|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-587 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 673.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 14 TAFSAAHLKRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYR 93
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 94 IRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDP 173
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 174 VLTLYSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAV 253
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 254 KIQFLLWPGVQNIAVMTTCLIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMD 330
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVG--GLLVlsgSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 331 VEPDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILV 410
Cdd:COG1132 320 EPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 411 DGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSA 490
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 491 GQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHE 570
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
570
....*....|....*..
gi 346645039 571 ELMAQHGYYYNLYQSQF 587
Cdd:COG1132 560 ELLARGGLYARLYRLQF 576
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-586 |
3.11e-169 |
|
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: 498.20 E-value: 3.11e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 21 LKRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcMRY-RIRSITL 99
Cdd:COG2274 144 LRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGL-LRLlRSYLLLR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 100 IGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVvNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYS 179
Cdd:COG2274 223 LGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 180 LALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLL 259
Cdd:COG2274 302 LLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 260 WPGVQNIAVMTTCLIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIK 336
Cdd:COG2274 382 STLSGLLQQLATVALLWLG--AYLVidgQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPERE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 337 DIPNAKKMPPIVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV 415
Cdd:COG2274 460 EGRSKLSLPRLKGDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 416 EEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQL 495
Cdd:COG2274 540 RQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 496 ISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
570
....*....|.
gi 346645039 576 HGYYYNLYQSQ 586
Cdd:COG2274 700 KGLYAELVQQQ 710
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
35-325 |
7.13e-131 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 384.51 E-value: 7.13e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIK 194
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 195 TAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLI 274
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 346645039 275 YFVGIKG-YGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18545 242 YWYGGKLvLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
19-587 |
6.17e-130 |
|
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: 392.53 E-value: 6.17e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 19 AHLKRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSIT 98
Cdd:TIGR02204 4 RPLAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 99 LIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLY 178
Cdd:TIGR02204 84 WLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 179 SLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIF-TEVSNEYR--------RSW 249
Cdd:TIGR02204 164 VLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFgGAVEKAYEaarqrirtRAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 250 MKAVKIQF-------LLWPGVQNIavmttcliyfvgIKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYL 322
Cdd:TIGR02204 244 LTAIVIVLvfgaivgVLWVGAHDV------------IAG---KMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 323 ERIFETMDVEPDIKDIPNAKKMP-PIVGNVDFKDVYFRYEEGVD--ILKGINFHVDAGESIALVGPTGAGKTTIINLLSR 399
Cdd:TIGR02204 309 ERLIELLQAEPDIKAPAHPKTLPvPLRGEIEFEQVNFAYPARPDqpALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 400 FYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYT 479
Cdd:TIGR02204 389 FYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 480 EVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYID 559
Cdd:TIGR02204 469 YLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMD 548
|
570 580
....*....|....*....|....*...
gi 346645039 560 NGRIQEAGSHEELMAQHGYYYNLYQSQF 587
Cdd:TIGR02204 549 QGRIVAQGTHAELIAKGGLYARLARLQF 576
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-588 |
7.09e-130 |
|
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: 392.16 E-value: 7.09e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 20 HLKRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITL 99
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 100 IGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYS 179
Cdd:TIGR02203 81 VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 180 LALIPVLFVIVMVIktaqRKAYQVLSNKQSNMNA----YIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKI 255
Cdd:TIGR02203 161 VVMLPVLSILMRRV----SKRLRRISKEIQNSMGqvttVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 256 QFLLWPGVQNIA-VMTTCLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPD 334
Cdd:TIGR02203 237 GSISSPITQLIAsLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 335 IKDipNAKKMPPIVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGE 413
Cdd:TIGR02203 317 KDT--GTRAIERARGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 414 NVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKL-DATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQ 492
Cdd:TIGR02203 395 DLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 493 RQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
570
....*....|....*.
gi 346645039 573 MAQHGYYYNLYQSQFD 588
Cdd:TIGR02203 555 LARNGLYAQLHNMQFR 570
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
351-583 |
7.69e-124 |
|
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: 364.24 E-value: 7.69e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYE-EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGV 429
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLY 583
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
349-577 |
1.53e-119 |
|
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: 353.07 E-value: 1.53e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 349 GNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMG 428
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKI 508
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 509 LILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHG 577
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
39-586 |
4.58e-114 |
|
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: 352.59 E-value: 4.58e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 39 LFVILLANVATMIGPYLTKIVIDDtiPNKNMTQLFWIAVIFIVSVIVTGLCMRY--RIRSI--TLIGQDILKDMRTAIFG 114
Cdd:COG5265 42 LLLLLLAAALALVVPPLLKDAIDA--LLSGAAALLVVPVGLLLAYGLLRLLSVLfgELRDAlfARVTQRAVRRLALEVFR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHG---KILIRVVNYInmlSDLLSNGLINLISDILSVIVTLGFML-MIDPVLTLYSLALIpVLFVIV 190
Cdd:COG5265 120 HLHALSLRFHLERQTGglsRDIERGTKGI---EFLLRFLLFNILPTLLEIALVAGILLvKYDWWFALITLVTV-VLYIAF 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 191 MVIKTAQRKAYQVLSNKQ-SNMNAYIHESIAGIKVTQSFSREEenFEiftevSNEYRRSWMK----AVKIQFLLwpGVQN 265
Cdd:COG5265 196 TVVVTEWRTKFRREMNEAdSEANTRAVDSLLNYETVKYFGNEA--RE-----ARRYDEALARyeraAVKSQTSL--ALLN 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 266 I---AVMTTCLIYFVGIKGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIKDIP 339
Cdd:COG5265 267 FgqaLIIALGLTAMMLMAAQGVvagTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 340 NAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT 419
Cdd:COG5265 347 DAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 420 LRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFA 499
Cdd:COG5265 427 QASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIA 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 500 RALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYY 579
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLY 586
|
....*..
gi 346645039 580 YNLYQSQ 586
Cdd:COG5265 587 AQMWARQ 593
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
351-586 |
2.83e-113 |
|
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: 337.59 E-value: 2.83e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEE--GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMG 428
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKI 508
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 509 LILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLYQSQ 586
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
22-577 |
1.27e-111 |
|
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: 344.82 E-value: 1.27e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 22 KRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTI-PNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLI 100
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIiGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 101 GQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLIsdiLSVIVT---LGFMLMIDPV--- 174
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLF---LAALVPlliLVAVFPLDWLsgl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 175 LTLYSLALIPVLFVIVMVI-KTAQRKAYQVLSNkqsnMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAV 253
Cdd:COG4988 163 ILLVTAPLIPLFMILVGKGaAKASRRQWRALAR----LSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 254 KIQFLlwpgvqNIAVM-------TTCLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIF 326
Cdd:COG4988 239 RVAFL------SSAVLeffaslsIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 327 ETMDVEPDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSG 406
Cdd:COG4988 313 ALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 407 EILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGS 486
Cdd:COG4988 393 SILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 487 TLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEA 566
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
570
....*....|.
gi 346645039 567 GSHEELMAQHG 577
Cdd:COG4988 553 GTHEELLAKNG 563
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-591 |
2.78e-107 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 334.62 E-value: 2.78e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 23 RILVYVKPYQK-SIYITLFVILLAnVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcmryrirsITLIG 101
Cdd:PRK13657 9 RVLQYLGAEKRlGILLAVANVLLA-AATFAEPILFGRIIDAISGKGDIFPLLAAWAGFGLFNIIAGV--------LVARH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 102 QDILKDMR-----TAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDpvlt 176
Cdd:PRK13657 80 ADRLAHRRrlavlTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMN---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 177 lYSLALIPVLFVIVMVIKTA--QRKAY---QVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEyrrswMK 251
Cdd:PRK13657 156 -WRLSLVLVVLGIVYTLITTlvMRKTKdgqAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADN-----LL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 252 AVKIQFLLWPGVQNI-----AVMTTCLIYFVGI----KGygvDVSTGTLIAFIGyvgnFWNPVI----NIGNFYNSLITA 318
Cdd:PRK13657 230 AAQMPVLSWWALASVlnraaSTITMLAILVLGAalvqKG---QLRVGEVVAFVG----FATLLIgrldQVVAFINQVFMA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 319 TTYLERIFETMDVEPDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLS 398
Cdd:PRK13657 303 APKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 399 RFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYY 478
Cdd:PRK13657 383 RVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 479 TEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYI 558
Cdd:PRK13657 463 TVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVF 542
|
570 580 590
....*....|....*....|....*....|...
gi 346645039 559 DNGRIQEAGSHEELMAQHGYYYNLYQSQFdMLQ 591
Cdd:PRK13657 543 DNGRVVESGSFDELVARGGRFAALLRAQG-MLQ 574
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-588 |
8.97e-107 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 333.14 E-value: 8.97e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 22 KRILVYVKPYqKSIYITLFVILLANVAT---MIgpYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSIT 98
Cdd:PRK11176 14 RRLWPTIAPF-KAGLIVAGVALILNAASdtfML--SLLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGITSFISSYCIS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 99 LIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMidpvltlY 178
Cdd:PRK11176 91 WVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFY-------Y 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 179 SLALIPVLFVIVMVIKTAQR---KAYQVLS-NKQSNM---NAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMK 251
Cdd:PRK11176 164 SWQLSLILIVIAPIVSIAIRvvsKRFRNISkNMQNTMgqvTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 252 AVKIQFLLWPGVQNIAVMT-TCLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVinignfyNSLITATTYLER------ 324
Cdd:PRK11176 244 MVSASSISDPIIQLIASLAlAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPL-------KSLTNVNAQFQRgmaacq 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 325 -IFETMDVEPDiKDIpNAKKMPPIVGNVDFKDVYFRYEeGVDI--LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFY 401
Cdd:PRK11176 317 tLFAILDLEQE-KDE-GKRVIERAKGDIEFRNVTFTYP-GKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 402 NINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDA-TEEEIIAAAKVVRAHDFISGLKDGYYTE 480
Cdd:PRK11176 394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 481 VKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDN 560
Cdd:PRK11176 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVED 553
|
570 580
....*....|....*....|....*...
gi 346645039 561 GRIQEAGSHEELMAQHGYYYNLYQSQFD 588
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVYAQLHKMQFG 581
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
351-586 |
1.59e-106 |
|
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: 320.33 E-value: 1.59e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVM 430
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILI 510
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 511 LDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLYQSQ 586
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
24-586 |
5.11e-106 |
|
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: 334.40 E-value: 5.11e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 24 ILVYVKPYQKSIYITLFVILLAnvatMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQD 103
Cdd:TIGR01846 134 IIRYRKQFREVLLISLALQLFA----LVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 104 ILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVvNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALI 183
Cdd:TIGR01846 210 IDVELGARLYRHLLGLPLGYFESRRVGDTVARV-RELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 184 PVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGV 263
Cdd:TIGR01846 289 VCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAI 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 264 QNIAVMTTCLIYFVGIKGY-GVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDvEPDIKDIPNAK 342
Cdd:TIGR01846 369 ELIQKLTFAILLWFGAHLViGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAGLA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 343 KMPPIVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLR 421
Cdd:TIGR01846 448 ALPELRGAITFENIRFRYaPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 422 SLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARA 501
Cdd:TIGR01846 528 WLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARA 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 502 LLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYN 581
Cdd:TIGR01846 608 LVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYAR 687
|
....*
gi 346645039 582 LYQSQ 586
Cdd:TIGR01846 688 LWQQQ 692
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-582 |
9.69e-106 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 334.00 E-value: 9.69e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 2 ARNKFDIDEELETAfsaAHLKRILVYVKPyQKSIYITLFVIL-LANVATMIGPYLTKIVIDdTIPNKNMTQLFWIAVIF- 79
Cdd:TIGR00958 133 ASEKEAEQGQSETA---DLLFRLLGLSGR-DWPWLISAFVFLtLSSLGEMFIPFYTGRVID-TLGGDKGPPALASAIFFm 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 80 ----IVSVIVTGL---CMRYRIRSITLigqdilkDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLI 152
Cdd:TIGR00958 208 cllsIASSVSAGLrggSFNYTMARINL-------RIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVN 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 153 NLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKtaqrKAYQVLSNK------QSNMNAyiHESIAGIKVTQ 226
Cdd:TIGR00958 281 VLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFG----KRYQLLSEElqeavaKANQVA--EEALSGMRTVR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 227 SFSREEENFEIFTEVSNEYRR-SWMKAVKIQFLLWpgvqNIAVMTtcLIYFVGIKGYGV------DVSTGTLIAFIGYVG 299
Cdd:TIGR00958 355 SFAAEEGEASRFKEALEETLQlNKRKALAYAGYLW----TTSVLG--MLIQVLVLYYGGqlvltgKVSSGNLVSFLLYQE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 300 NFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIKdiPNAKKMP-PIVGNVDFKDVYFRY--EEGVDILKGINFHVDA 376
Cdd:TIGR00958 429 QLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIP--LTGTLAPlNLEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHP 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 377 GESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEE 456
Cdd:TIGR00958 507 GEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 457 IIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERllEG 536
Cdd:TIGR00958 587 IMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--AS 664
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 346645039 537 RTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNL 582
Cdd:TIGR00958 665 RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
78-584 |
2.47e-98 |
|
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: 310.54 E-value: 2.47e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 78 IFIVSVIVTGLCM-----RY--RIRS--ITLigqDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLS 148
Cdd:COG4987 54 LFVPIVGVRAFAIgrtvfRYleRLVShdATL---RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 149 NGLINLISDILSVIVTLGFMLMIDPVLTL-YSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQS 227
Cdd:COG4987 131 RVLLPLLVALLVILAAVAFLAFFSPALALvLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 228 FSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYFVGIKGYGVDVSTGTLIAFIGY----VGNFWN 303
Cdd:COG4987 211 YGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLaalaLFEALA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 304 PVINIGNFYNSLITAttyLERIFETMDVEPDIKDiPNAKKMPPIVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIAL 382
Cdd:COG4987 291 PLPAAAQHLGRVRAA---ARRLNELLDAPPAVTE-PAEPAPAPGGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 383 VGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAK 462
Cdd:COG4987 367 VGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALE 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 463 VVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFII 542
Cdd:COG4987 447 RVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLI 526
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 346645039 543 AHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLYQ 584
Cdd:COG4987 527 THRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-586 |
8.89e-96 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 304.72 E-value: 8.89e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 21 LKRILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNM--TQLFWIAVIFIVSVIVTGLCMRYRIRSIT 98
Cdd:PRK10790 11 LKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLplGLVAGLAAAYVGLQLLAAGLHYAQSLLFN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 99 LIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLsnglINLISDILSVIVTLGFML----MIDPV 174
Cdd:PRK10790 91 RAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLY----VTVVATVLRSAALIGAMLvamfSLDWR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 175 LTLYSLALIPVLFvIVMVIktAQRKAYQVLSNKQS---NMNAYIHESIAGIKVTQSFsREEENF-EIFTEVSNEYRRSWM 250
Cdd:PRK10790 167 MALVAIMIFPAVL-VVMVI--YQRYSTPIVRRVRAylaDINDGFNEVINGMSVIQQF-RQQARFgERMGEASRSHYMARM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 251 KAVKIQ-FLLWPGVQNIAVMTTC-LIYFVGIKGYGVdVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFET 328
Cdd:PRK10790 243 QTLRLDgFLLRPLLSLFSALILCgLLMLFGFSASGT-IEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 329 MDVE-----PDIKdipnakkmPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNI 403
Cdd:PRK10790 322 MDGPrqqygNDDR--------PLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 404 NSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKlDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKE 483
Cdd:PRK10790 394 TEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 484 RGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:PRK10790 473 QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
570 580
....*....|....*....|...
gi 346645039 564 QEAGSHEELMAQHGYYYNLYQSQ 586
Cdd:PRK10790 553 VEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
28-586 |
4.27e-85 |
|
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: 279.15 E-value: 4.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 28 VKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRyrIRSITLIGQDILKD 107
Cdd:TIGR03797 131 LRGARRDLLAILAMGLLGTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQL--AQSLAVLRLETRMD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 108 MRT--AIFGHLQKLPFSYFDSRPHGKILIRVVNyINMLSDLLSN-GLINLISDILSVIvTLGFMLMIDPVLTLYSLALIP 184
Cdd:TIGR03797 209 ASLqaAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGsTLTTLLSGIFALL-NLGLMFYYSWKLALVAVALAL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 185 VLFVIVMVIK----TAQRKAyQVLSNKQSNMNAYIHESIAGIKVTQSfsrEEENFEIFTEVSNEYRRSWMKAVKIQFLL- 259
Cdd:TIGR03797 287 VAIAVTLVLGllqvRKERRL-LELSGKISGLTVQLINGISKLRVAGA---ENRAFARWAKLFSRQRKLELSAQRIENLLt 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 260 -----WPGVQNIAvmttcLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPD 334
Cdd:TIGR03797 363 vfnavLPVLTSAA-----LFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 335 IkdipNAKKMPP--IVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVD 411
Cdd:TIGR03797 438 V----DEAKTDPgkLSGAIEVDRVTFRYrPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYD 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 412 GENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIrYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAG 491
Cdd:TIGR03797 514 GQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGG 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 492 QRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLleGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEE 571
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDE 670
|
570
....*....|....*
gi 346645039 572 LMAQHGYYYNLYQSQ 586
Cdd:TIGR03797 671 LMAREGLFAQLARRQ 685
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
351-586 |
7.31e-83 |
|
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: 259.34 E-value: 7.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYE-EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGV 429
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLYQSQ 586
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
35-325 |
5.49e-81 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 256.55 E-value: 5.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 35 IYITLFVILLANVATMIGPYLTKIVIDDTI--PNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIvpGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 193 IKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTC 272
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 346645039 273 LI-YFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18544 241 LVlWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
41-582 |
5.80e-80 |
|
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: 262.90 E-value: 5.80e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 41 VILLANVA----TMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRyriRSITLIGQDILKDMRTAIFGHL 116
Cdd:TIGR01192 23 LIVIANITlaaiTIAEPILFGRIIDAISSKSDVLPTLALWAGFGVFNTIAYVLVA---READRLAHGRRATLLTEAFGRI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTA 196
Cdd:TIGR01192 100 ISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSIVLMVLGILYILIAKLVMQR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSR-EEENFEI--FTE--VSNEYR--RSWMKAVKIQFLlwpgVQNIAVM 269
Cdd:TIGR01192 180 TKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRiEAETSALkqFTNnlLSAQYPvlDWWALASGLNRM----ASTISMM 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 270 TTCLI-YFVGIKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIKDIPNAKKMPPIV 348
Cdd:TIGR01192 256 CILVIgTVLVIKG---ELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPELPNVK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 349 GNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMG 428
Cdd:TIGR01192 333 GAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKI 508
Cdd:TIGR01192 413 TVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPI 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 509 LILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNL 582
Cdd:TIGR01192 493 LVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKL 566
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
32-583 |
1.20e-78 |
|
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: 262.75 E-value: 1.20e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 32 QKS-IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRT 110
Cdd:TIGR01193 154 QKKlIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIIL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 111 AIFGHLQKLPFSYFDSRPHGKILIRVVNyINMLSDLLSNGLINLISDiLSVIVTLGFMLMI-DPVLTLYSLALIPVLFVI 189
Cdd:TIGR01193 234 SYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTILSLFLD-MWILVIVGLFLVRqNMLLFLLSLLSIPVYAVI 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 190 VMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENF-EIFTEVSNEYRRS--WMKAVKIQFLLWPGVQNI 266
Cdd:TIGR01193 312 IILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYsKIDSEFGDYLNKSfkYQKADQGQQAIKAVTKLI 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 267 avMTTCLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIKDIPNAKKMPP 346
Cdd:TIGR01193 392 --LNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNN 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 347 IVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQ 426
Cdd:TIGR01193 470 LNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 427 MGVMLQDTFIFSGTIIENIRYG-KLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLAD 505
Cdd:TIGR01193 550 INYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTD 629
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 506 PKILILDEATSSIDTQTEILLQEGLERLLEgRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLY 583
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
38-582 |
3.63e-77 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 258.72 E-value: 3.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 38 TLFVILLANVATMIG----PYLTKIVIDDTIPNKN---MTQLFWIAVIfivSVIVTGLCMRYRIRSITLIGQDILKDMRT 110
Cdd:TIGR03796 155 ALLYLLLAGLLLVLPglviPAFSQIFVDEILVQGRqdwLRPLLLGMGL---TALLQGVLTWLQLYYLRRLEIKLAVGMSA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 111 AIFGHLQKLPFSYFDSRPHGKILIRV-VNyiNMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIpVLFVI 189
Cdd:TIGR03796 232 RFLWHILRLPVRFFAQRHAGDIASRVqLN--DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFA-AINVL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 190 VMVIKTAQRkayqVLSNKQSNMNA--YIHESIAGIKVTQSF--SREEENFeiFTEVSNEYRRSWMKAVKIQFLL-WPGV- 263
Cdd:TIGR03796 309 ALQLVSRRR----VDANRRLQQDAgkLTGVAISGLQSIETLkaSGLESDF--FSRWAGYQAKLLNAQQELGVLTqILGVl 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 264 -QNIAVMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIKDI 338
Cdd:TIGR03796 383 pTLLTSLNSALILVVGglrvMEG---QLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRNPVDPLLE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 339 ------PNAKKMPPIVGNVDFKDVYFRYEE-GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVD 411
Cdd:TIGR03796 460 epegsaATSEPPRRLSGYVELRNITFGYSPlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFD 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 412 GENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYgkLDAT--EEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLS 489
Cdd:TIGR03796 540 GIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTL--WDPTipDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLS 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 490 AGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERllEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSH 569
Cdd:TIGR03796 618 GGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTH 695
|
570
....*....|...
