:PRK09544 73 PQklylDTTLPLTVNRFLRL--RPGTKKEDILPALKRVQA-----------------GHLIDAPMqKLSGGETQRVLLAR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 517 VLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTI-ARMDRLVVLDkGHIAESGT------HAE 587
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCLN-HHICCSGTpevvslHPE 212
|
....*.
gi 15598424 588 LLAHGG 593
Cdd:PRK09544 213 FISMFG 218
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
363-582 |
2.30e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.18 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFHYgkgSGV--IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIA-GVTQESLRAQIG 439
Cdd:PRK11288 6 SFDGIGKTF---PGVkaLDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQDTSLL-HRSIRDNLLYGRPGASDAELMEAVRKARADEFIpllsdaeGRRGFDAHVGERGVKLSGGQRQRIAIARVL 518
Cdd:PRK11288 83 IIYQELHLVpEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQL-------EHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 519 LKDAPILILDEATSALDS-EVES--AIQESLETlmQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAES 582
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSArEIEQlfRVIRELRA--EGRVILYVSHRMEEIFALcDAITVFKDGRYVAT 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
377-597 |
6.39e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.43 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQ--DIAGVTQESLRAQIGMVTQD--TSLLHRSI 452
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDpeQQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 453 RDNLLYG--RPGASDAELMEavrkaRADEFIPLLsDAEGRRgfdahvgERGVK-LSGGQRQRIAIARVLLKDAPILILDE 529
Cdd:PRK13638 96 DSDIAFSlrNLGVPEAEITR-----RVDEALTLV-DAQHFR-------HQPIQcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 530 ATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAHGGLYAR 597
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEIsDAVYVLRQGQILTHGAPGEVFACTEAMEQ 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
378-588 |
8.07e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 74.64 E-value: 8.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 378 IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLrAQIGMV------------TQDT 445
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVrtfqhvrlfremTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 446 SLL---HRSIRDNLLYG---RPGASDAElMEAV-RKARADEFIPLLSDAEGRRGfdahvgergvKLSGGQRQRIAIARVL 518
Cdd:PRK11300 100 NLLvaqHQQLKTGLFSGllkTPAFRRAE-SEALdRAATWLERVGLLEHANRQAG----------NLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 519 LKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAEL 588
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGIsDRIYVVNQGTPLANGTPEEI 241
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
365-588 |
1.09e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.55 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 365 EHIAFHYGKGSGVIQGLD---LKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLeSGRILVD-----GQDIAGVTQESLR- 435
Cdd:PRK11022 7 DKLSVHFGDESAPFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAEklefnGQDLQRISEKERRn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 436 ---AQIGMVTQD--TSLlhrsirdNLLYgrpgASDAELMEAV-------RKARADEFIPLLS-----DAEGRRGFDAHvg 498
Cdd:PRK11022 86 lvgAEVAMIFQDpmTSL-------NPCY----TVGFQIMEAIkvhqggnKKTRRQRAIDLLNqvgipDPASRLDVYPH-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 499 ergvKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGK--TVIAIAHRLSTIARM-DRLVVLD 575
Cdd:PRK11022 153 ----QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVAEAaHKIIVMY 228
|
250
....*....|...
gi 15598424 576 KGHIAESGTHAEL 588
Cdd:PRK11022 229 AGQVVETGKAHDI 241
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
352-560 |
1.56e-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: 72.39 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 352 AQPLRVERGEVEfehiafhygkgsgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQ 431
Cdd:TIGR01189 3 ARNLACSRGERM-------------LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 432 ESLRAQIGMVTQDTSLLHRSIRDNLLYGRPGASDAELMeavrkaradefiplLSDAEGRRGFDAHVGERGVKLSGGQRQR 511
Cdd:TIGR01189 70 EPHENILYLGHLPGLKPELSALENLHFWAAIHGGAQRT--------------IEDALAAVGLTGFEDLPAAQLSAGQQRR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598424 512 IAIARVLLKDAPILILDEATSALDSEVESAIQESLET-LMQGKTVIAIAH 560
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
374-584 |
2.53e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 76.98 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 374 GSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAgVTQESLRAQIGMVTQDTSLLHR-SI 452
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHlTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 453 RDNLLY-----GRpGASDAEL-MEAvrkaradefipLLSDAegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILI 526
Cdd:TIGR01257 1021 AEHILFyaqlkGR-SWEEAQLeMEA-----------MLEDT----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 527 LDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGT 584
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
385-575 |
3.36e-14 |
|
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: 72.83 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 385 VRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEsLRAQIGMVTQDtsLLHRSIRDnllYGRPGAS 464
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY-IKADYEGTVRD--LLSSITKD---FYTHPYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 465 DAELMEavrkaradefiPLLSDaegrRGFDAHVGErgvkLSGGQRQRIAIARVLLKDAPILILDEATSALDSE----VES 540
Cdd:cd03237 96 KTEIAK-----------PLQIE----QILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASK 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598424 541 AIQESLETlmQGKTVIAIAHRLSTIARM-DRLVVLD 575
Cdd:cd03237 157 VIRRFAEN--NEKTAFVVEHDIIMIDYLaDRLIVFE 190
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
298-563 |
3.58e-14 |
|
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: 75.56 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 298 SVGAIALA-------TGLVIRINNMSGWIMWVVGGIFENiGQVQDGMQTIALPRKVVDREDAQPLRVERGEVEFEHIAFH 370
Cdd:TIGR00954 382 ALGRLMLAgrdmtrlAGFTARVDTLLQVLDDVKSGNFKR-PRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLV 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 371 YGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGqdiagvtqeslRAQIGMVTQDTSLLHR 450
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLG 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 451 SIRDNLLY-------GRPGASDAELMEAVRKARADEfiplLSDAEGrrGFDAhVGERGVKLSGGQRQRIAIARVLLKDAP 523
Cdd:TIGR00954 530 TLRDQIIYpdssedmKRRGLSDKDLEQILDNVQLTH----ILEREG--GWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQ 602
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15598424 524 ILILDEATSALDSEVESAIQESLETLmqGKTVIAIAHRLS 563
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
344-579 |
7.59e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.29 E-value: 7.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 344 RKVVDREDAQPlrVERGEV--EFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILV 421
Cdd:COG3845 240 REVLLRVEKAP--AEPGEVvlEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 422 DGQDIAGVT-QESLRAQIGMVTQDTslLHR------SIRDNLL---YGRPGASDAELMeavRKARADEFipllsdAEGR- 490
Cdd:COG3845 318 DGEDITGLSpRERRRLGVAYIPEDR--LGRglvpdmSVAENLIlgrYRRPPFSRGGFL---DRKAIRAF------AEELi 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 491 -------RGFDAHVGergvKLSGGQRQRIAIARVLLKDAPILILDEATSALDsevESAIQESLETLM----QGKTVIAIA 559
Cdd:COG3845 387 eefdvrtPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD---VGAIEFIHQRLLelrdAGAAVLLIS 459
|
250 260
....*....|....*....|.
gi 15598424 560 HRLSTIARM-DRLVVLDKGHI 579
Cdd:COG3845 460 EDLDEILALsDRIAVMYEGRI 480
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
40-302 |
9.64e-14 |
|
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: 72.20 E-value: 9.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 40 FLALLVVGLIVALIEVALFSYLGRIVDLAqsTPSAEFFRVHAneLIWMAVVALVLRPLFNALHDMLVHQSINpSMTNLIR 119
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV--IPAGDLSLLLW--IALLLLLLALLRALLSYLRRYLAARLGQ-RVVFDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 120 WQNHRYVLKQSLGFFQNDFAGRIAQRIMQTGNSLRDSAVQVVDALWHVLIYTVSALVLFAEADWRLMIPLVLWVFAYVGA 199
Cdd:cd07346 76 RDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 200 LAYFVPQVKRRSVEASDSRSKLMGRIVDGYTNITTLKLFAHTRQEEDYAREAIGDQTLKSQRAGRVVTSMDVTITVMNGV 279
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250 260
....*....|....*....|...