gi 346645039 570 EELMAQHGYYYNL 582
Cdd:TIGR03796 696 EELWAVGGAYARL 708
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
68-555 |
5.39e-73 |
|
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: 242.96 E-value: 5.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 68 NMTQLFWIAVIFIVsVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLL 147
Cdd:TIGR02857 40 LAELLPALGALALV-LLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 148 SNGLINLIsdiLSVIVTLGFMLMIDP------VLTLYSLALIPVLFVIV-MVIKTAQRKAYQVLSNkqsnMNAYIHESIA 220
Cdd:TIGR02857 119 ARYLPQLV---LAVIVPLAILAAVFPqdwisgLILLLTAPLIPIFMILIgWAAQAAARKQWAALSR----LSGHFLDRLR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 221 GIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLI-YFVGIK--GYGVDVSTGTLIAFIgy 297
Cdd:TIGR02857 192 GLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSVALVaVYIGFRllAGDLDLATGLFVLLL-- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 298 VGNFWNPVINIGNFYNSLITATTYLERIFETMD----VEPDIKDIPnAKKMPPIVgnvdFKDVYFRYEEGVDILKGINFH 373
Cdd:TIGR02857 270 APEFYLPLRQLGAQYHARADGVAAAEALFAVLDaaprPLAGKAPVT-AAPASSLE----FSGVSVAYPGRRPALRPVSFT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 374 VDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDAT 453
Cdd:TIGR02857 345 VPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDAS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 454 EEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERL 533
Cdd:TIGR02857 425 DAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL 504
|
490 500
....*....|....*....|..
gi 346645039 534 LEGRTSFIIAHRLSTIKNSSRI 555
Cdd:TIGR02857 505 AQGRTVLLVTHRLALAALADRI 526
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
351-562 |
6.75e-73 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 230.73 E-value: 6.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGV 429
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTFIFSGTIIENIrygkldateeeiiaaakvvrahdfisglkdgyytevkergstLSAGQRQLISFARALLADPKIL 509
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGR 562
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
37-325 |
1.75e-72 |
|
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: 234.37 E-value: 1.75e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 37 ITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTA 196
Cdd:cd07346 83 QRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYF 276
Cdd:cd07346 163 IRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 346645039 277 VGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd07346 243 YG--GYLVlqgSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
349-568 |
2.01e-71 |
|
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: 228.92 E-value: 2.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 349 GNVDFKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQM 427
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSGTIIENirygkLD----ATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALL 503
Cdd:cd03244 81 SIIPQDPVLFSGTIRSN-----LDpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 504 ADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGS 568
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
35-325 |
3.60e-71 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 230.84 E-value: 3.60e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIK 194
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 195 TAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLI 274
Cdd:cd18546 161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 346645039 275 YFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18546 241 LLVG--AWRVaagTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
41-586 |
2.06e-70 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 237.30 E-value: 2.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 41 VILLANVATM--IGPYLTKIVIDDtIPNKNMTQ---LFWIAVIFIVSVIVTGLcmRYRIRsITLIGQD--ILKDMRTAIF 113
Cdd:PRK10789 1 VALLIIIAMLqlIPPKVVGIIVDG-VTEQHMTTgqiLMWIGTMVLIAVVVYLL--RYVWR-VLLFGASyqLAVELREDFY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 114 GHL-QKLPFSYFDSRPhGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFM-LMIDPVLTLYSLALIPVLfviVM 191
Cdd:PRK10789 77 RQLsRQHPEFYLRHRT-GDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPVM---AI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 192 VIKTAQRKAYQVLSNKQ---SNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQnIAV 268
Cdd:PRK10789 153 MIKRYGDQLHERFKLAQaafSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIY-IAI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 269 MTTCLIYfVGIKGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFETMDVEPDIKDipNAKKMP 345
Cdd:PRK10789 232 GMANLLA-IGGGSWMVvngSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKD--GSEPVP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 346 PIVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLR 424
Cdd:PRK10789 309 EGRGELDVNIRQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLA 504
Cdd:PRK10789 389 SRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 505 DPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNLYQ 584
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR 548
|
..
gi 346645039 585 SQ 586
Cdd:PRK10789 549 YQ 550
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
349-563 |
7.77e-67 |
|
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: 216.95 E-value: 7.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 349 GNVDFKDVYFRYEEGVD--ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQ 426
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 427 MGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADP 506
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
31-582 |
3.99e-64 |
|
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: 229.06 E-value: 3.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 31 YQKSI--YITLFVILL---ANVATMIGPYLTKIVIDDTIPN--KNMTQlFWIAVIFIVSVIVTGLCMRYRIrSITLIGQD 103
Cdd:TIGR00957 958 YMKAIglFITFLSIFLfvcNHVSALASNYWLSLWTDDPMVNgtQNNTS-LRLSVYGALGILQGFAVFGYSM-AVSIGGIQ 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 104 ILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALI 183
Cdd:TIGR00957 1036 ASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLG 1115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 184 PVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSrEEENFEIFTEVS-NEYRRSWMKAVKIQFLLWPG 262
Cdd:TIGR00957 1116 LLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFE-EQERFIHQSDLKvDENQKAYYPSIVANRWLAVR 1194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 263 VQNIAvmtTCLIYFVGIkgYGVdVSTGTLIAfiGYVGNFWNPVINIGNFYNSLI-------TATTYLERIFETMDVEPDI 335
Cdd:TIGR00957 1195 LECVG---NCIVLFAAL--FAV-ISRHSLSA--GLVGLSVSYSLQVTFYLNWLVrmssemeTNIVAVERLKEYSETEKEA 1266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 336 KDIPNAKKMP---PIVGNVDFKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVD 411
Cdd:TIGR00957 1267 PWQIQETAPPsgwPPRGRVEFRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID 1346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 412 GENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIR-YGKLdaTEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSA 490
Cdd:TIGR00957 1347 GLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSV 1424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 491 GQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHE 570
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPS 1504
|
570
....*....|..
gi 346645039 571 ELMAQHGYYYNL 582
Cdd:TIGR00957 1505 NLLQQRGIFYSM 1516
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
349-563 |
1.27e-63 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 208.60 E-value: 1.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 349 GNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQM 427
Cdd:cd03245 1 GRIEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPK 507
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 508 ILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
35-325 |
8.45e-62 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 206.49 E-value: 8.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 35 IYITLFVILLANVATMIGPYLTKIVIDD------TIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDM 108
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLiieglgGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 109 RTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFV 188
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 189 IVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAV 268
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 269 MTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18547 241 LGYVLVAVVGgllvING---ALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
323-586 |
1.55e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 208.14 E-value: 1.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 323 ERIFETMDVEPDIKdIPNAKKMPPIVGNVDFKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFY 401
Cdd:PRK11160 312 RRINEITEQKPEVT-FPTTSTAAADQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAW 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 402 NINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGlKDGYYTEV 481
Cdd:PRK11160 391 DPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 482 KERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEillQEGLERLLE---GRTSFIIAHRLSTIKNSSRIFYI 558
Cdd:PRK11160 470 GEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETE---RQILELLAEhaqNKTVLMITHRLTGLEQFDRICVM 546
|
250 260
....*....|....*....|....*...
gi 346645039 559 DNGRIQEAGSHEELMAQHGYYYNLYQSQ 586
Cdd:PRK11160 547 DNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
37-325 |
7.05e-58 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 195.73 E-value: 7.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 37 ITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd18542 3 LAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTA 196
Cdd:cd18542 83 QRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEenFEI--FTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLI 274
Cdd:cd18542 163 VRPAFEEIREQEGELNTVLQENLTGVRVVKAFARED--YEIekFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 275 YFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18542 241 LWVGgylvING---EITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
43-584 |
3.44e-57 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 202.00 E-value: 3.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 43 LLANVatmigpyLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcmRYRIRSITliGQDILKDMRTAIFGHLQKLPFS 122
Cdd:PRK11174 44 LLATI-------LQALIIENIPREALLPPFILLILLFVLRALLAWL--RERVGFKA--GQHIRQQIRQQVLDKLQQLGPA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 123 YFDSRPHGKILIRVVNYINMLSDLLSNGLINLIsdiLSVIVTLGFMLMIDPV-----LTLYSLA-LIPvLFVIVMVIKTA 196
Cdd:PRK11174 113 WIQGKPAGSWATLVLEQVEDMHDFYARYLPQMA---LAVLVPLLILIAVFPInwaagLILLGTApLIP-LFMALVGMGAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 Q--RKAYQVLSNkqsnMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLwPGVQ------NIAV 268
Cdd:PRK11174 189 DanRRNFLALAR----LSGHFLDRLRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLS-SAVLeffasiSIAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 269 MTtclIYF---------VGIKGYGVDVSTGTLIAFIGyvGNFWNPVINIGNFYNS---LITATTYLERIFETmdvepDIK 336
Cdd:PRK11174 264 VA---VYFgfsylgelnFGHYGTGVTLFAGFFVLILA--PEFYQPLRDLGTFYHAkaqAVGAAESLVTFLET-----PLA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 337 DIPNAKKMPPIVGNVDF--KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRF--YNinsGEILVDG 412
Cdd:PRK11174 334 HPQQGEKELASNDPVTIeaEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKING 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 413 ENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQ 492
Cdd:PRK11174 411 IELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQ 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 493 RQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
570
....*....|..
gi 346645039 573 MAQHGYYYNLYQ 584
Cdd:PRK11174 571 SQAGGLFATLLA 582
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
91-546 |
3.81e-56 |
|
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: 197.97 E-value: 3.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 91 RYRIRsitLIGQD----ILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLG 166
Cdd:TIGR02868 70 RYLER---LVGHDaalrSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 167 FMLMIDPVLTLySLALIPVLFVIVM--VIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNE 244
Cdd:TIGR02868 147 AIAVLSVPAAL-ILAAGLLLAGFVAplVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 245 YRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYFVGIKGYGVDVSTGTLIA-FIGYVGNFWNPVINIGNFYNSLITATTYLE 323
Cdd:TIGR02868 226 LTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAvLVLLPLAAFEAFAALPAAAQQLTRVRAAAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 324 RIFETMDVEP--DIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFY 401
Cdd:TIGR02868 306 RIVEVLDAAGpvAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 402 NINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEV 481
Cdd:TIGR02868 386 DPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 482 KERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRL 546
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
308-575 |
6.41e-55 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 195.35 E-value: 6.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 308 IGNfYNSLITATTYLERIFETMDVEPdikdiPNAKKM--PPIVGNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVG 384
Cdd:COG4618 292 IGG-WKQFVSARQAYRRLNELLAAVP-----AEPERMplPRPKGRLSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIG 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 385 PTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENI-RYGklDATEEEIIAAAKV 463
Cdd:COG4618 366 PSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 464 VRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFII 542
Cdd:COG4618 444 AGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVI 523
|
250 260 270
....*....|....*....|....*....|...
gi 346645039 543 AHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:COG4618 524 THRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
37-325 |
9.15e-55 |
|
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: 187.72 E-value: 9.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 37 ITLFVILLANVATMIGPYLTKIVIDD----TIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:cd18563 3 LGFLLMLLGTALGLVPPYLTKILIDDvliqLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:cd18563 83 YEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 193 IKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTC 272
Cdd:cd18563 163 FWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 273 LIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18563 243 IVWYFG--GRQVlsgTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
37-325 |
1.08e-54 |
|
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: 187.36 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 37 ITLFVILLANVATMIGPYLTKIVIDD-TIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGH 115
Cdd:cd18778 3 LTLLCALLSTLLGLVPPWLIRELVDLvTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 116 LQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKT 195
Cdd:cd18778 83 LQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 196 AQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIY 275
Cdd:cd18778 163 KVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 346645039 276 FVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18778 243 GFG--GRLVlagELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
28-575 |
2.95e-54 |
|
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: 192.95 E-value: 2.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 28 VKPYQKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKD 107
Cdd:TIGR01842 1 LAKVKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 108 MRTAIFghlqKLPFSYFDSRPHGKILiRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLF 187
Cdd:TIGR01842 81 LNQPIF----AASFSATLRRGSGDGL-QALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGILALGGAVVLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 188 VIVMVIKTAQRKAYqvlsnKQSNMnayihESIAGIKVTQSFSREEENFEIFTEVSNEYRRsWMkAVKIQFLLWpgvQNIA 267
Cdd:TIGR01842 156 GLALLNNRATKKPL-----KEATE-----ASIRANNLADSALRNAEVIEAMGMMGNLTKR-WG-RFHSKYLSA---QSAA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 268 ---------------VMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERIFET 328
Cdd:TIGR01842 221 sdragmlsnlskyfrIVLQSLVLGLGaylaIDG---EITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNEL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 329 MDVEPdikdiPNAKKM--PPIVGNVDFKDVYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINS 405
Cdd:TIGR01842 298 LANYP-----SRDPAMplPEPEGHLSVENVTIVPPGGkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 406 GEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENI-RYGKlDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKER 484
Cdd:TIGR01842 373 GSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 485 GSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:TIGR01842 452 GATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
570
....*....|..
gi 346645039 564 QEAGSHEELMAQ 575
Cdd:TIGR01842 532 ARFGERDEVLAK 543
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
37-325 |
5.85e-54 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 185.79 E-value: 5.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 37 ITLFVILLANVATMIGPYLTKIVIDDTIPNK---------------NMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIG 101
Cdd:cd18564 3 LALLALLLETALRLLEPWPLKVVIDDVLGDKplpgllglapllgpdPLALLLLAAAALVGIALLRGLASYAGTYLTALVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 102 QDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLA 181
Cdd:cd18564 83 QRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 182 LIPVLFVIVMV----IKTAQRKAYQvlsnKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQF 257
Cdd:cd18564 163 VAPLLLLAARRfsrrIKEASREQRR----REGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 258 LLWPGVQNIAVMTTCLIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18564 239 LLSPVVDVLVAVGTALVLWFG--AWLVlagRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
31-579 |
3.27e-51 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 190.63 E-value: 3.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 31 YQKSIYITLFVILLAN-----VATMIGPYLTKIV-IDDTIPNKNMTQLFwIAVIFIVSVIVTGLCMRYRirsiTLIGQDI 104
Cdd:PTZ00265 823 YKKDVTIIALSILVAGglypvFALLYAKYVSTLFdFANLEANSNKYSLY-ILVIAIAMFISETLKNYYN----NVIGEKV 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 105 LKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVvnYINMLSDLLSNGLIN--------LISDILSVIVTLGFMLMIDPVLT 176
Cdd:PTZ00265 898 EKTMKRRLFENILYQEISFFDQDKHAPGLLSA--HINRDVHLLKTGLVNnivifthfIVLFLVSMVMSFYFCPIVAAVLT 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 177 LyslalIPVLFVIVMVIKtAQRKAYQVLSNKQSNM--NAYIHESIAGIKVTQSFSREEENFEIFT--------------E 240
Cdd:PTZ00265 976 G-----TYFIFMRVFAIR-ARLTANKDVEKKEINQpgTVFAYNSDDEIFKDPSFLIQEAFYNMNTviiygledyfcnliE 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 241 VSNEYRRSWMK-AVKIQFLLWPGVQNIAVMTTCLIYFVG---IK--GYGVDVSTGTLIAFIgYVGNFWNPVINI-GNFYN 313
Cdd:PTZ00265 1050 KAIDYSNKGQKrKTLVNSMLWGFSQSAQLFINSFAYWFGsflIRrgTILVDDFMKSLFTFL-FTGSYAGKLMSLkGDSEN 1128
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 314 SLITATTYLERIFETMDVepDIKD-----IPNAKKmppIVGNVDFKDVYFRY--EEGVDILKGINFHVDAGESIALVGPT 386
Cdd:PTZ00265 1129 AKLSFEKYYPLIIRKSNI--DVRDnggirIKNKND---IKGKIEIMDVNFRYisRPNVPIYKDLTFSCDSKKTTAIVGET 1203
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 387 GAGKTTIINLLSRFYNI------------------------------------------------------NSGEILVDG 412
Cdd:PTZ00265 1204 GSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDG 1283
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 413 ENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQ 492
Cdd:PTZ00265 1284 VDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQ 1363
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 493 RQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKNSSRIFYIDN-----GRIQE 565
Cdd:PTZ00265 1364 KQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQA 1443
|
650
....*....|....*
gi 346645039 566 AGSHEELM-AQHGYY 579
Cdd:PTZ00265 1444 HGTHEELLsVQDGVY 1458
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
346-568 |
1.02e-50 |
|
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: 173.75 E-value: 1.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 346 PIVGNVDFKDVYFRYEEGV-DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLR 424
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQDTFIFSGTIIENI-RYGKLDatEEEIIAAAKVvrahdfisglkdgyytevKERGSTLSAGQRQLISFARALL 503
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALRV------------------SEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 504 ADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGS 568
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
35-325 |
2.85e-50 |
|
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: 175.30 E-value: 2.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIK 194
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 195 TAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNI-AVMTTCL 273
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLgAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 346645039 274 IYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
33-325 |
4.23e-50 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 174.98 E-value: 4.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 33 KSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:cd18540 2 KLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:cd18540 82 FEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 193 IKT----AQRKAYQVLSNKQSNMNayihESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAV 268
Cdd:cd18540 162 FQKkilkAYRKVRKINSRITGAFN----EGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGS 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 269 MTTCLIYFVGikgyGVDV-----STGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18540 238 IATALVLWYG----GILVlagaiTIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
39-325 |
2.91e-49 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 172.60 E-value: 2.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 39 LFVILLANVATMIGPYLTKIVIDD-TIPNKNMTQLFWIAVIFIVSVIVTGLcMRYrIRSITLIG--QDILKDMRTAIFGH 115
Cdd:cd18541 5 ILFLILVDLLQLLIPRIIGRAIDAlTAGTLTASQLLRYALLILLLALLIGI-FRF-LWRYLIFGasRRIEYDLRNDLFAH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 116 LQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKT 195
Cdd:cd18541 83 LLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 196 AQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIY 275
Cdd:cd18541 163 KIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVL 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 346645039 276 FVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18541 243 WYG--GRLVirgTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
36-311 |
1.55e-48 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 170.71 E-value: 1.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 36 YITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGH 115
Cdd:cd18549 5 FLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 116 LQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKT 195
Cdd:cd18549 85 LQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 196 AQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIY 275
Cdd:cd18549 165 KMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 346645039 276 FVG----IKGYgvdVSTGTLIAFIGYVGNFWNPVINIGNF 311
Cdd:cd18549 245 VAGgyfiIKGE---ITLGDLVAFLLYVNVFIKPIRRLVNF 281
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
79-560 |
1.10e-47 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 180.22 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 79 FIVSVIvTGLCMryrirsiTLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDI 158
Cdd:PTZ00265 111 FILSFI-SSFCM-------DVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 159 LSVIVTLGFMLMIDPVLTLYSLALIPVLFV--IVMVIKTAQRKAYQVLSNkqSNMNAYIHESIAGIKVTQSFSREEENFE 236
Cdd:PTZ00265 183 SAFLGLYIWSLFKNARLTLCITCVFPLIYIcgVICNKKVKINKKTSLLYN--NNTMSIIEEALVGIRTVVSYCGEKTILK 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 237 IFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYFVGIKGYGVDVST---------GTLIA-FIGYVGNFWNPVI 306
Cdd:PTZ00265 261 KFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNqqpnndfhgGSVISiLLGVLISMFMLTI 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 307 ---NIGNFYNSLiTATTYLeriFETMDVEPDIKDIPNAKKMPPIvGNVDFKDVYFRYE--EGVDILKGINFHVDAGESIA 381
Cdd:PTZ00265 341 ilpNITEYMKSL-EATNSL---YEIINRKPLVENNDDGKKLKDI-KKIQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYA 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 382 LVGPTGAGKTTIINLLSRFYNINSGEILV-DGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYG-----KLDATEE 455
Cdd:PTZ00265 416 FVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkDLEALSN 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 456 ----------------------------------------------------EIIAAAKVVRAHDFISGLKDGYYTEVKE 483
Cdd:PTZ00265 496 yynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGS 575
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 484 RGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLL--EGRTSFIIAHRLSTIKNSSRIFYIDN 560
Cdd:PTZ00265 576 NASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
37-325 |
1.72e-47 |
|
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: 168.04 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 37 ITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd18550 3 LVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVI-KT 195
Cdd:cd18550 83 QRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVgRR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 196 AQRKAYQVLsNKQSNMNAYIHE--SIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCL 273
Cdd:cd18550 163 RRKLTREQQ-EKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPAL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 274 IYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18550 242 VYWVG--GLLViggGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
106-577 |
3.35e-45 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 172.47 E-value: 3.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 106 KDMRTAIFGHLQKLPFSYFDSRPHGKILIRV---VNYINMLSDLLSNGLINLISDILSVIVTLGFmlmidpVLTLYSLAL 182
Cdd:PLN03232 983 KRLHDAMLNSILRAPMLFFHTNPTGRVINRFskdIGDIDRNVANLMNMFMNQLWQLLSTFALIGT------VSTISLWAI 1056
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 183 IPVL---FVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLL 259
Cdd:PLN03232 1057 MPLLilfYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWL 1136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 260 WPGVQNIAVMTTCLIYFVGIKGYGvdvSTGTLIAFIGYVGNFWNPVINIGNFYNSLI-------TATTYLERIFETMDVE 332
Cdd:PLN03232 1137 TIRLETLGGVMIWLTATFAVLRNG---NAENQAGFASTMGLLLSYTLNITTLLSGVLrqaskaeNSLNSVERVGNYIDLP 1213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 333 PDIKDIPNAKKMP---PIVGNVDFKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEI 408
Cdd:PLN03232 1214 SEATAIIENNRPVsgwPSRGSIKFEDVHLRYRPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRI 1293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 409 LVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIrygklDATEEEIIAA--AKVVRAH--DFISGLKDGYYTEVKER 484
Cdd:PLN03232 1294 MIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI-----DPFSEHNDADlwEALERAHikDVIDRNPFGLDAEVSEG 1368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 485 GSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQ 564
Cdd:PLN03232 1369 GENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVL 1448
|
490
....*....|...
gi 346645039 565 EAGSHEELMAQHG 577
Cdd:PLN03232 1449 EYDSPQELLSRDT 1461
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
351-576 |
3.09e-44 |
|
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: 157.11 E-value: 3.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVM 430
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQ--DTFIFSGTIIENIRYG--KLDATEEEIIA-AAKVVRAHDfISGLKDgyytevkERGSTLSAGQRQLISFARALLAD 505
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpeNLGLPREEIRErVEEALELVG-LEHLAD-------RPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 506 PKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIA-HRLSTI-KNSSRIFYIDNGRIQEAGSHEELMAQH 576
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
106-577 |
1.45e-43 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 167.61 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 106 KDMRTAIFGHLQKLPFSYFDSRPHGKILIR-----------VVNYINMLsdllsnglINLISDILSVIVTLGFmlmidpV 174
Cdd:PLN03130 986 KRLHDAMLGSILRAPMSFFHTNPLGRIINRfakdlgdidrnVAVFVNMF--------LGQIFQLLSTFVLIGI------V 1051
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 175 LTLYSLALIPVL---FVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEI----------FTEV 241
Cdd:PLN03130 1052 STISLWAIMPLLvlfYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEIngrsmdnnirFTLV 1131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 242 SNEYRRsWMkAVKIQFLlwPGVqniavmttcLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIgnfyNSLITATTY 321
Cdd:PLN03130 1132 NMSSNR-WL-AIRLETL--GGL---------MIWLTASFAVMQNGRAENQAAFASTMGLLLSYALNI----TSLLTAVLR 1194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 322 L-----------ERIFETMDVEPDIKDIPNAKKMPP---IVGNVDFKDVYFRYE-EGVDILKGINFHVDAGESIALVGPT 386
Cdd:PLN03130 1195 LaslaenslnavERVGTYIDLPSEAPLVIENNRPPPgwpSSGSIKFEDVVLRYRpELPPVLHGLSFEISPSEKVGIVGRT 1274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 387 GAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENirygkLDATEEEIIAA--AKVV 464
Cdd:PLN03130 1275 GAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN-----LDPFNEHNDADlwESLE 1349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 465 RAHdfisgLKD-------GYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGR 537
Cdd:PLN03130 1350 RAH-----LKDvirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSC 1424
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 346645039 538 TSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHG 577
Cdd:PLN03130 1425 TMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
37-325 |
1.64e-42 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 154.51 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 37 ITLFVILLANVATMIGPYLTKIVIDDTIPNK-NMTQLFWIAVIFIVSVIVTGLCMRYrirsITLIGQDILKDMRTAIFGH 115
Cdd:cd18551 3 LALLLSLLGTAASLAQPLLVKNLIDALSAGGsSGGLLALLVALFLLQAVLSALSSYL----LGRTGERVVLDLRRRLWRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 116 LQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKT 195
Cdd:cd18551 79 LLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 196 AQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPgVQNIAVMTTcliy 275
Cdd:cd18551 159 RIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGP-LMGLAVQLA---- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 276 FVGIKGYGV------DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18551 234 LLVVLGVGGarvasgALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
37-325 |
1.89e-42 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 154.18 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 37 ITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd18543 3 LALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLInLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIkta 196
Cdd:cd18543 83 QRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPF-LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRF--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 qRKAYQVLS----NKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTC 272
Cdd:cd18543 159 -RRRYFPASrraqDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 273 LIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18543 238 AVLALG--GWLVangSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
354-563 |
3.04e-42 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 149.67 E-value: 3.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQ 432
Cdd:cd03246 4 ENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 DTFIFSGTIIENIrygkldateeeiiaaakvvrahdfisglkdgyytevkergstLSAGQRQLISFARALLADPKILILD 512
Cdd:cd03246 84 DDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 346645039 513 EATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
351-576 |
7.80e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 145.21 E-value: 7.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGVM 430
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRY-GKLDATEEEIIAAakvvRAHDFIS--GLKDgyytEVKERGSTLSAGQRQLISFARALLADP 506
Cdd:COG1131 79 PQEPALYPDlTVRENLRFfARLYGLPRKEARE----RIDELLElfGLTD----AADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEELMAQH 576
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
367-516 |
7.54e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 139.71 E-value: 7.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSG-TIIENI 445
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 446 RYGkldATEEEIIAAAKVVRAHDFIS--GLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATS 516
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
353-562 |
1.17e-38 |
|
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: 141.45 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVML 431
Cdd:cd03225 2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 Q--DTFIFSGTIIENIRYG--KLDATEEEIIAAAKVVRAHDFISGLKDgyytevkERGSTLSAGQRQLISFARALLADPK 507
Cdd:cd03225 82 QnpDDQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEGLRD-------RSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 508 ILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGR 562
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
353-567 |
2.52e-38 |
|
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: 139.37 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlRSLRSQMGVML 431
Cdd:cd03247 3 INNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 QDTFIFSGTIIENIrygkldateeeiiaaakvvrahdfisglkdgyytevkerGSTLSAGQRQLISFARALLADPKILIL 511
Cdd:cd03247 82 QRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 512 DEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAG 567
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
122-593 |
5.56e-38 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 150.70 E-value: 5.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 122 SYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDP-VLtlysLALIPVLFV---IVMVIKTAQ 197
Cdd:PTZ00243 1047 SFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPfVL----VALVPCGYLyyrLMQFYNSAN 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 198 RKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFE-------------IFTEVSNEyrrsWMkAVKIQFLlwpgvQ 264
Cdd:PTZ00243 1123 REIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQealrrldvvyscsYLENVANR----WL-GVRVEFL-----S 1192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 265 NIAVmttcliyfvgikgygvdvstgTLIAFIGYVGN-FWNPVINIGNFYNSLITATT------YLERIFETMD-----VE 332
Cdd:PTZ00243 1193 NIVV---------------------TVIALIGVIGTmLRATSQEIGLVSLSLTMAMQttatlnWLVRQVATVEadmnsVE 1251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 333 --------------PDIKDIPNAKK-----------------------MPPIV--GNVDFKDVYFRYEEGVD-ILKGINF 372
Cdd:PTZ00243 1252 rllyytdevphedmPELDEEVDALErrtgmaadvtgtvviepasptsaAPHPVqaGSLVFEGVQMRYREGLPlVLRGVSF 1331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 373 HVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRyGKLDA 452
Cdd:PTZ00243 1332 RIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEA 1410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 453 TEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILIL-DEATSSIDTQTEILLQEGLE 531
Cdd:PTZ00243 1411 SSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVM 1490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 532 RLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHgyyynlyQSQF-DMLQAL 593
Cdd:PTZ00243 1491 SAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR-------QSIFhSMVEAL 1546
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
356-588 |
6.84e-38 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 140.32 E-value: 6.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 356 VYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDT- 434
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 435 ------FIFSGTIIENIRYGKLDATEEEIIAAAKVVrahdfisGLKDGYYTEvkeRGSTLSAGQRQLISFARALLADPKI 508
Cdd:COG1124 90 aslhprHTVDRILAEPLRIHGLPDREERIAELLEQV-------GLPPSFLDR---YPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 509 LILDEATSSID--TQTEILlqegleRLLE------GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELM--AQHG 577
Cdd:COG1124 160 LLLDEPTSALDvsVQAEIL------NLLKdlreerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLagPKHP 233
|
250
....*....|.
gi 346645039 578 YYYNLYQSQFD 588
Cdd:COG1124 234 YTRELLAASLA 244
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
354-577 |
2.01e-36 |
|
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: 136.14 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRsLRSQMGVMLQD 433
Cdd:COG4555 5 ENLSKKYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 TFIFSG-TIIENIRY-GKL--DATEEEIIAAAKVVRAHDFISGLkdgyytevKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:COG4555 83 RGLYDRlTVRENIRYfAELygLFDEELKKRIEELIELLGLEEFL--------DRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQHG 577
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
351-578 |
2.37e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 142.35 E-value: 2.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYE----EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSL 423
Cdd:COG1123 261 LEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 424 RSQMGVMLQDTF--------IFSgTIIENIR-YGKLDATEeeiiAAAKVVRAHDFIsGLKdgyyTEVKER-GSTLSAGQR 493
Cdd:COG1123 341 RRRVQMVFQDPYsslnprmtVGD-IIAEPLRlHGLLSRAE----RRERVAELLERV-GLP----PDLADRyPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 494 QLISFARALLADPKILILDEATSSID--TQTEIL-----LQEGLerlleGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQE 565
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDvsVQAQILnllrdLQREL-----GLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
250
....*....|....*
gi 346645039 566 AGSHEELMA--QHGY 578
Cdd:COG1123 486 DGPTEEVFAnpQHPY 500
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
33-325 |
2.62e-36 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 137.19 E-value: 2.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 33 KSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:cd18570 2 KLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRV--VNYINmlsDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIV 190
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRFndANKIR---EAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILII 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 191 MVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLlwpgvQNIAVMT 270
Cdd:cd18570 159 LLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNL-----QSSIKGL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 271 TCLIYFVGIKGYGV------DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18570 234 ISLIGSLLILWIGSylvikgQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
349-575 |
1.50e-35 |
|
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: 134.27 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 349 GNVDFKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQM 427
Cdd:cd03288 18 GEIKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSGTIIENIRYGKlDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPK 507
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 508 ILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
351-574 |
1.73e-35 |
|
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: 133.40 E-value: 1.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQM 427
Cdd:cd03261 1 IELRGLTKSFGGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSG-TIIENI-----RYGKLDATEEEIIAAAKVVRAhdfisGLKDgyytEVKERGSTLSAGQRQLISFARA 501
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVafplrEHTRLSEEEIREIVLEKLEAV-----GLRG----AEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 502 LLADPKILILDEATSSID--TQTEIL-----LQEGLerlleGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEELM 573
Cdd:cd03261 151 LALDPELLLYDEPTAGLDpiASGVIDdlirsLKKEL-----GLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELR 225
|
.
gi 346645039 574 A 574
Cdd:cd03261 226 A 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
351-544 |
4.65e-35 |
|
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: 131.83 E-value: 4.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEG---VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVtlrslRSQM 427
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFS-GTIIENIRYGkLDATeeEIIAAAKVVRAHDFIS--GLKD--GYYTevkergSTLSAGQRQLISFARAL 502
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG-LELQ--GVPKAEARERAEELLElvGLSGfeNAYP------HQLSGGMRQRVALARAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 346645039 503 LADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAH 544
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTH 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
354-573 |
5.96e-35 |
|
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: 132.47 E-value: 5.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQD 433
Cdd:COG1120 5 ENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 TFI-FSGTIIENIRYG---------KLDATEEEIIAAA-KVVRahdfISGLKDGYYTEvkergstLSAGQRQLISFARAL 502
Cdd:COG1120 84 PPApFGLTVRELVALGryphlglfgRPSAEDREAVEEAlERTG----LEHLADRPVDE-------LSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 503 LADPKILILDEATSSID--TQTEILlqEGLERL--LEGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELM 573
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDlaHQLEVL--ELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
39-325 |
6.59e-35 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 133.38 E-value: 6.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 39 LFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQK 118
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 119 LPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQR 198
Cdd:cd18576 82 LPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 199 KAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEenFEI--FTEVSNEYRRSWMKAVKIQFLLWPGVqnIAVMTTCLIYF 276
Cdd:cd18576 162 KLSKKVQDELAEANTIVEETLQGIRVVKAFTRED--YEIerYRKALERVVKLALKRARIRALFSSFI--IFLLFGAIVAV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 346645039 277 VGIKGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18576 238 LWYGGRLVlagELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
353-562 |
7.39e-35 |
|
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: 128.90 E-value: 7.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQ 432
Cdd:cd00267 2 IENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 dtfifsgtiienirygkldateeeiiaaakvvrahdfisglkdgyytevkergstLSAGQRQLISFARALLADPKILILD 512
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 346645039 513 EATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKNSS-RIFYIDNGR 562
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
351-572 |
7.68e-35 |
|
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: 131.15 E-value: 7.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGvDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNIN-----SGEILVDGENV--EEVTLRSL 423
Cdd:cd03260 1 IELRDLNVYYGDK-HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 424 RSQMGVMLQDTFIFSGTIIENIRYG------KLDATEEEIIAAA--KVvrahdfisGLKDgyytEVKER--GSTLSAGQR 493
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEAlrKA--------ALWD----EVKDRlhALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 494 QLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEEL 572
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
33-325 |
2.06e-34 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 132.25 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 33 KSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:cd18555 2 KLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRvVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:cd18555 82 FEHLLKLPYSFFENRSSGDLLFR-ANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 193 IKTAQRKAYQVLSNKQSNMNAYIHE---SIAGIKVT----QSFSREEENFEifTEVSNEYRRSwmkavKIQFLLWPGVQN 265
Cdd:cd18555 161 TRKKIKKLNQEEIVAQTKVQSYLTEtlyGIETIKSLgsekNIYKKWENLFK--KQLKAFKKKE-----RLSNILNSISSS 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 266 IAVMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18555 234 IQFIAPLLILWIGaylvING---ELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
39-325 |
4.31e-34 |
|
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: 131.14 E-value: 4.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 39 LFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQK 118
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 119 LPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQR 198
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 199 KAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIF-TEVSNEYRRSWMKAVkiQFLLWPGVQNIAVM-TTCLIYF 276
Cdd:cd18557 162 KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYsEALDRSYRLARKKAL--ANALFQGITSLLIYlSLLLVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 346645039 277 VGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18557 240 YG--GYLVlsgQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-575 |
5.34e-34 |
|
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: 138.50 E-value: 5.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 10 EELETAFSAAHLKRILVYVKPYQKSIY--ITLFVILLANVA-TMIG-------PYLTKIVIDDT-------------IPN 66
Cdd:TIGR01271 842 DERENVFETTTWNTYLRYITTNRNLVFvlIFCLVIFLAEVAaSLLGlwlitdnPSAPNYVDQQHanasspdvqkpviITP 921
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 67 KNMTQLFWIAVIFIVSVIVTGLcmrYR----IRSITLIGQDILKDMRTAIFghlqKLPFSYFDSRPHGKILIRVVNYINM 142
Cdd:TIGR01271 922 TSAYYIFYIYVGTADSVLALGF---FRglplVHTLLTVSKRLHEQMLHSVL----QAPMAVLNTMKAGRILNRFTKDMAI 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 143 LSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLyslALIPVLFVIVMV----IKTAQrKAYQVLSNKQSNMNAYIHES 218
Cdd:TIGR01271 995 IDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFI---AAIPVAVIFIMLrayfLRTSQ-QLKQLESEARSPIFSHLITS 1070
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 219 IAGIKVTQSFSREEENFEIFTEVSNEYRRSWMkaVKIQFLLWpgvqniaVMTTCLIYFVGIKGYGVDVSTGTLIAFIGYV 298
Cdd:TIGR01271 1071 LKGLWTIRAFGRQSYFETLFHKALNLHTANWF--LYLSTLRW-------FQMRIDIIFVFFFIAVTFIAIGTNQDGEGEV 1141
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 299 GNFWNPVINI-GNFYNSLITATTY------LERIFETMDVEPD-----------------IKDIPNAKKMPPIVGNVDFK 354
Cdd:TIGR01271 1142 GIILTLAMNIlSTLQWAVNSSIDVdglmrsVSRVFKFIDLPQEeprpsggggkyqlstvlVIENPHAQKCWPSGGQMDVQ 1221
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 355 DVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNiNSGEILVDGENVEEVTLRSLRSQMGVMLQD 433
Cdd:TIGR01271 1222 GLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQK 1300
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 TFIFSGTIIENI----RYgkldaTEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:TIGR01271 1301 VFIFSGTFRKNLdpyeQW-----SDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
351-571 |
7.80e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.25 E-value: 7.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeeVTLRS-----LRS 425
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL--SRLKRreipyLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 426 QMGVMLQDT-FIFSGTIIENIRYGkLDATEEEIIAAAKvvRAHDFIS--GLKDgyytevKERG--STLSAGQRQLISFAR 500
Cdd:COG2884 80 RIGVVFQDFrLLPDRTVYENVALP-LRVTGKSRKEIRR--RVREVLDlvGLSD------KAKAlpHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 501 ALLADPKILILDEATSSIDTQT--EILlqEGLERLLEGRTSFIIA-HRLSTIKNS-SRIFYIDNGRIQEAGSHEE 571
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETswEIM--ELLEEINRRGTTVLIAtHDLELVDRMpKRVLELEDGRLVRDEARGV 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
351-574 |
1.26e-33 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 128.17 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV---EEVTLRSLRSQM 427
Cdd:COG1127 6 IEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSG-TIIENI-----RYGKLDATEEEIIAAAKVVRAhdfisGLKD--GYYTevkergSTLSAGQRQLISFA 499
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVafplrEHTDLSEAEIRELVLEKLELV-----GLPGaaDKMP------SELSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 500 RALLADPKILILDEATSSID--TQTEI--LLQEGLERLleGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDpiTSAVIdeLIRELRDEL--GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
35-330 |
2.14e-33 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 129.46 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMT------QLFWIAVI-FIVSVIVTGLCMRYRIRSITLIGQDILKD 107
Cdd:cd18554 1 IIITIVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTldekvyKLFTIIGImFFIFLILRPPVEYYRQYFAQWIANKILYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 108 MRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLF 187
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 188 VIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIA 267
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTIT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 268 VMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVinignfyNSLITATTYLERIFETMD 330
Cdd:cd18554 241 DLAPLLVIGFAaylvIEG---NLTVGTLVAFVGYMERMYSPL-------RRLVNSFTTLTQSFASMD 297
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
351-574 |
2.31e-33 |
|
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: 127.80 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVM 430
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIR-YGKLDATEEEIIAAakvvRAHDFIS--GLKDGYYtevKER-GSTLSAGQRQLISFARALLAD 505
Cdd:cd03295 81 IQQIGLFPHmTVEENIAlVPKLLKWPKEKIRE----RADELLAlvGLDPAEF---ADRyPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 506 PKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRL-STIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
351-562 |
4.26e-33 |
|
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: 125.66 E-value: 4.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVD----ILKGINFHVDAGESIALVGPTGAGKTTIIN-LLsrfyninsGEI-LVDGEnveevtlRSLR 424
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLL--------GELeKLSGS-------VSVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQDTFIFSGTIIENIRYGK-LDATEEEiiaaaKVVRA---HDFISGLKDGYYTEVKERGSTLSAGQRQLISFAR 500
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFGKpFDEERYE-----KVIKAcalEPDLEILPDGDLTEIGEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 501 ALLADPKILILDEATSSIDTQTEILLQEG--LERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGR 562
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
351-567 |
5.92e-33 |
|
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: 125.71 E-value: 5.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRslRSQMGVM 430
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRYG------KLDATEEEIIAAAKVVRAHDFIsglkdgyytevKERGSTLSAGQRQLISFARALL 503
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLL-----------NRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 504 ADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAG 567
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
344-544 |
1.08e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 126.36 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 344 MPPIVGNVDFKDVYFRY---EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTL 420
Cdd:COG1116 1 MSAAAPALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 421 RslrsqMGVMLQDtfiFS----GTIIENIRYG--KLDATEEEIIAaakvvRAHDFIS--GLKD--GYYTevkergSTLSA 490
Cdd:COG1116 81 D-----RGVVFQE---PAllpwLTVLDNVALGleLRGVPKAERRE-----RARELLElvGLAGfeDAYP------HQLSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 491 GQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAH 544
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTH 197
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
353-576 |
1.25e-32 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 125.37 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQMGV 429
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQD-TFIFSGTIIENIRYGKLDA-----------TEEEIIAAAKVVRAhdfiSGLKDGYYTevkeRGSTLSAGQRQLIS 497
Cdd:cd03256 83 IFQQfNLIERLSVLENVLSGRLGRrstwrslfglfPKEEKQRALAALER----VGLLDKAYQ----RADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 498 FARALLADPKILILDEATSSIDTQT-----EILLQEGLErllEGRTSFIIAHRLSTIK-NSSRIFYIDNGRIQEAGSHEE 571
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASsrqvmDLLKRINRE---EGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAE 231
|
....*
gi 346645039 572 LMAQH 576
Cdd:cd03256 232 LTDEV 236
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
344-565 |
2.75e-32 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 124.00 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 344 MPPIVgnvDFKDVYFRYEEG---VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVE---E 417
Cdd:COG1136 1 MSPLL---ELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslsE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 418 VTLRSLRSQ-MGVMLQDTFIFSG-TIIENI----RYGKLDATE--EEIIAAAKVVrahdfisGLKDgyytEVKERGSTLS 489
Cdd:COG1136 78 RELARLRRRhIGFVFQFFNLLPElTALENValplLLAGVSRKErrERARELLERV-------GLGD----RLDHRPSQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 490 AGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFIIA-HRLSTIKNSSRIFYIDNGRIQE 565
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
354-563 |
5.06e-32 |
|
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: 121.74 E-value: 5.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGVMLQD 433
Cdd:cd03230 4 RNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 TFIFSG-TIIENIRYgkldateeeiiaaakvvrahdfisglkdgyytevkergstlSAGQRQLISFARALLADPKILILD 512
Cdd:cd03230 82 PSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 346645039 513 EATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
351-575 |
8.05e-32 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 123.07 E-value: 8.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEG---VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLR 424
Cdd:cd03258 2 IELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQDTFIFSG-TIIENIRYG-KLDATEEEIIAAaKVVRAHDFIsGLKDgyytEVKERGSTLSAGQRQLISFARAL 502
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPlEIAGVPKAEIEE-RVLELLELV-GLED----KADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 503 LADPKILILDEATSSIDTQTEillQEGLERLLE-----GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETT---QSILALLRDinrelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
356-567 |
8.57e-32 |
|
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: 122.61 E-value: 8.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 356 VYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQMGVML 431
Cdd:cd03257 9 VSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 QDTF-----IFS-GTIIENI--RYGKLDATEEEIIAAAKVVRAHdfisGLKDGYYtevKERGSTLSAGQRQLISFARALL 503
Cdd:cd03257 89 QDPMsslnpRMTiGEQIAEPlrIHGKLSKKEARKEAVLLLLVGV----GLPEEVL---NRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 504 ADPKILILDEATSSID--TQTEIL-----LQEGLerlleGRTSFIIAHRLSTIKNSS-RIFYIDNGRIQEAG 567
Cdd:cd03257 162 LNPKLLIADEPTSALDvsVQAQILdllkkLQEEL-----GLTLLFITHDLGVVAKIAdRVAVMYAGKIVEEG 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
351-562 |
1.52e-31 |
|
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: 120.37 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV--EEVTLRSLRSQMG 428
Cdd:cd03229 1 LELKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQDTFIFSG-TIIENIRYGkldateeeiiaaakvvrahdfisglkdgyytevkergstLSAGQRQLISFARALLADPK 507
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 508 ILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGR 562
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
343-584 |
2.21e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.12 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 343 KMPPIVgnvDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVtlrs 422
Cdd:COG1121 2 MMMPAI---ELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 423 lRSQMGVMLQDT------------FIFSGTIIENIRYGKLDATEEEIIAAA-KVVRAHDFIsglkdgyytevKERGSTLS 489
Cdd:COG1121 74 -RRRIGYVPQRAevdwdfpitvrdVVLMGRYGRRGLFRRPSRADREAVDEAlERVGLEDLA-----------DRPIGELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 490 AGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTI-KNSSRIFYIDNGRI---- 563
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVrEYFDRVLLLNRGLVahgp 221
|
250 260
....*....|....*....|..