gi 15598424 280 LITGTTGLALWLWSQELISVGAI 302
Cdd:cd07346 236 GTALVLLYGGYLVLQGSLTIGEL 258
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
355-560 |
1.78e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.45 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 355 LRVERGEvefeHIAFHygkgsgviqGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAgvtqesl 434
Cdd:PRK13538 7 LACERDE----RILFS---------GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 435 raqigmvTQDTSLlhrsiRDNLLY-GRPGASDAELMeavrkarADE----FIPLLSDAEGRRGFDA--HVGERGVK---- 503
Cdd:PRK13538 67 -------RQRDEY-----HQDLLYlGHQPGIKTELT-------ALEnlrfYQRLHGPGDDEALWEAlaQVGLAGFEdvpv 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 504 --LSGGQRQRIAIARVLLKDAPILILDEATSALD----SEVESAIQESLEtlmQGKTVIAIAH 560
Cdd:PRK13538 128 rqLSAGQQRRVALARLWLTRAPLWILDEPFTAIDkqgvARLEALLAQHAE---QGGMVILTTH 187
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
378-579 |
3.62e-13 |
|
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: 68.44 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 378 IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLL---LRLYDLESGRILVDGQDIAGvTQESLRAQIGMVTQDTSLLHrsird 454
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKE-FAEKYPGEIIYVSEEDVHFP----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 455 NLLYGrpgasdaELMEAVRKARADEFIpllsdaegrrgfdahvgeRGVklSGGQRQRIAIARVLLKDAPILILDEATSAL 534
Cdd:cd03233 97 TLTVR-------ETLDFALRCKGNEFV------------------RGI--SGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598424 535 DS----EVESAIQESLETLmqGKTVIAIAHRLS--TIARMDRLVVLDKGHI 579
Cdd:cd03233 150 DSstalEILKCIRTMADVL--KTTTFVSLYQASdeIYDLFDKVLVLYEGRQ 198
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
378-590 |
4.80e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.43 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 378 IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAgVTQESLRAQ-IGMVTQD--TSLLHRSiRD 454
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSQrIRMIFQDpsTSLNPRQ-RI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 455 NLLYGRPGASDAELMEAVRKARADEF---IPLLSDaegrrgfdaHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEAT 531
Cdd:PRK15112 107 SQILDFPLRLNTDLEPEQREKQIIETlrqVGLLPD---------HASYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 532 SALDSEVESAIQeSLETLMQGKTVIAIAHRLSTIARM----DRLVVLDKGHIAESGTHAELLA 590
Cdd:PRK15112 178 ASLDMSMRSQLI-NLMLELQEKQGISYIYVTQHLGMMkhisDQVLVMHQGEVVERGSTADVLA 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
347-582 |
5.12e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 347 VDREDAQPLRVER--GEvEFEHIAFHygkgsgviqgldlkVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQ 424
Cdd:PRK15439 261 QQAAGAPVLTVEDltGE-GFRNISLE--------------VRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 425 DIAGV-TQESLRAqiGMV-----TQDTSL-LHRSIRDN---LLYGRPG-----ASDAELMEAVRKARADEFipllsdaeg 489
Cdd:PRK15439 326 EINALsTAQRLAR--GLVylpedRQSSGLyLDAPLAWNvcaLTHNRRGfwikpARENAVLERYRRALNIKF--------- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 490 rrgfdAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARM 568
Cdd:PRK15439 395 -----NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAaQNVAVLFISSDLEEIEQM 469
|
250
....*....|....*
gi 15598424 569 -DRLVVLDKGHIAES 582
Cdd:PRK15439 470 aDRVLVMHQGEISGA 484
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
359-594 |
6.37e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.46 E-value: 6.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 359 RGEVEFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLrlydlesGRILVDgqdiAGVTQESLRAQI 438
Cdd:PRK15064 317 RNALEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-------GELEPD----SGTVKWSENANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSllHRSIRDNLLYgrpgasdaELMEAVRKARADEfiPLLSDAEGRRGFDAHVGERGVK-LSGGQRQRIAIARV 517
Cdd:PRK15064 385 GYYAQDHA--YDFENDLTLF--------DWMSQWRQEGDDE--QAVRGTLGRLLFSQDDIKKSVKvLSGGEKGRMLFGKL 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 518 LLKDAPILILDEATSALDSEVESAIQESLEtLMQGkTVIAIAH-R--LSTIArmDRLV-VLDKGHIAESGTHAELLAHGG 593
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESIESLNMALE-KYEG-TLIFVSHdRefVSSLA--TRIIeITPDGVVDFSGTYEEYLRSQG 528
|
.
gi 15598424 594 L 594
Cdd:PRK15064 529 I 529
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
371-560 |
7.71e-13 |
|
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: 71.12 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 371 YGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVnlllrlydlesgRIL--VDgQDIAGVTQESLRAQIGMVTQDTSL- 447
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLL------------RIMagVD-KDFNGEARPQPGIKVGYLPQEPQLd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 448 LHRSIRDN-------------------LLYGRPGASDAELMEavRKARADEFIpllsDAEgrrgfDAHVGERGV------ 502
Cdd:TIGR03719 81 PTKTVRENveegvaeikdaldrfneisAKYAEPDADFDKLAA--EQAELQEII----DAA-----DAWDLDSQLeiamda 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 503 -----------KLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLmQGkTVIAIAH 560
Cdd:TIGR03719 150 lrcppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
387-568 |
1.03e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 65.86 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 387 PGEKIGLVGPSGAGKSTLVNLLLRLYDLESGR-ILVDGQDIAGVTQESLRAQIgmvtqdtsllhrsirdnllygrpgasd 465
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 466 aelmeavrkaradefipllsdaegrrgfdahVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQES 545
Cdd:smart00382 54 -------------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLL 102
|
170 180 190
....*....|....*....|....*....|
gi 15598424 546 LETLM-------QGKTVIAIAHRLSTIARM 568
Cdd:smart00382 103 EELRLllllkseKNLTVILTTNDEKDLGPA 132
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
363-562 |
1.27e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.61 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 363 EFEHIAFH-YGKGSGVIQGLDLkVRPGEKIGLVGPSGAGKSTLVNLLlrlydleSGRILVD-GQDIAGVT-QESLRAQIG 439
Cdd:PRK13409 74 ELEEEPVHrYGVNGFKLYGLPI-PKEGKVTGILGPNGIGKTTAVKIL-------SGELIPNlGDYEEEPSwDEVLKRFRG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 440 MVTQD--TSLLHRSIRdnllygrpgasdaelmeAVRKARADEFIP---------LLSDAEGRRGFD--------AHVGER 500
Cdd:PRK13409 146 TELQNyfKKLYNGEIK-----------------VVHKPQYVDLIPkvfkgkvreLLKKVDERGKLDevverlglENILDR 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 501 GVK-LSGGQRQRIAIARVLLKDAPILILDEATSALD----SEVESAIQEsletLMQGKTVIAIAHRL 562
Cdd:PRK13409 209 DISeLSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrLNVARLIRE----LAEGKYVLVVEHDL 271
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
355-590 |
1.70e-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: 70.22 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 355 LRVERGEVEFEhiafhygkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLL--LRLYDLESGRIL------------ 420
Cdd:TIGR03269 1 IEVKNLTKKFD--------GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 421 ---------------------VDGQDIAGVTQESLRAQIGMVTQDTSLLH--RSIRDNLLYGRPGASdAELMEAVRkaRA 477
Cdd:TIGR03269 73 erpskvgepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYgdDTVLDNVLEALEEIG-YEGKEAVG--RA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 478 DEFIPLLsdaegrrgfdaHVGER----GVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ-- 551
Cdd:TIGR03269 150 VDLIEMV-----------QLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKas 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15598424 552 GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLA 590
Cdd:TIGR03269 219 GISMVLTSHWPEVIEDLsDKAIWLENGEIKEEGTPDEVVA 258
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
377-577 |
2.48e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.52 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGM---VTQDTSLLHRSir 453
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRkgdFKDAVELLNAV-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 454 dnllygrpGASDAELMeavrkaradefipllsdaegRRGFDAhvgergvkLSGGQRQRIAIARVLLKDAPILILDEATSA 533
Cdd:COG2401 123 --------GLSDAVLW--------------------LRRFKE--------LSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598424 534 LDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM--DRLVVLDKG 577
Cdd:COG2401 167 LDRQTAKRVARNLQKLARraGITLVVATHHYDVIDDLqpDLLIFVGYG 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
385-575 |
3.37e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 385 VRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDgQDIAGVTQESLRAQIGMVtqdtSLLHRSIRDNLlygrpGAS 464
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKPQYIKPDYDGTV----EDLLRSITDDL-----GSS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 465 --DAELMEavrkaradefiPLLSDaegrRGFDAHVGErgvkLSGGQRQRIAIARVLLKDAPILILDEATSALDSE----V 538
Cdd:PRK13409 432 yyKSEIIK-----------PLQLE----RLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaV 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598424 539 ESAIQESLETlmQGKTVIAIAHRLSTIARM-DRLVVLD 575
Cdd:PRK13409 493 AKAIRRIAEE--REATALVVDHDIYMIDYIsDRLMVFE 528
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
367-584 |
3.48e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 367 IAFHYGKGS-GVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQ----------DIAGVTQESLR 435
Cdd:PRK10261 20 IAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 436 ----AQIGMVTQD--TSL---------LHRSIRDNllygrPGASDAELMEAVRKARADEFIPllsDAEGRRGFDAHvger 500
Cdd:PRK10261 100 hvrgADMAMIFQEpmTSLnpvftvgeqIAESIRLH-----QGASREEAMVEAKRMLDQVRIP---EAQTILSRYPH---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 501 gvKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQGKT--VIAIAHRLSTIARM-DRLVVLDKG 577
Cdd:PRK10261 168 --QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIaDRVLVMYQG 245
|
....*..