gi 346645039 564 -QEAGSHEELMAQHGYYYNLYQ 584
Cdd:COG1121 222 pEEVLTPENLSRAYGGPVALLA 243
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
344-576 |
2.42e-31 |
|
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: 127.71 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 344 MPPIVgnvDFKDVYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNIN---SGEILVDGENVEEVT 419
Cdd:COG1123 1 MTPLL---EVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 420 LRSLRSQMGVMLQD--TFIFSGTIIENIRYG--KLDATEEEIIAAAKVVRAHDFISGLKDGYYTEvkergstLSAGQRQL 495
Cdd:COG1123 78 EALRGRRIGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYPHQ-------LSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 496 ISFARALLADPKILILDEATSSID--TQTEILlqEGLERLLE--GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHE 570
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDvtTQAEIL--DLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPE 228
|
....*.
gi 346645039 571 ELMAQH 576
Cdd:COG1123 229 EILAAP 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
351-573 |
2.97e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVE--EVTLRSLRSQMG 428
Cdd:PRK09493 2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQDTFIFSG-TIIENIRYG--------KLDATEEEIIAAAKV---VRAHDFisglkdgyytevkerGSTLSAGQRQLI 496
Cdd:PRK09493 81 MVFQQFYLFPHlTALENVMFGplrvrgasKEEAEKQARELLAKVglaERAHHY---------------PSELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 497 SFARALLADPKILILDEATSSIDTQteiLLQEGLE--RLL--EGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEE 571
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPE---LRHEVLKvmQDLaeEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQV 222
|
..
gi 346645039 572 LM 573
Cdd:PRK09493 223 LI 224
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
35-305 |
3.25e-31 |
|
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: 122.37 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNM--TQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPetQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 193 IKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTC 272
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 346645039 273 LIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPV 305
Cdd:pfam00664 241 LALWFGaylvISG---ELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
354-567 |
6.17e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 118.69 E-value: 6.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQd 433
Cdd:cd03214 3 ENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 tfifsgtiienirygkldateeeiiaAAKVVRahdfISGLKDGYYTEvkergstLSAGQRQLISFARALLADPKILILDE 513
Cdd:cd03214 81 --------------------------ALELLG----LAHLADRPFNE-------LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 514 ATSSIDTQTEILLQEGLERL--LEGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAG 567
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
351-563 |
9.05e-31 |
|
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: 119.52 E-value: 9.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEG---VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVE---EVTLRSLR 424
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklsEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 -SQMGvmlqdtFIFSG-------TIIENIRYG------KLDATEEEIIAAAKVVrahdfisGLKDgyytEVKERGSTLSA 490
Cdd:cd03255 81 rRHIG------FVFQSfnllpdlTALENVELPlllagvPKKERRERAEELLERV-------GLGD----RLNHYPSELSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 491 GQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERL--LEGRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
37-325 |
2.88e-29 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 117.50 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 37 ITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTA 196
Cdd:cd18548 83 QSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYF 276
Cdd:cd18548 163 AIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILW 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 346645039 277 VGikGYGVD---VSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18548 243 FG--GHLINagsLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
349-575 |
4.16e-29 |
|
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: 116.49 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 349 GNVDFKDVYFRY-EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINsGEILVDGENVEEVTLRSLRSQM 427
Cdd:cd03289 1 GQMTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSGTIIENIR-YGKLdaTEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADP 506
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
366-543 |
5.73e-29 |
|
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: 114.11 E-value: 5.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlRSLRSQMGVMLQDTFIFSG-TIIEN 444
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPElTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRY----GKLDATEEEIIAAAKVVRahdfISGLKDgyytevkERGSTLSAGQRQLISFARALLADPKILILDEATSSIDT 520
Cdd:COG4133 96 LRFwaalYGLRADREAIDEALEAVG----LAGLAD-------LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA 164
|
170 180
....*....|....*....|...
gi 346645039 521 QTEILLQEGLERLLEGRTSFIIA 543
Cdd:COG4133 165 AGVALLAELIAAHLARGGAVLLT 187
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
351-573 |
1.07e-28 |
|
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: 114.80 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSG-EILVDGENVEEVTLRSLRSQMGV 429
Cdd:COG1119 4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 M---LQDTFIFSGTIIENIRYGKLD-------ATEEEIIAAAKVVRAHDfISGLKDGYYTevkergsTLSAGQRQLISFA 499
Cdd:COG1119 83 VspaLQLRFPRDETVLDVVLSGFFDsiglyrePTDEQRERARELLELLG-LAHLADRPFG-------TLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 500 RALLADPKILILDEATSSID-TQTEILLQEgLERL-LEGRTSFI-IAHRLSTIKNS-SRIFYIDNGRIQEAGSHEELM 573
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDlGARELLLAL-LDKLaAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
366-563 |
5.18e-28 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 111.47 E-value: 5.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV--EEVTLRSLRSQMGVMLQDTFIFSG-TII 442
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYG--------KLDATEEEIIAAAKVvrahdfisGLKD--GYYTevkergSTLSAGQRQLISFARALLADPKILILD 512
Cdd:cd03262 95 ENITLApikvkgmsKAEAEERALELLEKV--------GLADkaDAYP------AQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 513 EATSSIDTQteiLLQEGLERLL----EGRTSFIIAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:cd03262 161 EPTSALDPE---LVGEVLDVMKdlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
354-563 |
1.46e-27 |
|
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: 110.04 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvtlRSLRSQMGVMLQD 433
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 T--FIFSGTIIENIRYGkLDATEEEIIAAAKVVRAHDfISGLKDgyytevkERGSTLSAGQRQLISFARALLADPKILIL 511
Cdd:cd03226 80 VdyQLFTDSVREELLLG-LKELDAGNEQAETVLKDLD-LYALKE-------RHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 346645039 512 DEATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
353-561 |
2.01e-27 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 109.93 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVtlrslRSQMGVMLQ 432
Cdd:cd03235 2 VEDLTVSYGGHP-VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 DTFI---FSGTIIENI---RYGKL-------DATEEEIIAAAKVVRAHDFIsglkdgyytevKERGSTLSAGQRQLISFA 499
Cdd:cd03235 76 RRSIdrdFPISVRDVVlmgLYGHKglfrrlsKADKAKVDEALERVGLSELA-----------DRQIGELSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 500 RALLADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRLSTI-KNSSRIFYIDNG 561
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
363-574 |
2.41e-27 |
|
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: 109.83 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSlRSQMGVML--QDTFIFSG- 439
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGIGYvpEGRRIFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIRYG-------KLDATEEEIIAaakvvrahdfisglkdgYYTEVKER----GSTLSAGQRQLISFARALLADPKI 508
Cdd:cd03224 91 TVEENLLLGayarrraKRKARLERVYE-----------------LFPRLKERrkqlAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 509 LILDEATS----SIDTQTEILLQEgLERllEGRTSFIIAHRLSTIKNSSRIFYI-DNGRIQEAGSHEELMA 574
Cdd:cd03224 154 LLLDEPSEglapKIVEEIFEAIRE-LRD--EGVTILLVEQNARFALEIADRAYVlERGRVVLEGTAAELLA 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
363-574 |
8.42e-27 |
|
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: 109.06 E-value: 8.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEevTLRS-LRSQMGV--MLQDTFIFSG 439
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT--GLPPhEIARLGIgrTFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 -TIIENIR----------YGKLDATEEEIIAAAKVVRAHDFIsGLKDGYYTEVkergSTLSAGQRQLISFARALLADPKI 508
Cdd:cd03219 90 lTVLENVMvaaqartgsgLLLARARREEREARERAEELLERV-GLADLADRPA----GELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 509 LILDEATSSIdTQTEIllQEGLERLLE----GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:cd03219 165 LLLDEPAAGL-NPEET--EELAELIRElrerGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
351-572 |
8.43e-27 |
|
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: 108.86 E-value: 8.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeeVTLRSLRSQMGVM 430
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRYG-KLDATEEEIIaAAKVVRAHDFI--SGLKDGYYTEvkergstLSAGQRQLISFARALLADP 506
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlRLKKLPKAEI-KERVAEALDLVqlEGYANRKPSQ-------LSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
351-563 |
8.49e-27 |
|
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: 108.26 E-value: 8.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRS---LRSQM 427
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDT-FIFSGTIIENIRYGkLDATEEEIIAAAKVVRAHDFISGLKDgyytevKERG--STLSAGQRQLISFARALLA 504
Cdd:cd03292 81 GVVFQDFrLLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSH------KHRAlpAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 505 DPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKN--SSRIFYIDNGRI 563
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
367-571 |
1.75e-26 |
|
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: 107.81 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeeVTLRSLRSQMGVMLQDTFIFSG-TIIENI 445
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPPEKRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 RYGKLDATEEEIIAAAKVVRAHDF--ISGLKDGYYTevkergsTLSAGQRQLISFARALLADPKILILDEATSSIDTQTE 523
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEMlgIDHLLNRKPE-------TLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 346645039 524 ILLQEGLERLL-EGRTSFI-IAHRLSTIKN-SSRIFYIDNGRIQEAGSHEE 571
Cdd:cd03299 166 EKLREELKKIRkEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
59-325 |
5.55e-26 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 108.42 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 59 VIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcMRYrIRSITL--IGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRV 136
Cdd:cd18565 40 VPASLGPADPRGQLWLLGGLTVAAFLLESL-FQY-LSGVLWrrFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 137 VNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIH 216
Cdd:cd18565 118 NNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 217 ESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQ---NIAVMTTCLI--YFV--GIKGYGVDVSTG 289
Cdd:cd18565 198 NNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRlvaGAGFVATFVVggYWVldGPPLFTGTLTVG 277
|
250 260 270
....*....|....*....|....*....|....*.
gi 346645039 290 TLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18565 278 TLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
353-576 |
1.01e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.61 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEegvDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeevtLRSLRSQMGV-ML 431
Cdd:COG3840 4 LDDLTYRYG---DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL----TALPPAERPVsML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 -QDTFIFSG-TIIENIRYG-----KLDATE-EEIIAAAKVVRahdfISGLKDgyytevkERGSTLSAGQRQLISFARALL 503
Cdd:COG3840 77 fQENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALERVG----LAGLLD-------RLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 504 ADPKILILDEATSSIDTqteILLQEGLERLLE-----GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQH 576
Cdd:COG3840 146 RKRPILLLDEPFSALDP---ALRQEMLDLVDElcrerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
363-574 |
1.16e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.99 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTI---INLLSRFYN--INSGEILVDGE---NVEEVTLRSLRSQMGVMLQDT 434
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLEQPEAgtIRVGDITIDTArslSQQKGLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 435 FIFSG-TIIENIRYGKL---DATEEEIIAAAKVVRAHDFISGLKDGYytevkerGSTLSAGQRQLISFARALLADPKILI 510
Cdd:PRK11264 95 NLFPHrTVLENIIEGPVivkGEPKEEATARARELLAKVGLAGKETSY-------PRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 511 LDEATSSIDTQteiLLQEGLE--RLL--EGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK11264 168 FDEPTSALDPE---LVGEVLNtiRQLaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
354-574 |
1.48e-25 |
|
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: 105.45 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeeVTLRS-LRSQMGVML- 431
Cdd:COG0410 7 ENLHAGYGG-IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI--TGLPPhRIARLGIGYv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 -QDTFIFSG-TIIENIRygkldateeeiiAAAKVVRAHDFISGLKDGYYT---EVKER----GSTLSAGQRQLISFARAL 502
Cdd:COG0410 84 pEGRRIFPSlTVEENLL------------LGAYARRDRAEVRADLERVYElfpRLKERrrqrAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 503 LADPKILILDEAT-----SSIDTQTEILLQ---EGLERLL-EGRTSFI--IAHRlstiknssriFYI-DNGRIQEAGSHE 570
Cdd:COG0410 152 MSRPKLLLLDEPSlglapLIVEEIFEIIRRlnrEGVTILLvEQNARFAleIADR----------AYVlERGRIVLEGTAA 221
|
....
gi 346645039 571 ELMA 574
Cdd:COG0410 222 ELLA 225
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
364-578 |
1.88e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 107.51 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 364 VDilkGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQMGVMLQDTfifsgt 440
Cdd:COG4608 34 VD---GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 iienirYGKLDA--TEEEIIAAAkvVRAHdfisGLKDGyyTEVKERGSTL------------------SAGQRQLISFAR 500
Cdd:COG4608 105 ------YASLNPrmTVGDIIAEP--LRIH----GLASK--AERRERVAELlelvglrpehadryphefSGGQRQRIGIAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 501 ALLADPKILILDEATSSIDT--QTEIL-----LQEGLerlleGRTSFIIAHRLSTIKN-SSRI--FYIdnGRIQEAGSHE 570
Cdd:COG4608 171 ALALNPKLIVCDEPVSALDVsiQAQVLnlledLQDEL-----GLTYLFISHDLSVVRHiSDRVavMYL--GKIVEIAPRD 243
|
250
....*....|
gi 346645039 571 ELMA--QHGY 578
Cdd:COG4608 244 ELYArpLHPY 253
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
351-572 |
1.90e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 107.88 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT--LRslrsQMG 428
Cdd:COG3842 6 LELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpeKR----NVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQDTFIFSG-TIIENIRYG----KLDATE-EEIIAAA-KVVRahdfISGLKDGYytevkerGSTLSAGQRQLISFARA 501
Cdd:COG3842 81 MVFQDYALFPHlTVAENVAFGlrmrGVPKAEiRARVAELlELVG----LEGLADRY-------PHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 502 LLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLS---TIknSSRIFYIDNGRIQEAGSHEEL 572
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
351-575 |
2.10e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.47 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEG---VDILKGINFHVDAGESIALVGPTGAGKTT---IINLLSRFyniNSGEILVDGENVEEVT---LR 421
Cdd:COG1135 2 IELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLERP---TSGSVLVDGVDLTALSereLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 422 SLRSQMGVmlqdtfIF-------SGTIIENI----RYGKLDAteEEIiaAAKVVRAHDFIsGLKD--GYYTevkergSTL 488
Cdd:COG1135 79 AARRKIGM------IFqhfnllsSRTVAENValplEIAGVPK--AEI--RKRVAELLELV-GLSDkaDAYP------SQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 489 SAGQRQLISFARALLADPKILILDEATSSIDTQT--EIL--LQEGLERLleGRTSFIIAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETtrSILdlLKDINREL--GLTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
250
....*....|..
gi 346645039 564 QEAGSHEELMAQ 575
Cdd:COG1135 220 VEQGPVLDVFAN 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
363-546 |
3.33e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSLRS--QMGVML--QDTFIFS 438
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSPRDaqAAGIAIihQELNLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 G-TIIENI-------RYGKLDaTEEEIIAAAKVVRAHDF-ISglkdgyyteVKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:COG1129 93 NlSVAENIflgreprRGGLID-WRAMRRRARELLARLGLdID---------PDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 346645039 510 ILDEATSSIdTQTEIllqeglERLLE--------GRTSFIIAHRL 546
Cdd:COG1129 163 ILDEPTASL-TEREV------ERLFRiirrlkaqGVAIIYISHRL 200
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
363-574 |
5.89e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 104.35 E-value: 5.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeeVTLRS-LRSQMGV--MLQDTFIFSG 439
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI--TGLPPhRIARLGIarTFQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 -TIIENI--------RYGKLDAT-------EEEIIAAAKVVRAHDFIsGLKDgyytEVKERGSTLSAGQRQLISFARALL 503
Cdd:COG0411 94 lTVLENVlvaaharlGRGLLAALlrlprarREEREARERAEELLERV-GLAD----RADEPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 504 ADPKILILDEATSSIdTQTEIllqEGLERLL------EGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:COG0411 169 TEPKLLLLDEPAAGL-NPEET---EELAELIrrlrdeRGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-582 |
8.20e-25 |
|
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: 110.04 E-value: 8.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 4 NKFDIDEELETAFSAAHLKR-----ILVYVKPYQKSIYITLFVILLANVATMIGPYLTKIVI----DDTIPNknmTQLFW 74
Cdd:TIGR00957 283 SQLDANEEVEALIVKSPHKPrkpslFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIrfvnDPMAPD---WQGYF 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 75 IAVIFIVSVIVTGLCMRYRIRSITLIGQDIlkdmRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINM----LSDLLSng 150
Cdd:TIGR00957 360 YTGLLFVCACLQTLILHQYFHICFVSGMRI----KTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVdaqrFMDLAT-- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 151 LINLI-SDILSVIVTLGFM-LMIDP-VLTLYSLALIPVLFVIVMVIKTaqrKAYQVLSNK-QSNMNAYIHESIAGIKVTQ 226
Cdd:TIGR00957 434 YINMIwSAPLQVILALYFLwLNLGPsVLAGVAVMVLMVPLNAVMAMKT---KTYQVAHMKsKDNRIKLMNEILNGIKVLK 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 227 SFSREEEnfeiFTEVSNEYRRSWMKAVKIQFLLwpgvqniAVMTT----CLIYFVGIKGYGVDVST---GTLIAFIGYVG 299
Cdd:TIGR00957 511 LYAWELA----FLDKVEGIRQEELKVLKKSAYL-------HAVGTftwvCTPFLVALITFAVYVTVdenNILDAEKAFVS 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 300 -NFWN----PVINIGNFYNSLITATTYLERIFETMDVEPDIKDIPNAKKMPPIVGN-VDFKDVYFRYEEGVD-ILKGINF 372
Cdd:TIGR00957 580 lALFNilrfPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNsITVHNATFTWARDLPpTLNGITF 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 373 HVDAGESIALVGPTGAGKTTIINLLsrfyninsgeiLVDGENVE-EVTLRSlrsQMGVMLQDTFIFSGTIIENIRYGKld 451
Cdd:TIGR00957 660 SIPEGALVAVVGQVGCGKSSLLSAL-----------LAEMDKVEgHVHMKG---SVAYVPQQAWIQNDSLRENILFGK-- 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 452 ATEEEIIAAakVVRAHDFISGLK---DGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQE 528
Cdd:TIGR00957 724 ALNEKYYQQ--VLEACALLPDLEilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 529 ---GLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQHGYYYNL 582
Cdd:TIGR00957 802 hviGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
351-572 |
9.64e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.05 E-value: 9.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVM 430
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQ--DTFIFSGTIIENIRYGKL------DATEEEIIAAAKVVRAHDFISglKDGYYtevkergstLSAGQRQLISFARAL 502
Cdd:PRK13647 85 FQdpDDQVFSSTVWDDVAFGPVnmgldkDEVERRVEEALKAVRMWDFRD--KPPYH---------LSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 503 LADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
367-572 |
1.73e-24 |
|
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: 102.42 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRslRSQMGVMLQDTFIFSG-TIIENI 445
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 RYG------KLDATEEEIiaAAKVVRAHDFI--SGLKDGYYTEvkergstLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:cd03296 96 AFGlrvkprSERPPEAEI--RAKVHELLKLVqlDWLADRYPAQ-------LSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 518 IDTQTEILLQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
356-578 |
2.91e-24 |
|
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: 103.59 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 356 VYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTT----IINLLSRfYNINSGEILVDGENVEEVT---LRSLR-SQ 426
Cdd:COG0444 9 VYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTlaraILGLLPP-PGITSGEILFDGEDLLKLSekeLRKIRgRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 427 MGVMLQDTF--------IfsGTII-ENIRY-GKLDATE--EEIIAAAKVVrahdfisGLkdgyyTEVKERGS----TLSA 490
Cdd:COG0444 88 IQMIFQDPMtslnpvmtV--GDQIaEPLRIhGGLSKAEarERAIELLERV-------GL-----PDPERRLDryphELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 491 GQRQLISFARALLADPKILILDEATSSID--TQTEIL-----LQEglerllEGRTSFI-IAHRLSTIKN-SSRI--FYid 559
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDvtIQAQILnllkdLQR------ELGLAILfITHDLGVVAEiADRVavMY-- 225
|
250 260
....*....|....*....|.
gi 346645039 560 NGRIQEAGSHEELMA--QHGY 578
Cdd:COG0444 226 AGRIVEEGPVEELFEnpRHPY 246
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
367-567 |
8.66e-24 |
|
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: 99.60 E-value: 8.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeeVTLRSLRSQMGVMLqDTFIFSG--TIIEN 444
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALI-EAPGFYPnlTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IR-----YGKLDATEEEIIAaakvvrahdfISGLKDgyytEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:cd03268 93 LRllarlLGIRKKRIDEVLD----------VVGLKD----SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 346645039 520 TQTEILLQEGLERLL-EGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAG 567
Cdd:cd03268 159 PDGIKELRELILSLRdQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
350-578 |
1.03e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 105.15 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 350 NVDF---KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTT----IINLLSrfyniNSGEILVDGENVEEVT--- 419
Cdd:COG4172 282 KVWFpikRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIP-----SEGEIRFDGQDLDGLSrra 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 420 LRSLRSQMGVMLQDTF-IFS-----GTIIE---NIRYGKLDATE-EEIIAAA--KVvrahdfisGLKDG----YYTEvke 483
Cdd:COG4172 357 LRPLRRRMQVVFQDPFgSLSprmtvGQIIAeglRVHGPGLSAAErRARVAEAleEV--------GLDPAarhrYPHE--- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 484 rgstLSAGQRQLISFARALLADPKILILDEATSSID--TQTEIL-----LQE--GLERLLegrtsfiIAHRLSTIKN-SS 553
Cdd:COG4172 426 ----FSGGQRQRIAIARALILEPKLLVLDEPTSALDvsVQAQILdllrdLQRehGLAYLF-------ISHDLAVVRAlAH 494
|
250 260
....*....|....*....|....*..
gi 346645039 554 RIFYIDNGRIQEAGSHEELMA--QHGY 578
Cdd:COG4172 495 RVMVMKDGKVVEQGPTEQVFDapQHPY 521
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
33-301 |
1.52e-23 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 101.00 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 33 KSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAI 112
Cdd:cd18567 2 RALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRVvNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:cd18567 82 FRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 193 IKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFtevSNEYRRSWMKAVKIQFL---------LWPGV 263
Cdd:cd18567 161 LYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARW---LNLLVDAINADIRLQRLqilfsaangLLFGL 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 346645039 264 QNIAVmttclIYFVGIKGYGVDVSTGTLIAFIGYVGNF 301
Cdd:cd18567 238 ENILV-----IYLGALLVLDGEFTVGMLFAFLAYKDQF 270
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
351-575 |
1.99e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.47 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI-LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGV 429
Cdd:PRK13635 6 IRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQ--DTFIFSGTIIENIRYG------KLDATEEEIIAAAKVVRAHDFIsglkdgyytevKERGSTLSAGQRQLISFARA 501
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGlenigvPREEMVERVDQALRQVGMEDFL-----------NREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 502 LLADPKILILDEATSSIDTQTEillQEGLE--RLL--EGRTSFI-IAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGR---REVLEtvRQLkeQKGITVLsITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
351-575 |
2.31e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.19 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVD--ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMG 428
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQ--DTFIFSGTIIENIRYG------KLDATEEEIIAAAKVVRAHDFisglkdgyytevKERG-STLSAGQRQLISFA 499
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDF------------KEREpARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 500 RALLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
370-575 |
2.58e-23 |
|
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: 99.64 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQ-MGVMLQDTFIFSG-TIIEN 444
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLPHrTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRYGkLD----ATEEEIIAAAKVVRAhdfiSGLKDGYYTEVKErgstLSAGQRQLISFARALLADPKILILDEATSSIDT 520
Cdd:cd03294 123 VAFG-LEvqgvPRAEREERAAEALEL----VGLEGWEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 521 QTEILLQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:cd03294 194 LIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
363-563 |
4.58e-23 |
|
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: 95.96 E-value: 4.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSLRsqmgvmlqdtfifsgtii 442
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPR------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 enirygklDAteeeiiAAAKVVRAHDfisglkdgyytevkergstLSAGQRQLISFARALLADPKILILDEATSSI-DTQ 521
Cdd:cd03216 71 --------DA------RRAGIAMVYQ-------------------LSVGERQMVEIARALARNARLLILDEPTAALtPAE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 346645039 522 TEILLQEgLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:cd03216 118 VERLFKV-IRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
351-572 |
5.53e-23 |
|
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: 97.58 E-value: 5.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI-LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGV 429
Cdd:cd03263 1 LQIRNLTKTYKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTFIFSG-TIIENIR-YGKLDATEEEIIAAAkvvrAHDFISGLKDGYYteVKERGSTLSAGQRQLISFARALLADPK 507
Cdd:cd03263 80 CPQFDALFDElTVREHLRfYARLKGLPKSEIKEE----VELLLRVLGLTDK--ANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 508 ILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEEL 572
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
351-572 |
5.88e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 100.53 E-value: 5.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRslRSQMGVM 430
Cdd:COG3839 4 LELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIF-SGTIIENIRYG----KLDATE--EEIIAAAKVVRahdfISGLKDgyytevkERGSTLSAGQRQLISFARALL 503
Cdd:COG3839 81 FQSYALYpHMTVYENIAFPlklrKVPKAEidRRVREAAELLG----LEDLLD-------RKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 504 ADPKILILDEATSSID----TQTEILLQEGLERLlegRTSFIIA-HRLS---TIknSSRIFYIDNGRIQEAGSHEEL 572
Cdd:COG3839 150 REPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL---GTTTIYVtHDQVeamTL--ADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
362-567 |
6.36e-23 |
|
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: 97.60 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 362 EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenveevTLRSLRSqMGVMLQDTFifsgTI 441
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLG-LGGGFNPEL----TG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IENIRYGK--LDATEEEIiaAAKVVRAHDFiSGLKDGYYTEVKergsTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:cd03220 102 RENIYLNGrlLGLSRKEI--DEKIDEIIEF-SELGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 346645039 520 TQTEILLQEGLERLLEGRTSFIIA-HRLSTIKN-SSRIFYIDNGRIQEAG 567
Cdd:cd03220 175 AAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
354-575 |
7.81e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 98.61 E-value: 7.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV--EEVTLRSLRSQMGVML 431
Cdd:PRK13639 5 RDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 Q--DTFIFSGTIIENIRYGKL------DATEEEIIAAAKVVRAHDFisglkdgyyteVKERGSTLSAGQRQLISFARALL 503
Cdd:PRK13639 85 QnpDDQLFAPTVEEDVAFGPLnlglskEEVEKRVKEALKAVGMEGF-----------ENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 504 ADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
351-567 |
9.08e-23 |
|
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: 96.79 E-value: 9.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEgvdilkgINFHVD----AGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenVEEVTLRSLRSQ 426
Cdd:cd03298 1 VRLDKIRFSYGE-------QPMHFDltfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTAAPPADRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 427 MGVMLQDTFIFSG-TIIENIRYG-----KLDATEEEIIAAAKvvrAHDFISGLKdgyytevKERGSTLSAGQRQLISFAR 500
Cdd:cd03298 72 VSMLFQENNLFAHlTVEQNVGLGlspglKLTAEDRQAIEVAL---ARVGLAGLE-------KRLPGELSGGERQRVALAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 501 ALLADPKILILDEATSSIDTqteILLQEGLERLLE-----GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAG 567
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDP---ALRAEMLDLVLDlhaetKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
345-577 |
1.08e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 98.72 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 345 PPIVGNVDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlRSLR 424
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQ-DTFIFSGTIIENI----RYGKLDATEeeiiAAAKVVRAHDFiSGLKDGYYTEVKErgstLSAGQRQLISFA 499
Cdd:PRK13537 80 QRVGVVPQfDNLDPDFTVRENLlvfgRYFGLSAAA----ARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 500 RALLADPKILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGR-IQEAGSHEELMAQH 576
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRkIAEGAPHALIESEI 230
|
.
gi 346645039 577 G 577
Cdd:PRK13537 231 G 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
367-572 |
2.05e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 98.68 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEeVTLRSLRSQMGVMLQDTFIFSG-TIIENI 445
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERRVGFVFQHYALFPHmTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 RYG--KLDATEEEIIAaakvvRAHDFI-----SGLKDGYYTEvkergstLSAGQRQLISFARALLADPKILILDEATSSI 518
Cdd:COG1118 97 AFGlrVRPPSKAEIRA-----RVEELLelvqlEGLADRYPSQ-------LSGGQRQRVALARALAVEPEVLLLDEPFGAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 519 DTQTEILLQEGLERLLE--GRTSFIIAH------RLstiknSSRIFYIDNGRIQEAGSHEEL 572
Cdd:COG1118 165 DAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEV 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
355-575 |
2.82e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.58 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 355 DVYFRYEEGvDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEV-------------TLR 421
Cdd:PRK10619 10 DLHKRYGEH-EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 422 SLRSQMGVMLQDTFIFSG-TIIENIR--------YGKLDATEEEIIAAAKVvrahdFISGLKDGYYTevkergSTLSAGQ 492
Cdd:PRK10619 89 LLRTRLTMVFQHFNLWSHmTVLENVMeapiqvlgLSKQEARERAVKYLAKV-----GIDERAQGKYP------VHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 493 RQLISFARALLADPKILILDEATSSIDTQT--EIL--LQEGLErllEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAG 567
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELvgEVLriMQQLAE---EGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
|
....*...
gi 346645039 568 SHEELMAQ 575
Cdd:PRK10619 235 APEQLFGN 242
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
365-548 |
3.99e-22 |
|
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: 94.15 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 365 DILKGINFHVDAGESIALVGPTGAGKTTIINLLS--RFYNINSGEILVDGENVEevtLRSLRSQMG-VMLQDTFIFSGTI 441
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KRSFRKIIGyVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IENIRYgkldateeeiiaAAKVvrahdfisglkdgyytevkeRGstLSAGQRQLISFARALLADPKILILDEATSSIDTQ 521
Cdd:cd03213 100 RETLMF------------AAKL--------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180
....*....|....*....|....*...
gi 346645039 522 TEILLQEGLERL-LEGRTSFIIAHRLST 548
Cdd:cd03213 146 SALQVMSLLRRLaDTGRTIICSIHQPSS 173
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
39-318 |
5.52e-22 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 96.46 E-value: 5.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 39 LFVILLANVATMIGPYLTKIVIDDTIPNKNMTQlFWIAVI-FIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQ 117
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREA-FYRAVLlLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 118 KLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQ 197
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 198 RKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRsWMKAVKIQFLLWPGVQNIAVM-TTCLIYF 276
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALK-LSVRQALAYAGYVAVNTLLQNgTQVLVLF 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 346645039 277 VGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITA 318
Cdd:cd18572 240 YG--GHLVlsgRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQA 282
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
351-567 |
6.79e-22 |
|
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: 94.24 E-value: 6.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVtlRSLRSQMGVM 430
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRYG-KLDATEEEIIA-----AAKVVRahdfISGLKDGYYTEvkergstLSAGQRQLISFARALL 503
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFGlKLRKVPKDEIDervreVAELLQ----IEHLLDRKPKQ-------LSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 504 ADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAH-RLSTIKNSSRIFYIDNGRIQEAG 567
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
74-572 |
1.38e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 99.67 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 74 WI----AVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSdLLSN 149
Cdd:PLN03232 338 WVgyvyAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQ-QIAE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 150 GLINLISDILSVIVTLGFMLMIDPVLTLY-SLAL---IPVLFVIVMVIKTAQRKAYQVLSNKQSNMNayihESIAGIKVT 225
Cdd:PLN03232 417 QLHGLWSAPFRIIVSMVLLYQQLGVASLFgSLILfllIPLQTLIVRKMRKLTKEGLQWTDKRVGIIN----EILASMDTV 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 226 QSFSREEeNFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPV 305
Cdd:PLN03232 493 KCYAWEK-SFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPL 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 306 INIGNFYNSLITATTYLERIFETMDVEPDIkdIPNAKKMPPIVGNVDFKDVYFRYEEGVD--ILKGINFHVDAGESIALV 383
Cdd:PLN03232 572 NMLPNLLSQVVNANVSLQRIEELLLSEERI--LAQNPPLQPGAPAISIKNGYFSWDSKTSkpTLSDINLEIPVGSLVAIV 649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 384 GPTGAGKTTIINLLSrfyninsGEIlvdgeNVEEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKLDATEEEIIAAAKV 463
Cdd:PLN03232 650 GGTGEGKTSLISAML-------GEL-----SHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVT 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 464 VRAHDFisGLKDGY-YTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQ-TEILLQEGLERLLEGRTSFI 541
Cdd:PLN03232 718 ALQHDL--DLLPGRdLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVL 795
|
490 500 510
....*....|....*....|....*....|.
gi 346645039 542 IAHRLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PLN03232 796 VTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
39-297 |
1.97e-21 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 94.86 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 39 LFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQK 118
Cdd:cd18575 2 LIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 119 LPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQR 198
Cdd:cd18575 82 LSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 199 KAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLwpgvqnIAVMTTC------ 272
Cdd:cd18575 162 RLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALL------TALVIFLvfgaiv 235
|
250 260 270
....*....|....*....|....*....|
gi 346645039 273 LIYFVGIKgygvDV-----STGTLIAFIGY 297
Cdd:cd18575 236 FVLWLGAH----DVlagrmSAGELSQFVFY 261
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
367-571 |
2.41e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 94.34 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV--EEVTLRSLRSQMGVMLQ--DTFIFSGTII 442
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQypEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYG--KLDATEEEIiaAAKVVRAHDfISGLKdgyYTEVKERGS-TLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:PRK13637 103 KDIAFGpiNLGLSEEEI--ENRVKRAMN-IVGLD---YEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 520 --TQTEILLQEGLERLLEGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEE 571
Cdd:PRK13637 177 pkGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
354-575 |
2.60e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.14 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVE--EVTLRSLRSQMGVML 431
Cdd:PRK13636 9 EELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysRKGLMKLRESVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 Q--DTFIFSGTIIENIRYGKLDAT--EEEIIAAAKVVRAHDFISGLKDgyytevkERGSTLSAGQRQLISFARALLADPK 507
Cdd:PRK13636 89 QdpDNQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 508 ILILDEATSSIDTQ--TEI--LLQEGLERLleGRTSFIIAHRLSTIK-NSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK13636 162 VLVLDEPTAGLDPMgvSEImkLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
344-573 |
2.99e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.06 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 344 MPPIvgnvDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSL 423
Cdd:PRK09536 1 MPMI----DVSDLSVEFGD-TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 424 RSQMGVMLQDT---FIFSG-TIIE------NIRYGKLDATE----EEIIAAAKVVRAHDfisglkdgyytevkERGSTLS 489
Cdd:PRK09536 76 SRRVASVPQDTslsFEFDVrQVVEmgrtphRSRFDTWTETDraavERAMERTGVAQFAD--------------RPVTSLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 490 AGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLE-GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAG 567
Cdd:PRK09536 142 GGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
....*.
gi 346645039 568 SHEELM 573
Cdd:PRK09536 222 PPADVL 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
366-573 |
3.01e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.30 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFI-FSGTIIEN 444
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRYG----KLDATEEEIIAAAkVVRAHDfISGLKDGYYTevkergsTLSAGQRQLISFARALL------ADPKILILDEA 514
Cdd:PRK13548 97 VAMGraphGLSRAEDDALVAA-ALAQVD-LAHLAGRDYP-------QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 515 TSSIDtqteILLQEGLERLL------EGRTSFIIAHRLstikN-----SSRIFYIDNGRIQEAGSHEELM 573
Cdd:PRK13548 168 TSALD----LAHQHHVLRLArqlaheRGLAVIVVLHDL----NlaaryADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
351-567 |
3.04e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 92.34 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlrslRSQMGVM 430
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRY-GKLDATEEEIIAAakvvRAHDFISGLKDGYYTEVKERgsTLSAGQRQLISFARALLADPKI 508
Cdd:cd03269 76 PEERGLYPKmKVIDQLVYlAQLKGLKKEEARR----RIDEWLERLELSEYANKRVE--ELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 509 LILDEATSSID-TQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAG 567
Cdd:cd03269 150 LILDEPFSGLDpVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
371-576 |
3.05e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.72 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 371 NFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENveevTLRSLRSQMGV-ML-QDTFIFSG-TIIENIRY 447
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTPPSRRPVsMLfQENNLFSHlTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 448 G-----KLDATEEEIIAA-AKVVRAHDFISGLKdgyytevkergSTLSAGQRQLISFARALLADPKILILDEATSSIDTQ 521
Cdd:PRK10771 95 GlnpglKLNAAQREKLHAiARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 522 teiLLQEGL--------ERLLegrTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELMAQH 576
Cdd:PRK10771 164 ---LRQEMLtlvsqvcqERQL---TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
351-575 |
3.84e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 94.87 E-value: 3.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEG---VDILKGINFHVDAGESIALVGPTGAGKTT---IINLLSRfynINSGEILVDGENV---EEVTLR 421
Cdd:PRK11153 2 IELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLtalSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 422 SLRSQMGvMlqdtfIF-------SGTIIENIRYG-KLDATEEEIIAAakvvRAHDF-----ISGLKDGYytevkerGSTL 488
Cdd:PRK11153 79 KARRQIG-M-----IFqhfnllsSRTVFDNVALPlELAGTPKAEIKA----RVTELlelvgLSDKADRY-------PAQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 489 SAGQRQLISFARALLADPKILILDEATSSIDTQT--EIL-LQEGLERLLeGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQ 564
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATtrSILeLLKDINREL-GLTIVLITHEMDVVKRiCDRVAVIDAGRLV 220
|
250
....*....|.
gi 346645039 565 EAGSHEELMAQ 575
Cdd:PRK11153 221 EQGTVSEVFSH 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
351-567 |
5.19e-21 |
|
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: 91.49 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGeSIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGVM 430
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQD-TFIFSGTIIENIRYgkldateeeiIAAAKVV---RAHDFISGL--KDGYYTEVKERGSTLSAGQRQLISFARALLA 504
Cdd:cd03264 78 PQEfGVYPNFTVREFLDY----------IAWLKGIpskEVKARVDEVleLVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 505 DPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNS-SRIFYIDNGRIQEAG 567
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
32-325 |
5.63e-21 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 93.43 E-value: 5.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 32 QKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTA 111
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 112 IFGHLQKLPFSYFDSRPHGKILIRVvNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVM 191
Cdd:cd18782 81 IIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 192 VIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSfsreeENFEIFT--EVSNEYRRSW---MKAVKIQFLLWPGVQNI 266
Cdd:cd18782 160 LFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA-----QNAELKArwRWQNRYARSLgegFKLTVLGTTSGSLSQFL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 267 AVMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18782 235 NKLSSLLVLWVGaylvLRG---ELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
33-325 |
5.70e-21 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 93.39 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 33 KSIYITLFVI-LLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTA 111
Cdd:cd18568 1 RKLLAEILLAsLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 112 IFGHLQKLPFSYFDSRPHGKILIRVvnYINM-LSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIV 190
Cdd:cd18568 81 FYKHLLSLPLSFFASRKVGDIITRF--QENQkIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 191 MVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEenfEIFTEVSNEYRRSWMKAVKIQFlLWPGVQNIA--- 267
Cdd:cd18568 159 LLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAER---PIRWRWENKFAKALNTRFRGQK-LSIVLQLISsli 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 268 -VMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18568 235 nHLGTIAVLWYGaylvISG---QLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
359-576 |
6.86e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 6.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 359 RYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenveevTLRSLRSQMGVMLQDtfiFS 438
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALLELGAGFHPE---LT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 GtiIENIR-----YG----KLDATEEEIIaaakvvrahDFiSGLKDGYYTEVKergsTLSAGQRQLISFARALLADPKIL 509
Cdd:COG1134 105 G--RENIYlngrlLGlsrkEIDEKFDEIV---------EF-AELGDFIDQPVK----TYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 510 ILDEATSSIDTQteilLQE-GLERLLE----GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQH 576
Cdd:COG1134 169 LVDEVLAVGDAA----FQKkCLARIRElresGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAAY 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
351-575 |
7.80e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.94 E-value: 7.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVM 430
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQ--DTFIFSGTIIENIRYGKLD-ATEEEIIaaakvvrAHDFISGLKDGYYTEVKERGS-TLSAGQRQLISFARALLADP 506
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGPINlGLDEETV-------AHRVSSALHMLGLEELRDRVPhHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-570 |
8.62e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.74 E-value: 8.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 319 TTYLERIFETMDVEPDIKDIPNAkkMPPIVGN-----VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTI 393
Cdd:PRK13536 7 AEEAPRRLELSPIERKHQGISEA--KASIPGSmstvaIDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 394 INLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGVMLQ-DTFIFSGTIIENI----RYGKLDATEEEIIaaakvvrahd 468
Cdd:PRK13536 84 ARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQfDNLDLEFTVRENLlvfgRYFGMSTREIEAV---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 469 fISGLKDGYYTEVKE--RGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHR 545
Cdd:PRK13536 153 -IPSLLEFARLESKAdaRVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHF 231
|
250 260
....*....|....*....|....*..