gi 15598424 578 HIAESGT 584
Cdd:PRK10261 246 EAVETGS 252
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
376-582 |
4.34e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 68.66 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 376 GV--IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLES--GRILVDGQ-----DIAgvtqESLRAQIGMVTQDTS 446
Cdd:NF040905 13 GVkaLDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIR----DSEALGIVIIHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 447 LL-HRSIRDNLLYG----RPGASDAElmEAVRKARAdefipLLSdaegRRGFDAH----VGERGVklsgGQRQRIAIARV 517
Cdd:NF040905 89 LIpYLSIAENIFLGneraKRGVIDWN--ETNRRARE-----LLA----KVGLDESpdtlVTDIGV----GKQQLVEIAKA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598424 518 LLKDAPILILDEATSALdSEVESaiqESLETLM-----QGKTVIAIAHRLSTIARM-DRLVVLDKGHIAES 582
Cdd:NF040905 154 LSKDVKLLILDEPTAAL-NEEDS---AALLDLLlelkaQGITSIIISHKLNEIRRVaDSITVLRDGRTIET 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
350-590 |
4.55e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 350 EDAQP-LRVERGEV--EFEHIAfhygkGSGViQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDI 426
Cdd:PRK10762 243 EDQYPrLDKAPGEVrlKVDNLS-----GPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 427 AGVT-QESLRAQIGMVTQDTS----LLHRSIRDNL-------LYGRPGASD-AELMEAVrkaraDEFIPLLSDAEGRRgf 493
Cdd:PRK10762 317 VTRSpQDGLANGIVYISEDRKrdglVLGMSVKENMsltalryFSRAGGSLKhADEQQAV-----SDFIRLFNIKTPSM-- 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 494 DAHVGergvKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ-GKTVIAIAHRLSTIARM-DRL 571
Cdd:PRK10762 390 EQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGMsDRI 465
|
250 260
....*....|....*....|....
gi 15598424 572 VVLDKGHI-----AESGTHAELLA 590
Cdd:PRK10762 466 LVMHEGRIsgeftREQATQEKLMA 489
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
385-577 |
4.62e-12 |
|
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: 65.34 E-value: 4.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 385 VRPGEKIGLVGPSGAGKSTLVNLL-LRLYD-LESGRILVDGQDIagvtQESLRAQIGMVTQdtsllhrsirdnllygrpg 462
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPL----DKNFQRSTGYVEQ------------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 463 asdaelmeavrkarADEFIPLLSDAEGRRgFDAHVgeRGvkLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAI 542
Cdd:cd03232 87 --------------QDVHSPNLTVREALR-FSALL--RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598424 543 QESLETL-MQGKTVIAIAHRLS--TIARMDRLVVLDKG 577
Cdd:cd03232 148 VRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
371-583 |
7.28e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.06 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 371 YGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHR 450
Cdd:PRK15056 16 WRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 451 SIRDNLLYGRPGAsdaelMEAVRKARADEFiPLLSDAEGRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEA 530
Cdd:PRK15056 96 LVEDVVMMGRYGH-----MGWLRRAKKRDR-QIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598424 531 TSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARMDRLVVLDKGHIAESG 583
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
351-583 |
8.11e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.72 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 351 DAQPLRVERGevefehIAFHYGKGSGvIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQ-----D 425
Cdd:PRK11701 2 MDQPLLSVRG------LTKLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 426 IAGVTQES----LRAQIGMVTQDTsllhrsiRDNLL--------------------YGRPGASDAELMEAVR--KARADE 479
Cdd:PRK11701 75 LYALSEAErrrlLRTEWGFVHQHP-------RDGLRmqvsaggnigerlmavgarhYGDIRATAGDWLERVEidAARIDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 480 FiPllsdaegrRGFdahvgergvklSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLM--QGKTVIA 557
Cdd:PRK11701 148 L-P--------TTF-----------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVreLGLAVVI 207
|
250 260
....*....|....*....|....*...
gi 15598424 558 IAHRLStIARM--DRLVVLDKGHIAESG 583
Cdd:PRK11701 208 VTHDLA-VARLlaHRLLVMKQGRVVESG 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
384-575 |
8.13e-12 |
|
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: 67.89 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 384 KVRPGEKIGLVGPSGAGKSTLVNLLlrlydleSGRILVDGQDIAGVTQESLRAQigMVTQDtsllhrsirdnllygrpga 463
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVDEDLKISYKPQ--YISPD------------------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 464 SDAELMEAVRKARADEF----------IPLLSDaegrRGFDAHVGErgvkLSGGQRQRIAIARVLLKDAPILILDEATSA 533
Cdd:COG1245 414 YDGTVEEFLRSANTDDFgssyykteiiKPLGLE----KLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598424 534 LDSE----VESAIQESLETlmQGKTVIAIAHRLSTIARM-DRLVVLD 575
Cdd:COG1245 486 LDVEqrlaVAKAIRRFAEN--RGKTAMVVDHDIYLIDYIsDRLMVFE 530
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
373-586 |
1.54e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.81 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 373 KGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLL--RLYDLESGRILVDGQDIAGVTQESlRAQIG--MVTQDTSLL 448
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGifMAFQYPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 449 hrsirdnllygrPGASDAELME----AVRKARADE------FIPLLSDAEGRRGFDAHVGERGVKL--SGGQRQRIAIAR 516
Cdd:PRK09580 91 ------------PGVSNQFFLQtalnAVRSYRGQEpldrfdFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 517 VLLKDAPILILDEATSALDSEVESAIQESLETLMQGK-TVIAIAH--RLSTIARMDRLVVLDKGHIAESGTHA 586
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKrSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFT 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
365-564 |
1.57e-11 |
|
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: 67.12 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 365 EHIAFHYGKGSGVIQGLDLkVRPGEKIGLVGPSGAGKSTLVNLLlrlydleSGRI---LVDGQDIAGvTQESLRAQIGMV 441
Cdd:COG1245 77 EDPVHRYGENGFRLYGLPV-PKKGKVTGILGPNGIGKSTALKIL-------SGELkpnLGDYDEEPS-WDEVLKRFRGTE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQD--TSLLHRSIR--------DNL---LYGRPGasdaELMEAV-RKARADEFIPLLSDAegrrgfdaHVGERGVK-LSG 506
Cdd:COG1245 148 LQDyfKKLANGEIKvahkpqyvDLIpkvFKGTVR----ELLEKVdERGKLDELAEKLGLE--------NILDRDISeLSG 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598424 507 GQRQRIAIARVLLKDAPILILDEATSALD----SEVESAIQESLEtlmQGKTVIAIAHRLST 564
Cdd:COG1245 216 GELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELAE---EGKYVLVVEHDLAI 274
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
40-291 |
2.50e-11 |
|
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: 64.59 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 40 FLALLVVGLIVALIEVALFSYLGRIVDLAQSTPSAEFFRVHANELIWMAVVALVLrpLFNALHDMLVHQsINPSMTNLIR 119
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQF--ILSFLQSYLLNH-TGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 120 WQNHRYVLKQSLGFFQNDFAGRIAQRIMQTGNSLRDSAVQVVDALWHVLIYTVSALVLFAEADWRLMIPLVLWVFAYVGA 199
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 200 LAYFVPQVKRRSVEASDSRSKLMGRIVDGYTNITTLKLFAHtrqeEDYAREAIGDQTLKSQRAGRVVTSMDVTITVMNGV 279
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGR----EEYELEKYDKALEEALKAGIKKAVANGLSFGITQF 233
|
250
....*....|..