gi 346645039 546 LSTIKN-SSRIFYIDNGR-IQEAGSHE 570
Cdd:PRK13536 232 MEEAERlCDRLCVLEAGRkIAEGRPHA 258
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
351-573 |
1.69e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.59 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVD-ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGV 429
Cdd:PRK13632 8 IKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQD---TFIFSgTIIENIRYG----KLDATE-EEIIA-AAKVVRAHDFIsglkdgyytevKERGSTLSAGQRQLISFAR 500
Cdd:PRK13632 88 IFQNpdnQFIGA-TVEDDIAFGlenkKVPPKKmKDIIDdLAKKVGMEDYL-----------DKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 501 ALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIA--HRLSTIKNSSRIFYIDNGRIQEAGSHEELM 573
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
367-572 |
1.72e-20 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 90.51 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlRSLRSQMGVMLQDTFIFSG-TIIENI 445
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 R-YGKLDATEEEiIAAAKVVRAHDFIsGLkdgyyTEVKER-GSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTE 523
Cdd:cd03265 95 YiHARLYGVPGA-ERRERIDELLDFV-GL-----LEAADRlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 346645039 524 ILLQEGLERLLE--GRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:cd03265 168 AHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
351-574 |
2.71e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.20 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT-LRSLRSQMGV 429
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQ--DTFIFSGTIIENIRYGKLDATEEEIIAAAKVVRAHDFIsGLKDGYYTEVKergsTLSAGQRQLISFARALLADPK 507
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEI-GLEKYRHRSPK----TLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 508 ILILDEATSSIDTQTEILLQEGLERLLE-GRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
371-567 |
2.72e-20 |
|
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: 89.66 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 371 NFHVDA-----GESIALVGPTGAGKTTIINLLSRFYNINSGEILVDG----ENVEEVTLRSLRSQMGVMLQDTFIFSG-T 440
Cdd:cd03297 12 DFTLKIdfdlnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfDSRKKINLPPQQRKIGLVFQQYALFPHlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYG-KLDATEEEIIAAAKVVRAHDfISGLKDGYYtevkergSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:cd03297 92 VRENLAFGlKRKRNREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 346645039 520 TQTEILLQEGLERLLE--GRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAG 567
Cdd:cd03297 164 RALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
310-545 |
3.52e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.49 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 310 NFYNSLITATTYLERI--FETMDVEPDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTG 387
Cdd:COG4178 320 DNYQSLAEWRATVDRLagFEEALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSG 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 388 AGKTTIINLLSRFYNINSGEIlvdgenveevtlrSLRSQMGVML--QDTFIFSGTIIENIRY--GKLDATEEEIIAAAKV 463
Cdd:COG4178 400 SGKSTLLRAIAGLWPYGSGRI-------------ARPAGARVLFlpQRPYLPLGTLREALLYpaTAEAFSDAELREALEA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 464 VRAHDFISGLkdgyyTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGrTSFI-I 542
Cdd:COG4178 467 VGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG-TTVIsV 540
|
...
gi 346645039 543 AHR 545
Cdd:COG4178 541 GHR 543
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
367-567 |
4.43e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 88.96 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGVMLQDTFIFSG-TIIENI 445
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 RY-GKLDATEEEIIAAakvvRAHDFISGLKDGYYTEVkeRGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEI 524
Cdd:cd03266 100 EYfAGLYGLKGDELTA----RLEELADRLGMEELLDR--RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 346645039 525 LLQEGLERLLE-GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAG 567
Cdd:cd03266 174 ALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
367-578 |
4.77e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.94 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV------------EEvtlRSLRSQMgvmlqdt 434
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLdpedrrrigylpEE---RGLYPKM------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 435 fifsgTIIENIRY-GKL---DAteeeiiAAAKvVRAHDFIS--GLKDGYYTEVKErgstLSAGQRQLISFARALLADPKI 508
Cdd:COG4152 87 -----KVGEQLVYlARLkglSK------AEAK-RRADEWLErlGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 509 LILDEATSSID-TQTEILLQEGLERLLEGRTsfII--AHRLSTI-KNSSRIFYIDNGRIQEAGSHEELMAQHGY 578
Cdd:COG4152 151 LILDEPFSGLDpVNVELLKDVIRELAAKGTT--VIfsSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
304-574 |
5.48e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 94.80 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 304 PVINIGNFYNSLITATTYLERIFETMDVEPDIKdIPNakkmPPIVGN---VDFKDVYFRYEEGVD--ILKGINFHVDAGE 378
Cdd:PLN03130 570 PLFMLPNLITQAVNANVSLKRLEELLLAEERVL-LPN----PPLEPGlpaISIKNGYFSWDSKAErpTLSNINLDVPVGS 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 379 SIALVGPTGAGKTTIINLLSrfyninsGEI--LVDGENVeevtlrsLRSQMGVMLQDTFIFSGTIIENIRYGK-LDATE- 454
Cdd:PLN03130 645 LVAIVGSTGEGKTSLISAML-------GELppRSDASVV-------IRGTVAYVPQVSWIFNATVRDNILFGSpFDPERy 710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 455 EEIIAAAKVVRAHDFISGlkdGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQT-EILLQEGLERL 533
Cdd:PLN03130 711 ERAIDVTALQHDLDLLPG---GDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgRQVFDKCIKDE 787
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 346645039 534 LEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PLN03130 788 LRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
366-572 |
8.78e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 91.30 E-value: 8.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSlrSQMGVMLQDTFIFSG-TIIEN 444
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRYG--KLDATEEEIIAA--AKVVRAHDFI--SGLKDGYytevkerGSTLSAGQRQLISFARALLADPKILILDEATSSI 518
Cdd:PRK10851 95 IAFGltVLPRRERPNAAAikAKVTQLLEMVqlAHLADRY-------PAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 519 DTQTEILLQEGLERLLE--GRTSFIIAH-RLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
344-578 |
1.29e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.02 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 344 MPPIVGNVDFKDVY------FRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV-- 415
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvkrglFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 416 -EEVTLRSLRSQMGVMLQDTFifsGTIieNIRYgKLDATEEE--II-----AAAKVVRAHDFIS--GLKDGYYtevKERG 485
Cdd:PRK11308 82 aDPEAQKLLRQKIQIVFQNPY---GSL--NPRK-KVGQILEEplLIntslsAAERREKALAMMAkvGLRPEHY---DRYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 486 STLSAGQRQLISFARALLADPKILILDEATSSIDT--QTEIL-----LQEglerllEGRTSFI-IAHRLST---IKNSSR 554
Cdd:PRK11308 153 HMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVsvQAQVLnlmmdLQQ------ELGLSYVfISHDLSVvehIADEVM 226
|
250 260
....*....|....*....|....*.
gi 346645039 555 IFYIdnGRIQEAGSHEELMA--QHGY 578
Cdd:PRK11308 227 VMYL--GRCVEKGTKEQIFNnpRHPY 250
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
42-315 |
1.45e-19 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 89.50 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 42 ILLANVATMIGPYLTKIVID-----DTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd18573 5 LLVSSAVTMSVPFAIGKLIDvaskeSGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTA 196
Cdd:cd18573 85 LRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNE-----YRRSWMKAVKIQFLLWPGvqNIAVMtt 271
Cdd:cd18573 165 VRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEvfdlaKKEALASGLFFGSTGFSG--NLSLL-- 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 346645039 272 CLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSL 315
Cdd:cd18573 241 SVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSEL 284
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
367-546 |
1.64e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSLR--SQMGV-------MLQDTFif 437
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSPRdaIALGIgmvhqhfMLVPNL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 438 sgTIIENIRYGkLDATEEEII---AAAKVVRAhdfIS---GLKdgyyTEVKERGSTLSAGQRQLISFARALLADPKILIL 511
Cdd:COG3845 96 --TVAENIVLG-LEPTKGGRLdrkAARARIRE---LSeryGLD----VDPDAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 346645039 512 DEATSSIDTQ-TEILLQEgLERLL-EGRTSFIIAHRL 546
Cdd:COG3845 166 DEPTAVLTPQeADELFEI-LRRLAaEGKSIIFITHKL 201
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
351-587 |
1.72e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.39 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRslRSQMGVM 430
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRYG-KLDATEEEIIA-----AAKVVRAHDFIsglkdgyytevKERGSTLSAGQRQLISFARALL 503
Cdd:PRK09452 92 FQSYALFPHmTVFENVAFGlRMQKTPAAEITprvmeALRMVQLEEFA-----------QRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 504 ADPKILILDEATSSID------TQTEIllqEGLERLLeGRTSFIIAH-RLSTIKNSSRIFYIDNGRIQEAGSHEELmaqh 576
Cdd:PRK09452 161 NKPKVLLLDESLSALDyklrkqMQNEL---KALQRKL-GITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI---- 232
|
250
....*....|....*
gi 346645039 577 gyyY----NLYQSQF 587
Cdd:PRK09452 233 ---YeepkNLFVARF 244
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
367-573 |
3.92e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.14 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNIN-----SGEILVDGENVEEVTLRS--LRSQMGVMLQDTFIFSG 439
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIRYG----------KLDATEEEIIAAAKVvrahdfisglkdgyYTEVKER----GSTLSAGQRQLISFARALLAD 505
Cdd:PRK14239 101 SIYENVVYGlrlkgikdkqVLDEAVEKSLKGASI--------------WDEVKDRlhdsALGLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 506 PKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHrlsTIKNSSRI-----FYIDNGRIQEAGSHEELM 573
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRIsdrtgFFLDGDLIEYNDTKQMFM 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
339-519 |
5.90e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 86.63 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 339 PNAKKMPPIVgnvDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRfynIN--------SGEILV 410
Cdd:COG1117 3 APASTLEPKI---EVRNLNVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNR---MNdlipgarvEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 411 DGENV--EEVTLRSLRSQMGVMLQDTFIFSGTIIENIRYG-----KLDATE-EEIiaaakVVRAhdfisgLKD-GYYTEV 481
Cdd:COG1117 76 DGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgIKSKSElDEI-----VEES------LRKaALWDEV 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 346645039 482 KER----GSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:COG1117 145 KDRlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
366-574 |
6.30e-19 |
|
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: 86.06 E-value: 6.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSlRSQMGV--MLQDTFIFSG-TII 442
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIgyLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIR-----YGKLDATEEEIIAAAkvvrAHDF-ISGLKdgyytevKERGSTLSAGQRQLISFARALLADPKILILDEATS 516
Cdd:cd03218 94 ENILavleiRGLSKKEREEKLEEL----LEEFhITHLR-------KSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 517 SIDTQTEILLQEGLERLLE-GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:cd03218 163 GVDPIAVQDIQKIIKILKDrGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
364-533 |
8.62e-19 |
|
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: 85.40 E-value: 8.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 364 VDILKGINFHVDAGESIALVGPTGAGKTTIINLLS---RFYNINSGEILVDGenvEEVTLRSLRSQMGVMLQDTFIFSG- 439
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIRYGKLDATEEEIIAAAKVVRAHDFisGLKDGYYTEVK-ERGSTLSAGQRQLISFARALLADPKILILDEATSSI 518
Cdd:cd03234 97 TVRETLTYTAILRLPRKSSDAIRKKRVEDV--LLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170
....*....|....*
gi 346645039 519 DTQTEILLQEGLERL 533
Cdd:cd03234 175 DSFTALNLVSTLSQL 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
353-564 |
1.00e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDgenveevtlRSLRsqMGVMLQ 432
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 DTFIFSG-TIIENIR----------------YGKLDATEEEIIAAAKV-------------VRAHDFISGLK---DGYYT 479
Cdd:COG0488 69 EPPLDDDlTVLDTVLdgdaelraleaeleelEAKLAEPDEDLERLAELqeefealggweaeARAEEILSGLGfpeEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 480 EVkergSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTeIllqEGLERLLEGRTS--FIIAH------RLSTikn 551
Cdd:COG0488 149 PV----SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES-I---EWLEEFLKNYPGtvLVVSHdryfldRVAT--- 217
|
250
....*....|...
gi 346645039 552 ssRIFYIDNGRIQ 564
Cdd:COG0488 218 --RILELDRGKLT 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-565 |
1.09e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 322 LERIfETMDVEPDIK----DIPNAKKMPPIVgnVDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLL 397
Cdd:COG0488 286 LEKL-EREEPPRRDKtveiRFPPPERLGKKV--LELEGLSKSYGDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 398 SRFYNINSGEILVdGENVEEVTLrslrSQMgvmlQDTFIFSGTIIENIRYGKLDATEEEIIAAAKvvrahDF-ISGlkdg 476
Cdd:COG0488 362 AGELEPDSGTVKL-GETVKIGYF----DQH----QEELDPDKTVLDELRDGAPGGTEQEVRGYLG-----RFlFSG---- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 477 yyTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERlLEGrTSFIIAH-R--LSTIKNss 553
Cdd:COG0488 424 --DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-FPG-TVLLVSHdRyfLDRVAT-- 497
|
250
....*....|..
gi 346645039 554 RIFYIDNGRIQE 565
Cdd:COG0488 498 RILEFEDGGVRE 509
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
329-584 |
1.29e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.38 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 329 MDVEPDIKDIPNAKKMPPIVgNVDFKDVYFRYEEG-----VD---ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRF 400
Cdd:PRK15134 257 LNSEPSGDPVPLPEPASPLL-DVEQLQVAFPIRKGilkrtVDhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 401 ynINS-GEILVDGENVEEVTLRSL---RSQMGVMLQDTF------IFSGTIIEN---IRYGKLDAT--EEEIIAAAKVVr 465
Cdd:PRK15134 336 --INSqGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNsslnprLNVLQIIEEglrVHQPTLSAAqrEQQVIAVMEEV- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 466 ahdfisglkdGYYTEVKER-GSTLSAGQRQLISFARALLADPKILILDEATSSID--TQTEIL-LQEGLERllEGRTSFI 541
Cdd:PRK15134 413 ----------GLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQAQILaLLKSLQQ--KHQLAYL 480
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 346645039 542 -IAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA--QHGYYYNLYQ 584
Cdd:PRK15134 481 fISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAapQQEYTRQLLA 527
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
362-578 |
1.46e-18 |
|
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: 84.12 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 362 EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRF--YNINSGEILVDGENVEEVTLrSLRSQMGVML--QDTFIF 437
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPP-EERARLGIFLafQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 438 SGtiienirygkldateeeiiaaakvVRAHDFISGLKDGyytevkergstLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:cd03217 90 PG------------------------VKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 518 IDTQTEILLQEGLERLLEGRTSF-IIAH--RLSTIKNSSRIFYIDNGRIQEAGSHE--ELMAQHGY 578
Cdd:cd03217 135 LDIDALRLVAEVINKLREEGKSVlIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKGY 200
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
366-563 |
1.46e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.50 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDgenveEVTLRSLRSQMGVMLQDTFIFS-GTIIEN 444
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRYG-KLDATEEEIIAAAKVvrahdfisGLKDgyytEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTE 523
Cdd:PRK11247 102 VGLGlKGQWRDAALQALAAV--------GLAD----RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 346645039 524 ILLQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGRI 563
Cdd:PRK11247 170 IEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
366-543 |
1.63e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.16 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSL------RSQMGVMLqdtfifsg 439
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghRNAMKPAL-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIRY--GKLDATEEEIIAAAKVVRAHDfISGLKDGYytevkergstLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:PRK13539 89 TVAENLEFwaAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*.
gi 346645039 518 IDTQTEILLQEGLERLLEGRTSFIIA 543
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
363-574 |
1.87e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.92 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNI-----NSGEILVDGENVEEV-TLRSLRSQMGVMLQDTFI 436
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 437 FSGTIIENIRYGkldateeeiIAAAKVVRAHDFiSGLKDGYYTEV------KERGST----LSAGQRQLISFARALLADP 506
Cdd:PRK14271 113 FPMSIMDNVLAG---------VRAHKLVPRKEF-RGVAQARLTEVglwdavKDRLSDspfrLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLST---IKNSSRIFYidNGRIQEAGSHEELMA 574
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQaarISDRAALFF--DGRLVEEGPTEQLFS 251
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
35-325 |
4.97e-18 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 84.86 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 35 IYITLFVILLAnvatMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLC--MRYRIRSITLIGQDILKDMRtaI 112
Cdd:cd18588 8 LLASLFLQLFA----LVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLsgLRTYLFSHTTNRIDAELGAR--L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 FGHLQKLPFSYFDSRPHGKILIRvVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMV 192
Cdd:cd18588 82 FRHLLRLPLSYFESRQVGDTVAR-VRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 193 IKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTC 272
Cdd:cd18588 161 VTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 273 LIYFVGikGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18588 241 AILWFG--AYLVmdgELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-563 |
5.03e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 84.37 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVeevTLRSL--RSQM-GVMLQDTFI---FSG 439
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV---TKLPEykRAKYiGRVFQDPMMgtaPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIrygkldateeeIIAAAKVvRAHDFISGLKDGYYTEVKERGST---------------LSAGQRQLISFARALLA 504
Cdd:COG1101 98 TIEENL-----------ALAYRRG-KRRGLRRGLTKKRRELFRELLATlglglenrldtkvglLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 505 DPKILILDEATSSIDTQTEILLQEGLERLLEGR--TSFIIAHRLS-TIKNSSRIFYIDNGRI 563
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
363-572 |
5.35e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlRSLRSQMGVML--QDTFIFSG- 439
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIYLvpQEPLLFPNl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIRYG--KLDATEEEIIAAAKVVRAHdfisglkdgyyTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:PRK15439 102 SVKENILFGlpKRQASMQKMKQLLAALGCQ-----------LDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 518 ID-TQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK15439 171 LTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
72-513 |
6.82e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 87.16 E-value: 6.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 72 LFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNgL 151
Cdd:COG4615 47 LARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-L 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 152 INLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIK-VTQSFSR 230
Cdd:COG4615 126 PELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKeLKLNRRR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 231 EEENFE-IFTEVSNEYRRSWMKAVKIQFLLWpgvqniaVMTTCLIYF-----VGIKGYGVDVSTGTLIAFIG---YVgnf 301
Cdd:COG4615 206 RRAFFDeDLQPTAERYRDLRIRADTIFALAN-------NWGNLLFFAligliLFLLPALGWADPAVLSGFVLvllFL--- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 302 WNPVINIGNFYNSLITATTYLERI---FETMDVEPDIKDIPNAKKMPPIVGNVDFKDVYFRY----EEGVDILKGINFHV 374
Cdd:COG4615 276 RGPLSQLVGALPTLSRANVALRKIeelELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYpgedGDEGFTLGPIDLTI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 375 DAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTiienirYGKLDATE 454
Cdd:COG4615 356 RRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEAD 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 455 EEIIAA-------AKVVRahdfisgLKDGYYTEVKergstLSAGQRQ---LISfarALLADPKILILDE 513
Cdd:COG4615 430 PARAREllerlelDHKVS-------VEDGRFSTTD-----LSQGQRKrlaLLV---ALLEDRPILVFDE 483
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
351-574 |
1.04e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEE-VTLRSLRSQMGV 429
Cdd:PRK11614 6 LSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTFIFSG-TIIENIRYGKLDATEEEIiaAAKVVRAHDFISGLkdgyYTEVKERGSTLSAGQRQLISFARALLADPKI 508
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGGFFAERDQF--QERIKWVYELFPRL----HERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 509 LILDEatSSIDTQTEILLQ--EGLERLL-EGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK11614 159 LLLDE--PSLGLAPIIIQQifDTIEQLReQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
351-563 |
1.56e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.84 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRS---LRSQM 427
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQD-TFIFSGTIIENIRYGKL--DATEEEIiaAAKVVRAHDfisglKDGYYTEVKERGSTLSAGQRQLISFARALLA 504
Cdd:PRK10908 82 GMIFQDhHLLMDRTVYDNVAIPLIiaGASGDDI--RRRVSAALD-----KVGLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 505 DPKILILDEATSSIDTQteilLQEGLERLLE-----GRTSFIIAHRLSTI-KNSSRIFYIDNGRI 563
Cdd:PRK10908 155 KPAVLLADEPTGNLDDA----LSEGILRLFEefnrvGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
362-574 |
2.14e-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: 85.24 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 362 EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRF--YNINSGEIL------------------------------ 409
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 410 ---VDGENVEEVTLRSLRSQMGVMLQDTFIFSG--TIIENIrygkLDATEEEIIAAAKVV-RAHDFISGLKDGYytEVKE 483
Cdd:TIGR03269 91 peeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNV----LEALEEIGYEGKEAVgRAVDLIEMVQLSH--RITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 484 RGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLL--EGRTSFIIAHRLSTIKN-SSRIFYIDN 560
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLEN 244
|
250
....*....|....
gi 346645039 561 GRIQEAGSHEELMA 574
Cdd:TIGR03269 245 GEIKEEGTPDEVVA 258
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
354-564 |
2.28e-17 |
|
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: 81.61 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGeNVEEVTLRSLRSQMGVML-- 431
Cdd:cd03267 24 KSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVFgq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 ----------QDTFIFSGTIIeNIRYGKLDATEEEIIAAAKVVRAHDfisglkdgyyTEVKErgstLSAGQRQLISFARA 501
Cdd:cd03267 103 ktqlwwdlpvIDSFYLLAAIY-DLPPARFKKRLDELSELLDLEELLD----------TPVRQ----LSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 502 LLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFII--AHRLSTI-KNSSRIFYIDNGRIQ 564
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLL 233
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
366-570 |
2.64e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.60 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDG------ENVEEVTLRSLRSQMGVMLQDTFIFSG 439
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 -TIIEN-----IRYGKLDatEEEIIAaakvvRAHDFISGLKdgyYTEVKERGST-LSAGQRQLISFARALLADPKILILD 512
Cdd:PRK11124 97 lTVQQNlieapCRVLGLS--KDQALA-----RAEKLLERLR---LKPYADRFPLhLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 513 EATSSIDtqTEILLQ--EGLERLLE-GRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHE 570
Cdd:PRK11124 167 EPTAALD--PEITAQivSIIRELAEtGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDAS 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
366-513 |
3.08e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.23 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIinllsrFYNI------NSGEILVDGENVEEVTLrSLRSQMGV--MLQDTFIF 437
Cdd:COG1137 18 VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYMIvglvkpDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 438 SG-TIIENIR----YGKLDATE-----EEIIAaakvvrahDF-ISGLKDgyytevkERGSTLSAGQRQLISFARALLADP 506
Cdd:COG1137 91 RKlTVEDNILavleLRKLSKKEreerlEELLE--------EFgITHLRK-------SKAYSLSGGERRRVEIARALATNP 155
|
....*..
gi 346645039 507 KILILDE 513
Cdd:COG1137 156 KFILLDE 162
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
357-561 |
3.12e-17 |
|
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: 80.84 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 357 YFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTII-NLLSRFYNInSGEI-----LVDGENVEEVTLRSlRSQMGVM 430
Cdd:cd03290 7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTL-EGKVhwsnkNESEPSFEATRSRN-RYSVAYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSGTIIENIRYGKlDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILI 510
Cdd:cd03290 85 AQKPWLLNATVEENITFGS-PFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 346645039 511 LDEATSSIDTQ-TEILLQEGLERLL--EGRTSFIIAHRLSTIKNSSRIFYIDNG 561
Cdd:cd03290 164 LDDPFSALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
369-572 |
3.14e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.57 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 369 GINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLrSQMGVMlqDTFifsgtiiENIR-Y 447
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVV--RTF-------QHVRlF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 448 GKLDATEEEIIAAAKVVRAhDFISGL-KDGYY--------------------TEVKER-GSTLSAGQRQLISFARALLAD 505
Cdd:PRK11300 93 REMTVIENLLVAQHQQLKT-GLFSGLlKTPAFrraesealdraatwlervglLEHANRqAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 506 PKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
366-565 |
3.24e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 82.04 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQMGVMLQDTF------- 435
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSIsavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 436 -IfsGTII-ENIRY-GKLDATEEEIIAAAkVVRAHDFISGLKDgyytevkERGSTLSAGQRQLISFARALLADPKILILD 512
Cdd:PRK10419 107 tV--REIIrEPLRHlLSLDKAERLARASE-MLRAVDLDDSVLD-------KRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 513 EATSSIDtqteILLQEGLERLLE------GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQE 565
Cdd:PRK10419 177 EAVSNLD----LVLQAGVIRLLKklqqqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
366-522 |
3.34e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.60 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTT----IINLLSRFYNInSGEILVDGENVEevTLRSLRSQMGVMLQDTFIFSG-T 440
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTllaaIAGTLSPAFSA-SGEVLLNGRRLT--ALPAEQRRIGILFQDDLLFPHlS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYgkldATEEEIIAAAKVVRAHDFIS--GLkDGYYtevkERG-STLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:COG4136 93 VGENLAF----ALPPTIGRAQRRARVEQALEeaGL-AGFA----DRDpATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
....*
gi 346645039 518 IDTQT 522
Cdd:COG4136 164 LDAAL 168
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
359-565 |
3.74e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.02 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 359 RYEEG---VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGEnveevTLRSLRSQMGVMLQDT- 434
Cdd:PRK11629 14 RYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ-----PMSKLSSAAKAELRNQk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 435 --FIFS-------GTIIENIRY-----GKLDATEEEiiaaakvvRAHDFISGLkdGYYTEVKERGSTLSAGQRQLISFAR 500
Cdd:PRK11629 89 lgFIYQfhhllpdFTALENVAMplligKKKPAEINS--------RALEMLAAV--GLEHRANHRPSELSGGERQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 501 ALLADPKILILDEATSSIDTQTEILLQEGLERL--LEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQE 565
Cdd:PRK11629 159 ALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
39-325 |
6.70e-17 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 81.44 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 39 LFVILLANVATMIGPYLTKIVIDDTIPNKNmTQLFWIAVIFIVSVIVTGLCMRYrIRSITLIG-QDIL-KDMRTAIFGHL 116
Cdd:cd18779 8 LLASLLLQLLGLALPLLTGVLVDRVIPRGD-RDLLGVLGLGLAALVLTQLLAGL-LRSHLLLRlRTRLdTQLTLGFLEHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRvVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVL--TLYSLALIPVLFVIVMvik 194
Cdd:cd18779 86 LRLPYRFFQQRSTGDLLMR-LSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLglVVLGLAALQVALLLAT--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 195 taqRKAYQVLSNK----QSNMNAYIHESIAGIKVTQSFSREEENFE----IFTEVSN-EYRRS----WMKAVK--IQF-- 257
Cdd:cd18779 162 ---RRRVRELMARelaaQAEAQSYLVEALSGIETLKASGAEDRALDrwsnLFVDQLNaSLRRGrldaLVDALLatLRLaa 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 258 ---LLWPGVQniAVMTTCLiyfvgikgygvdvSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18779 239 plvLLWVGAW--QVLDGQL-------------SLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
363-544 |
7.01e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 7.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlrslrSQMGVMLQDTFIFS-GTI 441
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQNEGLLPwRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IENIRYG-KLDATEEeiiaAAKVVRAHDFISglKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDT 520
Cdd:PRK11248 88 QDNVAFGlQLAGVEK----MQRLEIAHQMLK--KVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180
....*....|....*....|....*.
gi 346645039 521 QTEILLQEGLERLLE--GRTSFIIAH 544
Cdd:PRK11248 162 FTREQMQTLLLKLWQetGKQVLLITH 187
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
364-572 |
7.51e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 80.34 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 364 VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNIN-----SGEILVDGENVEEVTLRSLRSQMGVMLQ-DTFIF 437
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 438 SGTIIENIRYG----KLDATEEEIiaAAKVVRAHDfisglKDGYYTEVKER----GSTLSAGQRQLISFARALLADPKIL 509
Cdd:PRK14247 96 NLSIFENVALGlklnRLVKSKKEL--QERVRWALE-----KAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAH-RLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
367-573 |
7.53e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.77 E-value: 7.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQMGVMLQDTFIF--SGTI 441
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKIAMVFQSFALmpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IENIRYG------KLDATEEEIIAAAKVVRAHDFISGLKDgyytevkergsTLSAGQRQLISFARALLADPKILILDEAT 515
Cdd:PRK10070 124 LDNTAFGmelagiNAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 516 SSIDTQTEILLQEGLERLL--EGRTSFIIAHRL-STIKNSSRIFYIDNGRIQEAGSHEELM 573
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
361-563 |
9.21e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.62 E-value: 9.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 361 EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSL----RSQMGVMLQDTFI 436
Cdd:PRK10535 18 EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 437 FSG-TIIENIRYGKLDATEEEiiaAAKVVRAHDFISGLkdGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEAT 515
Cdd:PRK10535 98 LSHlTAAQNVEVPAVYAGLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 346645039 516 SSIDTQTEILLQEGLERLLE-GRTSFIIAHRLSTIKNSSRIFYIDNGRI 563
Cdd:PRK10535 173 GALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-565 |
9.38e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 9.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 344 MPPIVGNVDFKDVYFRYEEGvDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNInSGEILVDG------ENVEE 417
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnQNIYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 418 --VTLRSLRSQMGVMLQDTFIFSGTIIENIRYGKldateeEIIAAAKVVRAHDFI-SGLKDG-YYTEVKER----GSTLS 489
Cdd:PRK14258 79 rrVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGV------KIVGWRPKLEIDDIVeSALKDAdLWDEIKHKihksALDLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 490 AGQRQLISFARALLADPKILILDEATSSID----TQTEILLQEglERLLEGRTSFIIAHRL---STIKNSSRIFYIDNGR 562
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQS--LRLRSELTMVIVSHNLhqvSRLSDFTAFFKGNENR 230
|
...
gi 346645039 563 IQE 565
Cdd:PRK14258 231 IGQ 233
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
370-575 |
1.24e-16 |
|
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: 81.69 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGE----NVEEVTLRSLRSQMGVMLQDTFIFSG-TIIEN 444
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEARLFPHlSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRYG-KLDATEEEIIAAAKVVRAHDfISGLKDgyytevkeRG-STLSAGQRQLISFARALLADPKILILDEATSSIDTQT 522
Cdd:COG4148 98 LLYGrKRAPRAERRISFDEVVELLG-IGHLLD--------RRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 523 --EILlqEGLERLlegRTSF-----IIAH------RLSTiknssRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:COG4148 169 kaEIL--PYLERL---RDELdipilYVSHsldevaRLAD-----HVVLLEQGRVVASGPLAEVLSR 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
370-575 |
2.07e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.92 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSLRSQ-MGVMLQDTFIFSG-TIIENIRY 447
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRdICMVFQSYALFPHmSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 448 G--KLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVkergstlSAGQRQLISFARALLADPKILILDEATSSIDTQTEIL 525
Cdd:PRK11432 102 GlkMLGVPKEERKQRVKEALELVDLAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 346645039 526 LQEGLERLLE--GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK11432 175 MREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
356-578 |
2.64e-16 |
|
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: 82.04 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 356 VYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKT----TIINLLSRFYNINSGEILVDGENV---EEVTLRSLR-SQ 426
Cdd:COG4172 14 VAFGQGGGtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglSERELRRIRgNR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 427 MGvmlqdtFIFS------------GT-IIENIR-YGKLDATE--EEIIAAAKVVRAHDFISGLKDgYYTEvkergstLSA 490
Cdd:COG4172 94 IA------MIFQepmtslnplhtiGKqIAEVLRlHRGLSGAAarARALELLERVGIPDPERRLDA-YPHQ-------LSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 491 GQRQLISFARALLADPKILILDEATSSID--TQTEIL-----LQ--EGLERLLegrtsfiIAHRLSTIKN-SSRIFYIDN 560
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDvtVQAQILdllkdLQreLGMALLL-------ITHDLGVVRRfADRVAVMRQ 232
|
250 260
....*....|....*....|
gi 346645039 561 GRIQEAGSHEELMA--QHGY 578
Cdd:COG4172 233 GEIVEQGPTAELFAapQHPY 252
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
366-572 |
3.02e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.94 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGE------NVEEVTLRSLRSQMGVMLQDTFIFSG 439
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 -TIIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSI 518
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 519 DTQTEILLQEGLERLLEGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
363-575 |
3.62e-16 |
|
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: 79.13 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGEnveevtlRSLRSQMgvmlqdTFIFSGTII 442
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------ISFSSQF------SWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYGkLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQT 522
Cdd:cd03291 116 ENIIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 346645039 523 EI-LLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:cd03291 195 EKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
363-549 |
4.19e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.11 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLR-SLRSQMGVMLQD-TFIFSGT 440
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQElHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYGKLDAT-----EEEIIAAAKVVRAHdfiSGLKDGYYTEVKErgstLSAGQRQLISFARALLADPKILILDEAT 515
Cdd:PRK11288 96 VAENLYLGQLPHKggivnRRLLNYEAREQLEH---LGVDIDPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 346645039 516 SSIDTQ-TEILLQegLERLL--EGRTSFIIAHRLSTI 549
Cdd:PRK11288 169 SSLSAReIEQLFR--VIRELraEGRVILYVSHRMEEI 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
351-574 |
5.60e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.60 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI--LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMG 428
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 429 VMLQ--DTFIFSGTIIENIRYGkldaTEEEIIAAAKVVRAHDfiSGLKDGYYTEVKERG-STLSAGQRQLISFARALLAD 505
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFG----MENQGIPREEMIKRVD--EALLAVNMLDFKTREpARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 506 PKILILDEATSSIDTQTEILLQEGLERLLEGR--TSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
367-590 |
5.71e-16 |
|
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: 77.51 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLrsqmgVMLQDTFIFSG-TIIENI 445
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 RYG------KLDATEEEiiaaaKVVRAHDFISGLKDGyyteVKERGSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:TIGR01184 76 ALAvdrvlpDLSKSERR-----AIVEEHIALVGLTEA----ADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 520 TQTEILLQEGLERLLE--GRTSFIIAHRL-STIKNSSRIFYIDNGRIQEAGS----------HEELMAQHGYYYNLYQSQ 586
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQilevpfprprDRLEVVEDPSYYDLRNEA 226
|
....
gi 346645039 587 FDML 590
Cdd:TIGR01184 227 LYFL 230
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
353-560 |
6.98e-16 |
|
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: 75.27 E-value: 6.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILvdgenveevtlRSLRSQMGVMLQ 432
Cdd:cd03223 3 LENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------MPEGEDLLFLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 DTFIFSGTIIENIRYgkldateeeiiaaakvvrahdfisglkdgyytevkERGSTLSAGQRQLISFARALLADPKILILD 512
Cdd:cd03223 72 RPYLPLGTLREQLIY-----------------------------------PWDDVLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 346645039 513 EATSSIDTQTEILLqegLERLLEGRTSFI-IAHRLSTIKNSSRIFYIDN 560
Cdd:cd03223 117 EATSALDEESEDRL---YQLLKELGITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
362-572 |
7.61e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.49 E-value: 7.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 362 EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlrSLRSQMGVMLQDTFIFSGTI 441
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYALFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IE-NIRYG-KLDATEEEIIAAakvvRAHDFISGLKDGYYTevKERGSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:PRK11607 108 VEqNIAFGlKQDKLPKAEIAS----RVNEMLGLVHMQEFA--KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 520 TQTEILLQEGLERLLE--GRTSFIIAH-RLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK11607 182 KKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
351-572 |
7.66e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 78.30 E-value: 7.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFY---NINSGEILVDGENVEEVTLRSLRSQ 426
Cdd:PRK13640 6 VEFKHVSFTYPDSkKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 427 MGVMLQ--DTFIFSGTIIENIRYGkldaTEEEIIAAAKVVR-AHDFISGLkdGYYTEVKERGSTLSAGQRQLISFARALL 503
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFG----LENRAVPRPEMIKiVRDVLADV--GMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 504 ADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
363-575 |
8.70e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 81.50 E-value: 8.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenveevtlrslrsQMGVMLQDTFIFSGTII 442
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYGkLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQT 522
Cdd:TIGR01271 505 DNIIFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 346645039 523 EI-LLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:TIGR01271 584 EKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
366-544 |
9.10e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.19 E-value: 9.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNIN-----SGEILVDGENV--EEVTLRSLRSQMGVMLQDTFIFS 438
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 G-TIIENI----RYGKLDATEEEIiaaAKVVRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDE 513
Cdd:PRK14267 99 HlTIYDNVaigvKLNGLVKSKKEL---DERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190
....*....|....*....|....*....|.
gi 346645039 514 ATSSIDTQTEILLQEGLERLLEGRTSFIIAH 544
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
362-574 |
1.39e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.47 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 362 EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRS-LRSQMGVMLQDTFIFSGT 440
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYGKL----DATEEEIIAAAKVVRAHDFISGLKDGYytevkerGSTLSAGQRQLISFARALLADPKILILDEATS 516
Cdd:PRK10895 94 SVYDNLMAVLqirdDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 517 SIDTQTEILLQEGLERLLE-GRTSFIIAHRL-STIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
35-294 |
2.27e-15 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 76.85 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18566 4 LPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKILIRVvNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIK 194
Cdd:cd18566 84 HLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 195 TAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLI 274
Cdd:cd18566 163 PILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAV 242
|
250 260
....*....|....*....|....
gi 346645039 275 YFVG----IKGygvDVSTGTLIAF 294
Cdd:cd18566 243 VAFGallvING---DLTVGALIAC 263
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
354-563 |
2.37e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.05 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVDI----LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEI---LVDGEN----------VE 416
Cdd:PRK13651 6 KNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNkkktkekekvLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 417 EVTL-----------RSLRSQMGVMLQ--DTFIFSGTIIENIRYG--KLDATEEEiiaAAKvvRAHDFIS--GLKDGYyt 479
Cdd:PRK13651 86 KLVIqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEE---AKK--RAAKYIElvGLDESY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 480 eVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERL-LEGRTSFIIAHRL-STIKNSSRIFY 557
Cdd:PRK13651 159 -LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIF 237
|
....*.
gi 346645039 558 IDNGRI 563
Cdd:PRK13651 238 FKDGKI 243
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
343-574 |
3.09e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.44 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 343 KMPPIVGnvdfkDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDgenveevtlRS 422
Cdd:PTZ00243 658 KTPKMKT-----DDFFELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE---------RS 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 423 LrsqmGVMLQDTFIFSGTIIENIrygkLDATEEEIIAAAKVVRAHDF---ISGLKDGYYTEVKERGSTLSAGQRQLISFA 499
Cdd:PTZ00243 723 I----AYVPQQAWIMNATVRGNI----LFFDEEDAARLADAVRVSQLeadLAQLGGGLETEIGEKGVNLSGGQKARVSLA 794
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 500 RALLADPKILILDEATSSIDTQT-EILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PTZ00243 795 RAVYANRDVYLLDDPLSALDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
368-578 |
3.67e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.05 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 368 KGINFHVDAGESIALVGPTGAGKTT----IINLLsrfyNINSGEILVDGENV---EEVTLRSLRSQMGVMLQDTF----- 435
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTfaraIIGLV----KATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDPLaslnp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 436 -IFSGTII-ENIR--YGKLDATE--EEIIAAAKVVrahDFISGLKDGYYTEvkergstLSAGQRQLISFARALLADPKIL 509
Cdd:PRK15079 114 rMTIGEIIaEPLRtyHPKLSRQEvkDRVKAMMLKV---GLLPNLINRYPHE-------FSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 510 ILDEATS----SIDTQTEILLQEgLERllEGRTSFI-IAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA--QHGY 578
Cdd:PRK15079 184 ICDEPVSaldvSIQAQVVNLLQQ-LQR--EMGLSLIfIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHnpLHPY 257
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
363-550 |
4.04e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINS--GEILVDGENVEEVTLR-SLRSQMGVMLQD-TFIFS 438
Cdd:PRK13549 17 GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRdTERAGIAIIHQElALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 GTIIENIRYGKlDATEEEIIAAAKVV-RAHDFISGLKDGY--YTEVKERGStlsaGQRQLISFARALLADPKILILDEAT 515
Cdd:PRK13549 97 LSVLENIFLGN-EITPGGIMDYDAMYlRAQKLLAQLKLDInpATPVGNLGL----GQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 346645039 516 SSI-DTQTEILLQ--EGLERllEGRTSFIIAHRLSTIK 550
Cdd:PRK13549 172 ASLtESETAVLLDiiRDLKA--HGIACIYISHKLNEVK 207
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
366-581 |
7.54e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.78 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSrFYNIN----SGEILVDGENVEEVTLRsLRSQMgVMLQDTFIFSGTI 441
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKEMR-AISAY-VQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IENI------RYGKLDATEE------EIIAAAKVVRAHDFISGlkdgyyteVKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:TIGR00955 117 REHLmfqahlRMPRRVTKKEkrervdEVLQALGLRKCANTRIG--------VPGRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLLEGRTSFIIahrlsTI-KNSSRIF-------YIDNGRIQEAGSHEEL---MAQHGY 578
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIIC-----TIhQPSSELFelfdkiiLMAEGRVAYLGSPDQAvpfFSDLGH 263
|
....*..
gi 346645039 579 ----YYN 581
Cdd:TIGR00955 264 pcpeNYN 270
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
363-549 |
9.41e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.14 E-value: 9.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINS--GEILVDGenvEEVTLRSLRS--QMGVML--QD-TF 435
Cdd:NF040905 13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG---EVCRFKDIRDseALGIVIihQElAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 436 IFSGTIIENI-------RYGKLDATEEEIIAA---AKVvrahdfisGLKDGYYTEVKERGstlsAGQRQLISFARALLAD 505
Cdd:NF040905 90 IPYLSIAENIflgneraKRGVIDWNETNRRARellAKV--------GLDESPDTLVTDIG----VGKQQLVEIAKALSKD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 346645039 506 PKILILDEATSSI-DTQTEILLQEGLERLLEGRTSFIIAHRLSTI 549
Cdd:NF040905 158 VKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEI 202
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
353-576 |
9.93e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.93 E-value: 9.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQ 432
Cdd:PRK10522 325 LRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 DTFIFSGTIienirYGKLDATEEEIIAA--------AKVVRAHDFISGLKdgyytevkergstLSAGQRQLISFARALLA 504
Cdd:PRK10522 405 DFHLFDQLL-----GPEGKPANPALVEKwlerlkmaHKLELEDGRISNLK-------------LSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 505 DPKILILDEATSSIDTQ-TEILLQEGLERLLE-GRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQH 576
Cdd:PRK10522 467 ERDILLLDEWAADQDPHfRREFYQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASR 540
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
366-543 |
1.24e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 72.91 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENI 445
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 RYGKLDATEEEIIAAAKVVRahdfISGLKDGYYtevkergSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEIL 525
Cdd:cd03231 95 RFWHADHSDEQVEEALARVG----LNGFEDRPV-------AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170
....*....|....*...