gi 15598424 280 LITGTTGLALWL 291
Cdd:pfam00664 234 IGYLSYALALWF 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
373-587 |
1.29e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 373 KGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIA-GVTQESLRAQIGMVTQDTS----L 447
Cdd:PRK11288 264 KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLCPEDRKaegiI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 448 LHRSIRDNL-LYGRPGASDAELMEAVRKAR--ADEFIPLLS----DAEGRRGFdahvgergvkLSGGQRQRIAIARVLLK 520
Cdd:PRK11288 344 PVHSVADNInISARRHHLRAGCLINNRWEAenADRFIRSLNiktpSREQLIMN----------LSGGNQQKAILGRWLSE 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRL-STIARMDRLVVLDKGHIAESGTHAE 587
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAKHEIYNVIYELAaQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
387-560 |
1.29e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.98 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 387 PGEKIGLVGPSGAGKSTLVnlllrlydlesgRIL--VDgQDIAGVTQESLRAQIGMVTQDTSL-LHRSIRDNL------- 456
Cdd:PRK11819 32 PGAKIGVLGLNGAGKSTLL------------RIMagVD-KEFEGEARPAPGIKVGYLPQEPQLdPEKTVRENVeegvaev 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 457 ------------LYGRPGASDAELMEavRKARADEFIpllsDAEgrrgfDAHVGERGV-----------------KLSGG 507
Cdd:PRK11819 99 kaaldrfneiyaAYAEPDADFDALAA--EQGELQEII----DAA-----DAWDLDSQLeiamdalrcppwdakvtKLSGG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598424 508 QRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLmQGkTVIAIAH 560
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY-PG-TVVAVTH 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
372-581 |
1.95e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 372 GKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQ-ESLRAQIGMVTQ---DTSL 447
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrDNGF 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 448 LHR-SIRDNLLYGRpgasdaelmeAVRKARADEFIPLLSDAEGRRGFDAHVGERGVK----------LSGGQRQRIAIAR 516
Cdd:PRK09700 353 FPNfSIAQNMAISR----------SLKDGGYKGAMGLFHEVDEQRTAENQRELLALKchsvnqniteLSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 517 VLLKDAPILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTI-ARMDRLVVLDKGHIAE 581
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIiTVCDRIAVFCEGRLTQ 489
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
359-588 |
2.19e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.45 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 359 RGEVEFEHIAFHYGKGSGViQGLDLKVRPGEKIGLVGPSGAGKSTLVnLLLRLYDLESGRILVDGQDIAGvTQESLRAQI 438
Cdd:NF000106 11 RNAVEVRGLVKHFGEVKAV-DGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCA-NRRALRRTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMvtqdtsllHRSIR----------DNL-LYGRPgasdAELMEAVRKARADEFIPLLSDAEGrrgfdahVGERGVKLSGG 507
Cdd:NF000106 88 G*--------HRPVR*grresfsgrENLyMIGR*----LDLSRKDARARADELLERFSLTEA-------AGRAAAKYSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 508 QRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ-GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTH 585
Cdd:NF000106 149 MRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQLaHELTVIDRGRVIADGKV 228
|
...
gi 15598424 586 AEL 588
Cdd:NF000106 229 DEL 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
388-560 |
2.52e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 388 GEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQ-DIAGVTQeslraqigmvtqdtsllHRSIRDnllygrpgaSDA 466
Cdd:PRK11147 345 GDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQ-----------------HRAELD---------PEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 467 ELMEAVrkaradefipllsdAEGRR-----GFDAHV----------GERG---VK-LSGGQRQRIAIARVLLKDAPILIL 527
Cdd:PRK11147 399 TVMDNL--------------AEGKQevmvnGRPRHVlgylqdflfhPKRAmtpVKaLSGGERNRLLLARLFLKPSNLLIL 464
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598424 528 DEATSALDSEVesaiQESLETLM---QGkTVIAIAH 560
Cdd:PRK11147 465 DEPTNDLDVET----LELLEELLdsyQG-TVLLVSH 495
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
377-589 |
2.69e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRlyDLE----------SGRILVDGQDIAGVTQESL---RAQIGMVTQ 443
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTgggaprgarvTGDVTLNGEPLAAIDAPRLarlRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 444 DTSLLhrSIRDNLLYGR-PGASDAELMeavrkARADEFIplLSDAEGRRGFDAHVGERGVKLSGGQRQRIAIARVLLK-- 520
Cdd:PRK13547 94 PAFAF--SAREIVLLGRyPHARRAGAL-----THRDGEI--AWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 521 -------DAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIAR-MDRLVVLDKGHIAESGTHAELL 589
Cdd:PRK13547 165 pphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVL 243
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
362-593 |
3.60e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKgSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAgvtQESLRAQIGmv 441
Cdd:NF033858 2 ARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA---DARHRRAVC-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 tqdtsllHR----------------SIRDNL-----LYGRPGASdaelmeavRKARADEfiplLSDAEGRRGF-DAHVGe 499
Cdd:NF033858 76 -------PRiaympqglgknlyptlSVFENLdffgrLFGQDAAE--------RRRRIDE----LLRATGLAPFaDRPAG- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 500 rgvKLSGGQRQRIAIARVLLKDAPILILDEATSALDS-------EVESAIQESletlMQGKTVIaiahrLST-----IAR 567
Cdd:NF033858 136 ---KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDRIRAE----RPGMSVL-----VATaymeeAER 203
|
250 260
....*....|....*....|....*.
gi 15598424 568 MDRLVVLDKGHIAESGTHAELLAHGG 593
Cdd:NF033858 204 FDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
362-564 |
4.44e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 62.26 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVdgqdiaGVTqeslrAQIGMV 441
Cdd:TIGR03719 323 IEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GET-----VKLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQdtsllhrsIRDNLlygrpgASDAELMEAVRKArADEFipLLSDAE-------GRRGFDAHVGERGVK-LSGGQRQRIA 513
Cdd:TIGR03719 391 DQ--------SRDAL------DPNKTVWEEISGG-LDII--KLGKREipsrayvGRFNFKGSDQQKKVGqLSGGERNRVH 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 514 IARVLLKDAPILILDEATSALDSEVESAIQESLETLmqGKTVIAIAH------RLST 564
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
381-537 |
5.30e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 381 LDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAgvTQESLR-----AQIGMVTQDTSLLHRSIRDN 455
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT--RGDRSRfmaylGHLPGLKADLSTLENLHFLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 456 LLYGRpgasdaelmeavrkaRADEfipLLSDAEGRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALD 535
Cdd:PRK13543 108 GLHGR---------------RAKQ---MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
..
gi 15598424 536 SE 537
Cdd:PRK13543 170 LE 171
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
372-584 |
6.81e-10 |
|
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: 62.34 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 372 GKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQEsLRAQIGMVTQDTSLlhrs 451
Cdd:TIGR01257 1949 GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD-VHQNMGYCPQFDAI---- 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 452 irDNLLYGRpgaSDAELMEAVRKARADEFIPLLSDAEGRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEAT 531
Cdd:TIGR01257 2024 --DDLLTGR---EHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPT 2098
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598424 532 SALDSEVESAIQESLETLM-QGKTVIAIAHRLSTI-ARMDRLVVLDKGHIAESGT 584
Cdd:TIGR01257 2099 TGMDPQARRMLWNTIVSIIrEGRAVVLTSHSMEECeALCTRLAIMVKGAFQCLGT 2153
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
382-579 |
8.67e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 8.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 382 DLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDgQD--IAGVTQESLRAQIGMV---------------TQD 444
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDliVARLQQDPPRNVEGTVydfvaegieeqaeylKRY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 445 TSLLHRSIRD----NLlygrpgASDAELMEAVRKARADEFIPLLSDAEGRRGFDAHvgERGVKLSGGQRQRIAIARVLLK 520
Cdd:PRK11147 102 HDISHLVETDpsekNL------NELAKLQEQLDHHNLWQLENRINEVLAQLGLDPD--AALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598424 521 DAPILILDEATSALDSEvesAIqESLETLM---QGkTVIAIAHRLSTIARM-DRLVVLDKGHI 579
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIE---TI-EWLEGFLktfQG-SIIFISHDRSFIRNMaTRIVDLDRGKL 231
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
381-589 |
3.03e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.02 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 381 LDLKVRPGEKIGLVGPSGAGKSTlvnLLLRLYDL--ESGRILVDGQDIAGVTQESLRAQIGMVTQDTS-----------L 447
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTppfampvfqylT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 448 LHRSIRdnllyGRPGASDAELMEAVRKARadefiplLSDAEGRrgfdaHVGErgvkLSGGQRQRIAIARVLLKDAP---- 523
Cdd:PRK03695 92 LHQPDK-----TRTEAVASALNEVAEALG-------LDDKLGR-----SVNQ----LSGGEWQRVRLAAVVLQVWPdinp 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598424 524 ---ILILDEATSALDSEVESAIQESLETL-MQGKTVIAIAHRLS-TIARMDRLVVLDKGHIAESGTHAELL 589
Cdd:PRK03695 151 agqLLLLDEPMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
364-569 |
3.57e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 364 FEHIAFHYGKGsgviqGLdlkvrpgekIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGvTQESLRAQIGMVTQ 443
Cdd:PRK13540 17 LQQISFHLPAG-----GL---------LHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 444 DTSL-LHRSIRDNLLYGRPGASDA-ELMEAVRKARADEFIpllsdaegrrgfDAHVGergvKLSGGQRQRIAIARVLLKD 521
Cdd:PRK13540 82 RSGInPYLTLRENCLYDIHFSPGAvGITELCRLFSLEHLI------------DYPCG----LLSSGQKRQVALLRLWMSK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598424 522 APILILDEATSALDS-EVESAIQESLETLMQGKTVIAIAHRLSTIARMD 569
Cdd:PRK13540 146 AKLWLLDEPLVALDElSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
371-563 |
7.90e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.99 E-value: 7.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 371 YGKGSGVIQGLDLkVRPGEKIGLVGPSGAGKSTLVNLL-------LRLYDLESgrilvDGQDIagvtqesLRAQIGMVTQ 443
Cdd:cd03236 10 YGPNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILagklkpnLGKFDDPP-----DWDEI-------LDEFRGSELQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 444 D--TSLLHRSIR--------DNLlygrPGASDAELMEAVRKARADEFIPLLSDAEGRRgfdaHVGERGV-KLSGGQRQRI 512
Cdd:cd03236 77 NyfTKLLEGDVKvivkpqyvDLI----PKAVKGKVGELLKKKDERGKLDELVDQLELR----HVLDRNIdQLSGGELQRV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598424 513 AIARVLLKDAPILILDEATSALDS----EVESAIQESLEtlmQGKTVIAIAHRLS 563
Cdd:cd03236 149 AIAAALARDADFYFFDEPSSYLDIkqrlNAARLIRELAE---DDNYVLVVEHDLA 200
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
377-535 |
1.30e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLL-----------LRLYdlesGRilvdgQDIAGVTQESLRAQIGMVTQDT 445
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndLTLF----GR-----RRGSGETIWDIKKHIGYVSSSL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 446 SLLHR---SIRDNLLYG-------RPGASDAElmeavrKARADEFIPLLsdaegrrGFDAHVGERGVK-LSGGQrQRIA- 513
Cdd:PRK10938 346 HLDYRvstSVRNVILSGffdsigiYQAVSDRQ------QKLAQQWLDIL-------GIDKRTADAPFHsLSWGQ-QRLAl 411
|
170 180
....*....|....*....|..
gi 15598424 514 IARVLLKDAPILILDEATSALD 535
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
362-547 |
2.23e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGkGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVdgqdiaGVTqeslrAQIGMV 441
Cdd:PRK11819 325 IEAENLSKSFG-DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GET-----VKLAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQDtsllhrsiRDNLlygrpgASDAELMEAVrkARADEFIpLLSDAE-------GRRGFDA-----HVGErgvkLSGGQR 509
Cdd:PRK11819 393 DQS--------RDAL------DPNKTVWEEI--SGGLDII-KVGNREipsrayvGRFNFKGgdqqkKVGV----LSGGER 451
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598424 510 QRIAIARVLLKDAPILILDEATSALDSEVESAIQESLE 547
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
385-579 |
3.51e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.37 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 385 VRPGEKIGLVGPSGAGKSTLVNLLLRLYDLE-SGRILVDGQDIAGVT-QESLRAQIGMVTQDTSllhrsiRDNLLygrpg 462
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRK------RHGIV----- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 463 aSDAELMEAVRKARADEF--IPLLSDAEGRRGFDAHVGERGVK----------LSGGQRQRIAIARVLLKDAPILILDEA 530
Cdd:TIGR02633 352 -PILGVGKNITLSVLKSFcfKMRIDAAAELQIIGSAIQRLKVKtaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598424 531 TSALDSEVESAIQESLETLMQ-GKTVIAIAHRLSTIARM-DRLVVLDKGHI 579
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQeGVAIIVVSSELAEVLGLsDRVLVIGEGKL 481
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
388-590 |
6.07e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.81 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 388 GEKIGLVGPSGAGKSTLvnlllrlydlesgrilvdGQDIAGVTQESLRAQIG-MVTQDTSLLHRSIRD---------NLL 457
Cdd:PRK15093 33 GEIRGLVGESGSGKSLI------------------AKAICGVTKDNWRVTADrMRFDDIDLLRLSPRErrklvghnvSMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 458 YGRPGAS-------DAELMEAV---------------RKARAdefIPLLSdaegRRGFDAH---VGERGVKLSGGQRQRI 512
Cdd:PRK15093 95 FQEPQSCldpservGRQLMQNIpgwtykgrwwqrfgwRKRRA---IELLH----RVGIKDHkdaMRSFPYELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 513 AIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELL 589
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQWaDKINVLYCGQTVETAPSKELV 247
|
.
gi 15598424 590 A 590
Cdd:PRK15093 248 T 248
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
377-579 |
6.95e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.18 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 377 VIQGLDLKVRPGEKIGLVGPSGAGKSTL-VNLLLRLYDL-ESGRILVDGQDIAGVT-QESLRAQIGMVTQDTS----LLH 449
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRnISGTVFKDGKEVDVSTvSDAIDAGLAYVTEDRKgyglNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 450 RSIRDNL-LYGRPGASDAELMEAVRKAR-ADEFipllsdaegRRGFD---AHVGERGVKLSGGQRQRIAIARVLLKDAPI 524
Cdd:NF040905 355 DDIKRNItLANLGKVSRRGVIDENEEIKvAEEY---------RKKMNiktPSVFQKVGNLSGGNQQKVVLSKWLFTDPDV 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 525 LILDEATSALDS----EVESAIQESLEtlmQGKTVIAIAHRLSTIARM-DRLVVLDKGHI 579
Cdd:NF040905 426 LILDEPTRGIDVgakyEIYTIINELAA---EGKGVIVISSELPELLGMcDRIYVMNEGRI 482
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
48-337 |
1.01e-07 |
|
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: 53.72 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 48 LIVALIEVALFSYLGRIVDLAQSTPSAEFFrvhaNELIWMAVVALVLRPLFNALHDMLVhQSINPSMTNLIRWQNHRYVL 127
Cdd:cd18557 6 LISSAAQLLLPYLIGRLIDTIIKGGDLDVL----NELALILLAIYLLQSVFTFVRYYLF-NIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 128 KQSLGFFQNDFAGRIAQRIMQTGNSLRDSA-VQVVDALWHVLIYTVSALVLFAEAdWRLMIPLVLWVFAYVGALAYFVPQ 206
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVtDNLSQLLRNILQVIGGLIILFILS-WKLTLVLLLVIPLLLIASKIYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 207 VKRRSVEASDSRSKLMGRIVDGYTNITTLKLFAHTRQEEDYAREAIGDQTLKSQRAGRVVTSMDVTITVMNGVLITGTTG 286
Cdd:cd18557 160 IRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15598424 287 LALWLWSQELISVGAIA---LATGLVIRinnmsgwimwVVGGIFENIGQVQDGM 337
Cdd:cd18557 240 YGGYLVLSGQLTVGELTsfiLYTIMVAS----------SVGGLSSLLADIMKAL 283
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
362-587 |
1.24e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSGVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLlrlydleSGRIlvdgQDIAGVTQESLRAQIGMV 441
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLI-------SGEL----QPSSGTVFRSAKVRMAVF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 442 TQ------DTSllhrsiRDNLLYGR---PGASDAELMeavrkaradefipllsdaegrrgfdAHVGERGVK--------- 503
Cdd:PLN03073 578 SQhhvdglDLS------SNPLLYMMrcfPGVPEQKLR-------------------------AHLGSFGVTgnlalqpmy 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 504 -LSGGQRQRIAIARVLLKDAPILILDEATSALDSE-VESAIQESLetLMQGKtVIAIAHRLSTIA-RMDRLVVLDKGHIA 580
Cdd:PLN03073 627 tLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDaVEALIQGLV--LFQGG-VLMVSHDEHLISgSVDELWVVSEGKVT 703
|
....*...
gi 15598424 581 E-SGTHAE 587
Cdd:PLN03073 704 PfHGTFHD 711
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
384-592 |
1.54e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 384 KVRPGEKIGLVGPSGAGKSTLVNLLLRLYD-LESGRILVDGQDIAGVT-QESLRAQIGMVTQDTS----LLHRSIRDNLL 457
Cdd:PRK13549 284 SLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNpQQAIAQGIAMVPEDRKrdgiVPVMGVGKNIT 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 458 ------YGRPGASD--AELM---EAVRKARADEFIPLLSDAegrrgfdahvgergvKLSGGQRQRIAIARVLLKDAPILI 526
Cdd:PRK13549 364 laaldrFTGGSRIDdaAELKtilESIQRLKVKTASPELAIA---------------RLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 527 LDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARM-DRLVVLDKGHIAesgthAELLAHG 592
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQLVqQGVAIIVISSELPEVLGLsDRVLVMHEGKLK-----GDLINHN 491
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
369-591 |
1.84e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 369 FHYGkgsgvIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLllrlydlesgrilvdgqdIAGVTQESlRAQIGMVTQDTSLL 448
Cdd:PRK13545 36 YHYA-----LNNISFEVPEGEIVGIIGLNGSGKSTLSNL------------------IAGVTMPN-KGTVDIKGSAALIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 449 HRSIRDNLLYGRPGASDAELMEAVRKARADEFIPLLSDAegrrgfdAHVGE---RGVK-LSGGQRQRIAIARVLLKDAPI 524
Cdd:PRK13545 92 ISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEF-------ADIGKfiyQPVKtYSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 525 LILDEATSALDSEVESAIQESL-ETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIAESGTHAELLAH 591
Cdd:PRK13545 165 LVIDEALSVGDQTFTKKCLDKMnEFKEQGKTIFFISHSLSQVKSFcTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
365-546 |
2.62e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 365 EHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRI-LVDGQDIAGVTQ---ESLRAqigm 440
Cdd:PRK10636 316 EKVSAGYGDRI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQhqlEFLRA---- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 441 vtqDTSLLHRSIRdnllygrpgASDAELMEAVRkaradefipllsDAEGRRGFDA-HVGERGVKLSGGQRQRIAIARVLL 519
Cdd:PRK10636 391 ---DESPLQHLAR---------LAPQELEQKLR------------DYLGGFGFQGdKVTEETRRFSGGEKARLVLALIVW 446
|
170 180
....*....|....*....|....*..
gi 15598424 520 KDAPILILDEATSALDSEVESAIQESL 546
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
502-575 |
2.75e-07 |
|
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: 51.03 E-value: 2.75e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 502 VKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVESAIQESLETLMQ--GKTVIAIAHRLSTIARM-DRLVVLD 575
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLsDRIHVFE 146
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
386-577 |
3.42e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.70 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 386 RPGEKIGLVGPSGAGKSTLVNLLlrlydleSGRI---LVDGQ-DIAGVT--QESLRAQIGMVTQ-DTSLLHRSIRDNLLY 458
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVL-------AGRKtggYIEGDiRISGFPkkQETFARISGYCEQnDIHSPQVTVRESLIY 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 459 GRPGASDAELMEAVRKARADEFIPLLSDAEGRrgfDAHVGERGVK-LSGGQRQRIAIARVLLKDAPILILDEATSALDSE 537
Cdd:PLN03140 977 SAFLRLPKEVSKEEKMMFVDEVMELVELDNLK---DAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDAR 1053
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598424 538 VESAIQESLE-TLMQGKTVIAIAHRLS--TIARMDRLVVLDKG 577
Cdd:PLN03140 1054 AAAIVMRTVRnTVDTGRTVVCTIHQPSidIFEAFDELLLMKRG 1096
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
502-578 |
3.55e-07 |
|
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: 50.44 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 502 VKLSGGQRQRIAIARVL----LKDAPILILDEATSALDSEVESAIQESL-ETLMQGKTVIAIAHRLSTIARMDRLVVLDK 576
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAIlEHLVKGAQVIVITHLPELAELADKLIHIKK 155
|
..
gi 15598424 577 GH 578
Cdd:cd03227 156 VI 157
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
504-583 |
5.73e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.01 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 504 LSGGQRQRIAIARVLLKDAP--ILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARMDRLVVLDK---- 576
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPgsgk 167
|
....*....
gi 15598424 577 --GHIAESG 583
Cdd:cd03238 168 sgGKVVFSG 176
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
385-579 |
7.19e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 385 VRPGEKIGLVGPSGAGKSTLvnLLLRLYDLESGRILVDGQdIA--GVTQESLRAQI-GMVT----QDTSLLHRSIRDNLL 457
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTL--LKTIASNTDGFHIGVEGV-ITydGITPEEIKKHYrGDVVynaeTDVHFPHLTVGETLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 458 YgrpgasdAELMEAV--------RKARADEFIPLLSDAEG-RRGFDAHVGE---RGVklSGGQRQRIAIARVLLKDAPIL 525
Cdd:TIGR00956 161 F-------AARCKTPqnrpdgvsREEYAKHIADVYMATYGlSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 526 ILDEATSALDS----EVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVLDKGHI 579
Cdd:TIGR00956 232 CWDNATRGLDSatalEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQ 289
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
382-598 |
2.33e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 382 DLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESLRAQIGMVTQD--TSLLHRSIRDnllYG 459
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRnnTDMLSPGEDD---TG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 460 RPgASDAELMEAVRKARADEFIPLLsdaegrrGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILDEATSALDSEVE 539
Cdd:PRK10938 100 RT-TAEIIQDEVKDPARCEQLAQQF-------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598424 540 SAIQESLETLMQGK-TVIAIAHRLSTI-ARMDRLVVLDKGHIAESGTHAELLAHgGLYARL 598
Cdd:PRK10938 172 QQLAELLASLHQSGiTLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQQ-ALVAQL 231
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
393-569 |
3.40e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.99 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 393 LVGPSGAGKSTLVN-LLLRLY-DLESGRILVDGQ-DIAGVTQEslRAQIGM----VTQDTSLLHRSIR--DNLLYGRPGA 463
Cdd:cd03240 27 IVGQNGAGKTTIIEaLKYALTgELPPNSKGGAHDpKLIREGEV--RAQVKLafenANGKKYTITRSLAilENVIFCHQGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 464 SDAELMEavrkaradefipllsdaegrrgfdahvgERGvKLSGGQRQ------RIAIARVLLKDAPILILDEATSALDSE 537
Cdd:cd03240 105 SNWPLLD----------------------------MRG-RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEE 155
|
170 180 190
....*....|....*....|....*....|....*
gi 15598424 538 -VESAIQESLETLMQGKT--VIAIAHRLSTIARMD 569
Cdd:cd03240 156 nIEESLAEIIEERKSQKNfqLIVITHDEELVDAAD 190
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
378-584 |
3.63e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 48.76 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 378 IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLrlYDLESGRILVDGQDIAGVTQESLRAQIGMVTQ-DTSLLHRSIRDNL 456
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTL--YPALARRLHLKKEQPGNHDRIEGLEHIDKVIViDQSPIGRTPRSNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 457 L---------------------YGRP-------GASDAELME-AVRKARadEF---IP-------LLSDAegrrGFD-AH 496
Cdd:cd03271 89 AtytgvfdeirelfcevckgkrYNREtlevrykGKSIADVLDmTVEEAL--EFfenIPkiarklqTLCDV----GLGyIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 497 VGERGVKLSGGQRQRIAIARVLLKDAP---ILILDEATSALDSEVESAIQESLETLM-QGKTVIAIAHRLSTIARMDRLV 572
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKCADWII 242
|
250
....*....|....*...
gi 15598424 573 VL-----DK-GHIAESGT 584
Cdd:cd03271 243 DLgpeggDGgGQVVASGT 260
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
385-535 |
7.23e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 385 VRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQ-DIAGVTQESL---RAQIGMVTQ--------DTSLLHRSI 452
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPalpQPALEYVIDgdreyrqlEAQLHDANE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 453 RDN-----LLYGRPGASDAELMeavrKARADEFIPLLsdaegrrGFDAHVGERGVK-LSGGQRQRIAIARVLLKDAPILI 526
Cdd:PRK10636 104 RNDghaiaTIHGKLDAIDAWTI----RSRAASLLHGL-------GFSNEQLERPVSdFSGGWRMRLNLAQALICRSDLLL 172
|
....*....
gi 15598424 527 LDEATSALD 535
Cdd:PRK10636 173 LDEPTNHLD 181
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
362-529 |
7.95e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.84 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 362 VEFEHIAFHYGKGSgVIQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVTQESL---RAQI 438
Cdd:PRK11831 8 VDMRGVSFTRGNRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 439 GMVTQDTSLL-HRSIRDNLLYgrPGASDAELMEAVRKARadefIPLLSDAEGRRGfDAHVgeRGVKLSGGQRQRIAIARV 517
Cdd:PRK11831 87 SMLFQSGALFtDMNVFDNVAY--PLREHTQLPAPLLHST----VMMKLEAVGLRG-AAKL--MPSELSGGMARRAALARA 157
|
170
....*....|..
gi 15598424 518 LLKDAPILILDE 529
Cdd:PRK11831 158 IALEPDLIMFDE 169
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
40-301 |
1.01e-05 |
|
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: 47.80 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 40 FLALLVVGLIVALIEVALFSYLGRIVDLAQSTPSAEFFRVhaneLIWMAVVALVLRPLFNALHDMLVhQSINPSMTNLIR 119
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLL----VPLAIIGLFLLRGLASYLQTYLM-AYVGQRVVRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 120 WQNHRYVLKQSLGFFQNDFAGRIAQRIMQTGNSLRDSAVQVVDALW----HVLIYTVSALVLfaeaDWRL------MIPL 189
Cdd:cd18552 76 NDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVrdplTVIGLLGVLFYL----DWKLtlialvVLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 190 VLWVFAYVGAlayfvpQVKRRSVEASDSRSKLMGRIVDGYTNITTLKLFAHTRQEEDYAREAIGD---QTLKSQRAGRVV 266
Cdd:cd18552 152 AALPIRRIGK------RLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERlrrLSMKIARARALS 225
|
250 260 270
....*....|....*....|....*....|....*
gi 15598424 267 TSMdvtITVMNGVLITGTTGLALWLWSQELISVGA 301
Cdd:cd18552 226 SPL---MELLGAIAIALVLWYGGYQVISGELTPGE 257
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
41-320 |
1.27e-05 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. 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: 350006 [Multi-domain] Cd Length: 289 Bit Score: 47.24 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 41 LALLVVGLIVALIEVALFSYLGRIVDLAQSTPSAefFRVHAnelIWMAV-VALVLRPLFNALH-DMLVHQSINPSMTnli 118
Cdd:cd18562 2 LGLALANVALAGVQFAEPVLFGRVVDALSSGGDA--FPLLA---LWAALgLFSILAGVLVALLaDRLAHRRRLAVMA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 119 rwQNHRYVLKQSLGFFQNDFAGRIAqRIMQTGnslrdsavqvVDALWHV--------LIYTVSALVLFAEA---DWRLMI 187
Cdd:cd18562 74 --SYFEHVITLPLSFHSQRGSGRLL-RIMLRG----------TDALFGLwlgffrehLAALVSLIVLLPVAlwmNWRLAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 188 PLVLWVFAYVGALAYFVPQVKRRSVEASDSRSKLMGRIVDGYTNITTLKLFAHTRQEEDYAREAIGdQTLKSQ------- 260
Cdd:cd18562 141 LLVVLAAVYAALNRLVMRRTKAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITR-RLLAAQypvlnww 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 261 RAGRVVTSMDVTITVMnGVLITGTtglalWLWSQELISVGAI----ALATGLVIRINNMSGWIM 320
Cdd:cd18562 220 ALASVLTRAASTLTMV-AIFALGA-----WLVQRGELTVGEIvsfvGFATLLIGRLDQLSGFIN 277
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
378-580 |
1.98e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 378 IQGLDLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRILVDGQDIAGVT-QESLRAQIGMVTQDTsllhrsiRDNL 456
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEER-------RSTG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 457 LYGRPGASDAELMEAVRKARADefIPLLSDAEGRR--------------GFDAHVGErgvkLSGGQRQRIAIARVLLKDA 522
Cdd:PRK10982 337 IYAYLDIGFNSLISNIRNYKNK--VGLLDNSRMKSdtqwvidsmrvktpGHRTQIGS----LSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 523 PILILDEATSALDSEVESAI-QESLETLMQGKTVIAIAHRLSTIARM-DRLVVLDKGHIA 580
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGItDRILVMSNGLVA 470
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
43-250 |
4.55e-05 |
|
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: 45.54 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 43 LLVVGLIVALIEVALFSYLGRIVDLAQSTPSAEFFRvhaneliwMAVVALVLRPLFNALHDMLVHQSINPSMTNL---IR 119
Cdd:cd18589 1 VLGLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFT--------AAITVMSLLTIASAVSEFVCDLIYNITMSRIhsrLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 120 WQNHRYVLKQSLGFFQNDFAGRIAQRIMQTGNSLRDSAVQvvdALWHVLIYTVSALVLF---AEADWRLMI------PLV 190
Cdd:cd18589 73 GLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSE---NLSLLMWYLARGLFLFifmLWLSPKLALltalglPLL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598424 191 LWVFAYVG----ALAyfvPQVKRRSVEASDSrsklmgrIVDGYTNITTLKLFAHTRQEEDYARE 250
Cdd:cd18589 150 LLVPKFVGkfqqSLA---VQVQKSLARANQV-------AVETFSAMKTVRSFANEEGEAQRYRQ 203
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
382-535 |
5.06e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 382 DLKVRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRIL-----VDGQDIAgvtqesLRAQIGMVTQDTSL---LhrSIR 453
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDIA------TRRRVGYMSQAFSLygeL--TVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 454 DNL-----LYGRPgasdaelmEAVRKARADEFIpllsdaeGRRGFDAHVGERGVKLSGGQRQRIAIARVLLKDAPILILD 528
Cdd:NF033858 358 QNLelharLFHLP--------AAEIAARVAEML-------ERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
....*..
gi 15598424 529 EATSALD 535
Cdd:NF033858 423 EPTSGVD 429
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
504-588 |
3.06e-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: 43.85 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 504 LSGGQRQRIAIARVLLKDA---PILILDEATSALDSEvesAIQESLETLM----QGKTVIAIAHRLSTIARMDRLVVL-- 574
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFD---DIKKLLEVLQrlvdKGNTVVVIEHNLDVIKTADYIIDLgp 906
|
90
....*....|....*...
gi 15598424 575 ---DK-GHIAESGTHAEL 588
Cdd:TIGR00630 907 eggDGgGTVVASGTPEEV 924
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
493-576 |
3.28e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 493 FDAHVGERGV-----KLSGGQRQ------RIAIARVLLKDAPILILDEATSALDSEVESAIQESLE-TLMQGK---TVIA 557
Cdd:PRK01156 786 FNITVSRGGMvegidSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSdipQVIM 865
|
90
....*....|....*....
gi 15598424 558 IAHRLSTIARMDRLVVLDK 576
Cdd:PRK01156 866 ISHHRELLSVADVAYEVKK 884
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
393-489 |
3.74e-04 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 40.98 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 393 LVGPSGAGKSTLVNLLLRLYDLESGRIL-----------VDGQDIAGVTQESLRAqigMVTQDTSLLHRSIRDNlLYGRP 461
Cdd:cd00071 4 LSGPSGVGKSTLLKRLLEEFDPNFGFSVshttrkprpgeVDGVDYHFVSKEEFER---LIENGEFLEWAEFHGN-YYGTS 79
|
90 100
....*....|....*....|....*....
gi 15598424 462 gasdaelMEAVRKARADEFIPLLS-DAEG 489
Cdd:cd00071 80 -------KAAVEEALAEGKIVILEiDVQG 101
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
385-419 |
3.86e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 43.00 E-value: 3.86e-04
10 20 30
....*....|....*....|....*....|....*
gi 15598424 385 VRPGEKIGLVGPSGAGKSTLVNLLLRLYDLESGRI 419
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
388-560 |
4.31e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 388 GEKIGLVGPSGAGKSTLVNLLlRLYDLE----SGRILVDGQDIAGVTQESLRAQIGMVTQDTSLLHRSI------RDNLL 457
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYM-AMHAIDgipkNCQILHVEQEVVGDDTTALQCVLNTDIERTQLLEEEAqlvaqqRELEF 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 458 YGRPGASDAELMEAVRK----ARADEFIPLLS-----DAEGRRG-------FDAHVGERGVK-LSGGQRQRIAIARVLLK 520
Cdd:PLN03073 282 ETETGKGKGANKDGVDKdavsQRLEEIYKRLElidayTAEARAAsilaglsFTPEMQVKATKtFSGGWRMRIALARALFI 361
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598424 521 DAPILILDEATSALDSEVESAIQESLetLMQGKTVIAIAH 560
Cdd:PLN03073 362 EPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
393-422 |
5.30e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 41.61 E-value: 5.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 15598424 393 LVGPSGAGKSTLVNLLL------------------------RLYDLESGRILVD 422
Cdd:cd01854 90 LVGQSGVGKSTLLNALLpelvlatgeiseklgrgrhttthrELFPLPGGGLIID 143
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
390-438 |
6.40e-04 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 39.52 E-value: 6.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15598424 390 KIGLVGPSGAGKSTLVNLLLRlydlesGRILVDgqDIAGVTQESLRAQI 438
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTG------AKAIVS--DYPGTTRDPNEGRL 41
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
504-572 |
7.93e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 40.91 E-value: 7.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598424 504 LSGGQRQRIAIARV----LLKDAPILILDEATSALD-SEVE---SAIQEsletlMQGKT-VIAIAHRLSTIARMDRLV 572
Cdd:cd03278 114 LSGGEKALTALALLfaifRVRPSPFCVLDEVDAALDdANVErfaRLLKE-----FSKETqFIVITHRKGTMEAADRLY 186
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
493-572 |
8.24e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 493 FDAHVGERGVK----LSGGQRQRIAIARVL----LKDAPILILDEATSALDSEVESAIQESLETLMQGKTVIAIAHRLST 564
Cdd:pfam02463 1063 ISARPPGKGVKnldlLSGGEKTLVALALIFaiqkYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEM 1142
|
....*...
gi 15598424 565 IARMDRLV 572
Cdd:pfam02463 1143 LEKADKLV 1150
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
44-265 |
8.94e-04 |
|
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: 41.75 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 44 LVVGLIVALIEVALFSY----LGRIVDLAQSTPSAeffrvhANELIWMAVVAL---VLRPLFNALHDMLVH---QSINPS 113
Cdd:cd18778 1 LILTLLCALLSTLLGLVppwlIRELVDLVTIGSKS------LGLLLGLALLLLgayLLRALLNFLRIYLNHvaeQKVVAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 114 MtnliRWQNHRYVLKQSLGFFQNDFAGRIAQRIMQTGNSLRDSAVQVV-DALWHVLIYTVSALVLFAeADWRL----MIP 188
Cdd:cd18778 75 L----RSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIpQGITNVLTLVGVAIILFS-INPKLalltLIP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598424 189 LvlwVFAYVGALaYFVPQVKRRSVEASDSRSKLMGRIVDGYTNITTLKLFahTRQEEDYAR--EAIGDQTLKSQRAGRV 265
Cdd:cd18778 150 I---PFLALGAW-LYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAF--GREEEEAKRfeALSRRYRKAQLRAMKL 222
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
40-312 |
9.40e-04 |
|
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: 41.70 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 40 FLALLVVGLIVALIEVALFSYLGRIVDLAqstpsaeFFRVHANELIWMAVVALVLrPLFNALHDML-------VHQSInp 112
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDA-------LPQGDLGLLVLLALGMVAV-AVASALLGVVqtylsarIGQGV-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 113 sMTNLiRWQNHRYVLKQSLGFFQNDFAGRIAQRI------MQtgNSLRDSAVQVVDALWhVLIYTVSALVLFaeaDWRL- 185
Cdd:cd18550 71 -MYDL-RVQLYAHLQRMSLAFFTRTRTGEIQSRLnndvggAQ--SVVTGTLTSVVSNVV-TLVATLVAMLAL---DWRLa 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 186 -----MIPLVLWVFAYVGALAYfvpQVKRRSVEASDSRSKLMGRI--VDGytnITTLKLFAHTRQEED-YAREA--IGDQ 255
Cdd:cd18550 143 llslvLLPLFVLPTRRVGRRRR---KLTREQQEKLAELNSIMQETlsVSG---ALLVKLFGREDDEAArFARRSreLRDL 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598424 256 TLKSQRAGRVVTsmdVTITVMNGVLITGTTGLALWLWSQELISVGAIALATGLVIRI 312
Cdd:cd18550 217 GVRQALAGRWFF---AALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRL 270
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
42-290 |
3.50e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 39.80 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 42 ALLVVGLIVALIEVALFS-YL-GRIVD--LAQSTPSAEFfrvhanELIWMAVVAL----VLRPLFNALHDMLVhQSINPS 113
Cdd:cd18563 1 LILGFLLMLLGTALGLVPpYLtKILIDdvLIQLGPGGNT------SLLLLLVLGLagayVLSALLGILRGRLL-ARLGER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 114 MTNLIRWQNHRYVLKQSLGFFQNDFAGRIAQRIMQTGNSLRDSAVQ-VVDALWHVLIYTVSALVLFAeADWRLM------ 186
Cdd:cd18563 74 ITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDgLPDFLTNILMIIGIGVVLFS-LNWKLAllvlip 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 187 IPLVLWVFAYVGalayfvPQVKRRSVEASDSRSKLMGRIVDGYTNITTLKLFAHTRQEEDYAREAIGDQTLKSQRAGRVV 266
Cdd:cd18563 153 VPLVVWGSYFFW------KKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLW 226
|
250 260
....*....|....*....|....
gi 15598424 267 TSMDVTITvmngvLITGTTGLALW 290
Cdd:cd18563 227 ATFFPLLT-----FLTSLGTLIVW 245
|
|
| AAA_28 |
pfam13521 |
AAA domain; |
390-478 |
4.69e-03 |
|
AAA domain;
Pssm-ID: 433278 [Multi-domain] Cd Length: 164 Bit Score: 38.40 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598424 390 KIGLVGPSGAGKSTLVNLLLRLYD----LESGRILVDGQDIAG-----VTQESLRAQIGMVTQDTSLLH----------- 449
Cdd:pfam13521 1 RIVITGGPSTGKTTLAEALAARFGypvvPEAAREILEELGADGgdalpWVEDLLAFARGVLEAQLEDEAaaaandllffd 80
|
90 100 110
....*....|....*....|....*....|.
gi 15598424 450 RSIRDNLLYGRP--GASDAELMEAVRKARAD 478
Cdd:pfam13521 81 RGPLDTLAYSRAygGPCPPELEAAARASRYD 111
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
504-535 |
5.20e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 39.20 E-value: 5.20e-03
10 20 30
....*....|....*....|....*....|....*.
gi 15598424 504 LSGGQRQRIAIARVL----LKDAPILILDEATSALD 535
Cdd:cd03273 167 LSGGQRSLVALSLILalllFKPAPMYILDEVDAALD 202
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
393-422 |
5.91e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.91 E-value: 5.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 15598424 393 LVGPSGAGKSTLVNLLL------------------------RLYDLESGRILVD 422
Cdd:pfam03193 111 LAGQSGVGKSTLLNALLpeldlrtgeiseklgrgrhttthvELFPLPGGGLLID 164
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
504-574 |
6.35e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 6.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598424 504 LSGGQRQRIAIARVLL---KDAPILILDEATSALDS-EVESAIQESLETLMQGKTVIAIAHRLSTIARMDRLVVL 574
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHThDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
393-422 |
8.89e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 38.65 E-value: 8.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 15598424 393 LVGPSGAGKSTLVNLLL------------------------RLYDLESGRILVD 422
Cdd:PRK00098 169 LAGQSGVGKSTLLNALApdlelktgeisealgrgkhttthvELYDLPGGGLLID 222
|
|
| |