gi 346645039 526 LQEGLERLLEGRTSFIIA 543
Cdd:cd03231 164 FAEAMAGHCARGGMVVLT 181
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
367-568 |
1.25e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.05 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYN-INS----GEILVDGENV--EEVTLRSLRSQMGVMLQDTFIFSG 439
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlIPGfrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIRYG--------KLDATEEEIIAAAkvvrahdfisGLKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILIL 511
Cdd:PRK14243 106 SIYDNIAYGaringykgDMDELVERSLRQA----------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 512 DEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGS 568
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
351-568 |
1.69e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.01 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI----LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT----LRS 422
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 423 LRSQMGVMLQ--DTFIFSGTIIENIRYG--KLDATEEEiiaAAKVVRAHDFISGLKDgyytEVKERGS-TLSAGQRQLIS 497
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEE---AEALAREKLALVGISE----SLFEKNPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 498 FARALLADPKILILDEATSSIDTQTEILLQEGLERLLE-GRTSFIIAHRLSTIKNSSRIFYI-DNGRIQEAGS 568
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANYADFVYVlEKGKLVLSGK 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
366-521 |
1.72e-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: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIENI 445
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 446 R-YGKLDATEEEII--AAAKVvrahdfisGLKDGYYTEVkergSTLSAGQRQLISFARALLADPKILILDEATSSIDTQ 521
Cdd:TIGR01189 95 HfWAAIHGGAQRTIedALAAV--------GLTGFEDLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
351-574 |
2.03e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.10 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI----LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT----LRS 422
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 423 LRSQMGVMLQ--DTFIFSGTIIENIRYGKLD--ATEEEI-IAAAKVVRahdfisglKDGYYTEVKERGS-TLSAGQRQLI 496
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAkEKALKWLK--------KVGLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 497 SFARALLADPKILILDEATSSIDTQT-EILLQEGLERLLEGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
358-588 |
2.74e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.29 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 358 FRYEEG------VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVE--EVTLRSLRSQMgv 429
Cdd:PRK15112 14 FRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRM-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTfifSGTIIENIRYGKL-------------DATEEEIIAAAKVVrahdfisGLKD---GYYTEVkergstLSAGQR 493
Cdd:PRK15112 92 IFQDP---STSLNPRQRISQIldfplrlntdlepEQREKQIIETLRQV-------GLLPdhaSYYPHM------LAPGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 494 QLISFARALLADPKILILDEATSSID----TQTEILLQEGLERllEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGS 568
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDmsmrSQLINLMLELQEK--QGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
250 260
....*....|....*....|..
gi 346645039 569 HEELMA--QHGYYYNLYQSQFD 588
Cdd:PRK15112 234 TADVLAspLHELTKRLIAGHFG 255
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
350-580 |
3.09e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 74.68 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 350 NVDFKDVYFRYEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTlRSLRSqMGV 429
Cdd:PRK11000 3 SVTLRNVTKAYGD-VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP-PAERG-VGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTFIFSG-TIIENIRYG-KLDATEEEII-----AAAKVVR-AHdfisgLKDgyytevkERGSTLSAGQRQLISFARA 501
Cdd:PRK11000 80 VFQSYALYPHlSVAENMSFGlKLAGAKKEEInqrvnQVAEVLQlAH-----LLD-------RKPKALSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 502 LLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAH-RLSTIKNSSRIFYIDNGRIQEAGSHEELmaqhgY 578
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL-----Y 222
|
..
gi 346645039 579 YY 580
Cdd:PRK11000 223 HY 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
354-535 |
3.22e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.05 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQD 433
Cdd:PRK10247 11 QNVGYLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 TFIFSGTIIENIRYG---KLDATEEEIIaAAKVVRahdFisGLKDgyyTEVKERGSTLSAGQRQLISFARALLADPKILI 510
Cdd:PRK10247 90 PTLFGDTVYDNLIFPwqiRNQQPDPAIF-LDDLER---F--ALPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180
....*....|....*....|....*
gi 346645039 511 LDEATSSIDTQTEILLQEGLERLLE 535
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVR 185
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
366-589 |
3.24e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 72.74 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSG-TIIEN 444
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRY---------GKLDATEEEIIAAAkVVRAHdfISGLKDgyytevkERGSTLSAGQRQLISFARALLADPKILILDEAT 515
Cdd:PRK11231 97 VAYgrspwlslwGRLSAEDNARVNQA-MEQTR--INHLAD-------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 516 SSIDT--QTEILlqeGLERLL--EGRTSFIIAHRLStikNSSRifYID------NGRIQEAGSHEELMAQHgyyynLYQS 585
Cdd:PRK11231 167 TYLDInhQVELM---RLMRELntQGKTVVTVLHDLN---QASR--YCDhlvvlaNGHVMAQGTPEEVMTPG-----LLRT 233
|
....
gi 346645039 586 QFDM 589
Cdd:PRK11231 234 VFDV 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
351-575 |
5.42e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.84 E-value: 5.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI----LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEI----LVDGENVEEVTLRS 422
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 423 LRSQMGVMLQ--DTFIFSGTIIENIRYGK----LDATEEEIIAAAKVVrahdfISGLKDGYYtevKERGSTLSAGQRQLI 496
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPqnfgIPKEKAEKIAAEKLE-----MVGLADEFW---EKSPFELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 497 SFARALLADPKILILDEATSSIDTQTEILLQEGLERLLE-GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
.
gi 346645039 575 Q 575
Cdd:PRK13643 234 E 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
363-550 |
6.27e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.44 E-value: 6.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLR-SLRSQMGVMLQD-TFIFSGT 440
Cdd:PRK09700 17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQElSVIDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYGKL-----------DATEEEIIAAAKVVRAhdfisGLKdgyyTEVKERGSTLSAGQRQLISFARALLADPKIL 509
Cdd:PRK09700 97 VLENLYIGRHltkkvcgvniiDWREMRVRAAMMLLRV-----GLK----VDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 346645039 510 ILDEATSSIdTQTEILLQEGLERLL--EGRTSFIIAHRLSTIK 550
Cdd:PRK09700 168 IMDEPTSSL-TNKEVDYLFLIMNQLrkEGTAIVYISHKLAEIR 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
351-572 |
9.72e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 71.71 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVDI-LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGV 429
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQD-TFIFSGTIIE-NIRYGkldaTEEEIIAAAKVVRahDFISGLKD-GYYTEVKERGSTLSAGQRQLISFARALLADP 506
Cdd:PRK13648 88 VFQNpDNQFVGSIVKyDVAFG----LENHAVPYDEMHR--RVSEALKQvDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 507 KILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIA--HRLSTIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
363-562 |
1.08e-13 |
|
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: 73.71 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINS--GEILVDGENVEEVTLRSL-RSQMGVMLQD-TFIFS 438
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTeRAGIVIIHQElTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 GTIIENIRYGKLDATEEEIIA-AAKVVRAHDFISGLKDGYYTEVKERGStLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:TIGR02633 93 LSVAENIFLGNEITLPGGRMAyNAMYLRAKNLLRELQLDADNVTRPVGD-YGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 346645039 518 I-DTQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYIDNGR 562
Cdd:TIGR02633 172 LtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
359-578 |
1.25e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.74 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 359 RYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT---LRSLRSQMGVMLQDTF 435
Cdd:PRK10261 332 RVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 436 -------IFSGTIIENIR-YGKLDATEeeiiAAAKVVRAHDFISGLKDGYYTEVKErgstLSAGQRQLISFARALLADPK 507
Cdd:PRK10261 412 asldprqTVGDSIMEPLRvHGLLPGKA----AAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 508 ILILDEATSSIDTQTE---ILLQEGLERLLeGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELM--AQHGY 578
Cdd:PRK10261 484 VIIADEAVSALDVSIRgqiINLLLDLQRDF-GIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFenPQHPY 559
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
369-535 |
1.46e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.83 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 369 GINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENveevtLRSLRSQmgvmLQDTFIFSG--------- 439
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP-----IRRQRDE----YHQDLLYLGhqpgiktel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 TIIENIR-YGKL--DATEEEIIAA-AKVvrahdfisGLKDgyYTEVKERgsTLSAGQRQLISFARALLADPKILILDEAT 515
Cdd:PRK13538 90 TALENLRfYQRLhgPGDDEALWEAlAQV--------GLAG--FEDVPVR--QLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180
....*....|....*....|...
gi 346645039 516 SSIDTQteillqeG---LERLLE 535
Cdd:PRK13538 158 TAIDKQ-------GvarLEALLA 173
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
329-575 |
1.73e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.91 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 329 MDVEPDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGV-DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGE 407
Cdd:TIGR03269 261 MEGVSEVEKECEVEVGEPIIKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 408 ILVD-GENVEEVTLRSLRSQ------MGVMLQDTFIFS-GTIIENIRygklDATEEEIIAAAKVVRAhdfISGLKDGYYT 479
Cdd:TIGR03269 341 VNVRvGDEWVDMTKPGPDGRgrakryIGILHQEYDLYPhRTVLDNLT----EAIGLELPDELARMKA---VITLKMVGFD 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 480 EVKERG------STLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKN 551
Cdd:TIGR03269 414 EEKAEEildkypDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLD 493
|
250 260
....*....|....*....|....*
gi 346645039 552 -SSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:TIGR03269 494 vCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
336-579 |
2.06e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.27 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 336 KDIPNAKKMPPIVGNVdfKDVYFR-YEEgVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGEN 414
Cdd:COG4586 9 KTYRVYEKEPGLKGAL--KGLFRReYRE-VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 415 -VEEvtLRSLRSQMGVM------------LQDTFIFSGTI--IENIRYgklDATEEEIIAaakvvrahdfISGLKDGYYT 479
Cdd:COG4586 86 pFKR--RKEFARRIGVVfgqrsqlwwdlpAIDSFRLLKAIyrIPDAEY---KKRLDELVE----------LLDLGELLDT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 480 EVKErgstLSAGQRQLISFARALLADPKILILDEATSSIDtqteILLQEGLERLL------EGRTSFIIAHRLSTIKN-S 552
Cdd:COG4586 151 PVRQ----LSLGQRMRCELAAALLHRPKILFLDEPTIGLD----VVSKEAIREFLkeynreRGTTILLTSHDMDDIEAlC 222
|
250 260
....*....|....*....|....*..
gi 346645039 553 SRIFYIDNGRIQEAGSHEELMAQHGYY 579
Cdd:COG4586 223 DRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
40-318 |
2.36e-13 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 70.80 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 40 FVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLC--MRYRIRSITLIGQDIlkDMRTAIFGHLQ 117
Cdd:cd18784 3 FFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAagIRGGLFTLAMARLNI--RIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 118 KLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQ 197
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 198 RKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMK-AVKIQFLLWPGVQNIAVMTTCLIYF 276
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKeALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 346645039 277 VG---IKGYgvdVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITA 318
Cdd:cd18784 241 GGhlvITGQ---ISGGNLISFILYQLELGSCLESVGSVYTGLMQA 282
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
353-574 |
2.42e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.82 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 353 FKDVYFRYEEGV----DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVdGENV-----EEVTLRSL 423
Cdd:PRK13634 5 FQKVEHRYQYKTpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKKLKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 424 RSQMGVMLQ--DTFIFSGTIIENIRYGKLD--ATEEEIIAAAKVVRAhdfISGLKDgyytEVKERGS-TLSAGQRQLISF 498
Cdd:PRK13634 84 RKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLPE----ELLARSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 499 ARALLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
367-572 |
2.64e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFY---NINSGEILVDGENVEEV-----TLRSLRSQMGVMLQD-TFIF 437
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREgrlarDIRKSRANTGYIFQQfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 438 SGTIIENIRYGKLDAT---------------EEEIIAAAKVVRAHdfisglkdgyytEVKERGSTLSAGQRQLISFARAL 502
Cdd:PRK09984 100 RLSVLENVLIGALGSTpfwrtcfswftreqkQRALQALTRVGMVH------------FAHQRVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 503 LADPKILILDEATSSIDTQTEILLQEGLERL--LEGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
33-294 |
2.68e-13 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 70.62 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 33 KSIYITLFVI-LLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcMRYRIRSITLIGQDILkDMRTA 111
Cdd:cd18783 1 KRLFRDVAIAsLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGI-LGYLRRYLLLVATTRI-DARLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 112 --IFGHLQKLPFSYFDSRPHGKIlIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVI 189
Cdd:cd18783 79 lrTFDRLLSLPIDFFERTPAGVL-TKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 190 VMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQflLWPgvQNIA-- 267
Cdd:cd18783 158 ILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLS--NWP--QTLTgp 233
|
250 260 270
....*....|....*....|....*....|...
gi 346645039 268 ---VMTTCLIyFVGIkgYGV---DVSTGTLIAF 294
Cdd:cd18783 234 lekLMTVGVI-WVGA--YLVfagSLTVGALIAF 263
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
351-591 |
3.11e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.58 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGV----DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVT----LRS 422
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 423 LRSQMGVMLQ--DTFIFSGTIIENIRYG----KLDATEEEiiaaakvVRAHDFISGLkdGYYTEVKERGS-TLSAGQRQL 495
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGpknfKMNLDEVK-------NYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 496 ISFARALLADPKILILDEATSSIDTQTEILLQEGLERLL--EGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEEL 572
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
250
....*....|....*....
gi 346645039 573 MAQHGYYYNLYQSQFDMLQ 591
Cdd:PRK13646 234 FKDKKKLADWHIGLPEIVQ 252
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
35-325 |
3.19e-13 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 70.58 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 35 IYITLFVILLAnVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcmryrirsITLIGQDILKDMRTAI-- 112
Cdd:cd18569 5 LFVVLAGLLLV-IPGLVIPVFSRIFIDDILVGGLPDWLRPLLLGMALTALLQGL--------LTWLQQYYLLRLETKLal 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 113 ------FGHLQKLPFSYFDSRPHGKILIRVvNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVL 186
Cdd:cd18569 76 ssssrfFWHVLRLPVEFFSQRYAGDIASRV-QSNDRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 187 FVIVMVIKTAQRKAYQVLSNKQSNMNAYiheSIAGIKVTQSF---SREEENFE----IFTEVSNEYRRSwmkAVKIQFL- 258
Cdd:cd18569 155 LLVLRLVSRKRVDLNRRLLQDSGKLTGT---TMSGLQMIETLkasGAESDFFSrwagYQAKVLNAQQEL---GRTNQLLg 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346645039 259 LWPGVqnIAVMTTCLIYFVG----IKGygvDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18569 229 ALPTL--LSALTNAAILGLGgllvMDG---ALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
366-586 |
3.25e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKT----TIINLL-SRFYNINSGEILVDGENV---EEVTLRSLR-SQMGVMLQDTFI 436
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLlhaSEQTLRGVRgNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 437 fSGTIIENI-----------RYGKLDATEEEIIAAAKVVRAHDFISGLKDgyYTEvkergsTLSAGQRQLISFARALLAD 505
Cdd:PRK15134 104 -SLNPLHTLekqlyevlslhRGMRREAARGEILNCLDRVGIRQAAKRLTD--YPH------QLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 506 PKILILDEATSSIDT--QTEI--LLQEgLERLLEGRTSFiIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA--QHGY 578
Cdd:PRK15134 175 PELLIADEPTTALDVsvQAQIlqLLRE-LQQELNMGLLF-ITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSapTHPY 252
|
....*...
gi 346645039 579 YYNLYQSQ 586
Cdd:PRK15134 253 TQKLLNSE 260
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
366-573 |
3.44e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.02 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQD-TFIFSGTIIEN 444
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNaTTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 445 IRYGKLDAT-------EEEIIAAAKVVRAhdfiSGLKDGYYTEVkergSTLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:PRK10253 102 VARGRYPHQplftrwrKEDEEAVTKAMQA----TGITHLADQSV----DTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 518 IDTQTEILLQEGLERL--LEGRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELM 573
Cdd:PRK10253 174 LDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
366-560 |
4.53e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 68.04 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNIN--SGEILVDGENVEEvtlrSLRSQMG-VMLQDTFIFSGTII 442
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK----NFQRSTGyVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYgkldateeeiiaAAKVvrahdfisglkdgyytevkeRGstLSAGQRQLISFARALLADPKILILDEATSSIDTQT 522
Cdd:cd03232 98 EALRF------------SALL--------------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 346645039 523 EILLQEGLERL-LEGRTSfiiahrLSTIKN-SSRIF-YIDN 560
Cdd:cd03232 144 AYNIVRFLKKLaDSGQAI------LCTIHQpSASIFeKFDR 178
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
363-549 |
4.79e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.57 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSLR-SQ---MGVMLQD-TFIF 437
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKsSQeagIGIIHQElNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 438 SGTIIENI--------RYGKLDAteEEIIAAAKVVRAHdfiSGLKDGYYTEVKErgstLSAGQRQLISFARALLADPKIL 509
Cdd:PRK10762 93 QLTIAENIflgrefvnRFGRIDW--KKMYAEADKLLAR---LNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 346645039 510 ILDEATSSI-DTQTEILLQEGLERLLEGRTSFIIAHRLSTI 549
Cdd:PRK10762 164 IMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEI 204
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
355-574 |
8.63e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.88 E-value: 8.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 355 DVYFRYEEGvDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGE--NVEEVTLRSLRSQMGVMLQ 432
Cdd:PRK13638 6 DLWFRYQDE-PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 433 D--TFIFSGTIIENIRYG--KLDATEEEII----AAAKVVRAHDFisglkdgyyteVKERGSTLSAGQRQLISFARALLA 504
Cdd:PRK13638 85 DpeQQIFYTDIDSDIAFSlrNLGVPEAEITrrvdEALTLVDAQHF-----------RHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 505 DPKILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
350-519 |
1.04e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.87 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 350 NVDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLR-------- 421
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAdrdiamvf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 422 ---SLRSQMgvmlqdtfifsgTIIENIRYG----KLDATE--EEIIAAAKVvrahdfisgLKDGYYTEVKERgsTLSAGQ 492
Cdd:PRK11650 83 qnyALYPHM------------SVRENMAYGlkirGMPKAEieERVAEAARI---------LELEPLLDRKPR--ELSGGQ 139
|
170 180
....*....|....*....|....*..
gi 346645039 493 RQLISFARALLADPKILILDEATSSID 519
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
351-562 |
1.79e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 65.16 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSrfyninsgeilvdgenveevtlrslrsqmgvm 430
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA-------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 lqdtfifsgtiieniryGKLDATEEEIIaaakvvrahdFISGLKDGYYTEvkergstLSAGQRQLISFARALLADPKILI 510
Cdd:cd03221 48 -----------------GELEPDEGIVT----------WGSTVKIGYFEQ-------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 346645039 511 LDEATSSIDTQTEILLQEGLERLleGRTSFIIAHRLSTIKN-SSRIFYIDNGR 562
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
361-522 |
1.99e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.11 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 361 EEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV---EEVTLRSLRSQ-MGVMLQdTFI 436
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmDEEARAKLRAKhVGFVFQ-SFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 437 FSGTI--IENIRYGKLDATEEEiiaAAKVVRAHDFISGLkdGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEA 514
Cdd:PRK10584 99 LIPTLnaLENVELPALLRGESS---RQSRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
....*...
gi 346645039 515 TSSIDTQT 522
Cdd:PRK10584 174 TGNLDRQT 181
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
327-568 |
2.64e-12 |
|
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: 70.04 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 327 ETMDVE-PD-IKDIPNAKKMPPIVGNVDFKDVYFRYEE-GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNI 403
Cdd:TIGR01257 903 EMEDPEhPEgINDSFFERELPGLVPGVCVKNLVKIFEPsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 404 NSGEILVDGENVEeVTLRSLRSQMGVMLQDTFIFSG-TIIENIR-YGKLDATEEEiiaAAKVvrahDFISGLKD-GYYTE 480
Cdd:TIGR01257 983 TSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHlTVAEHILfYAQLKGRSWE---EAQL----EMEAMLEDtGLHHK 1054
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 481 VKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYID 559
Cdd:TIGR01257 1055 RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIIS 1134
|
....*....
gi 346645039 560 NGRIQEAGS 568
Cdd:TIGR01257 1135 QGRLYCSGT 1143
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
354-583 |
6.01e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 68.38 E-value: 6.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGV--DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenveEVTLRSLRSQMGVML 431
Cdd:PRK13545 25 KDLFFRSKDGEyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----SAALIAISSGLNGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 qdtfifsgTIIENIRYGKL--DATEEEIIA-AAKVVRAHD---FIsglkdgyYTEVKergsTLSAGQRQLISFARALLAD 505
Cdd:PRK13545 101 --------TGIENIELKGLmmGLTKEKIKEiIPEIIEFADigkFI-------YQPVK----TYSSGMKSRLGFAISVHIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 506 PKILILDEATSSID-TQTEILLQEGLERLLEGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQHGYYYNLY 583
Cdd:PRK13545 162 PDILVIDEALSVGDqTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKY 241
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
352-578 |
6.10e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 352 DFKD--VYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKT----TIINLLSRFYNI------NSGEILvdgeNVEEV 418
Cdd:PRK09473 14 DVKDlrVTFSTPDGdVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIggsatfNGREIL----NLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 419 TLRSLRS-QMGVMLQDTFI-------FSGTIIENI----RYGKLDATEEEI--IAAAKVVRA--------HDFisglkdg 476
Cdd:PRK09473 90 ELNKLRAeQISMIFQDPMTslnpymrVGEQLMEVLmlhkGMSKAEAFEESVrmLDAVKMPEArkrmkmypHEF------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 477 yytevkergstlSAGQRQLISFARALLADPKILILDEATSSIDT--QTEI--LLQEgLERllEGRTSFI-IAHRLSTIKN 551
Cdd:PRK09473 163 ------------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvQAQImtLLNE-LKR--EFNTAIImITHDLGVVAG 227
|
250 260 270
....*....|....*....|....*....|
gi 346645039 552 S-SRIFYIDNGRIQEAGSHEELMAQ--HGY 578
Cdd:PRK09473 228 IcDKVLVMYAGRTMEYGNARDVFYQpsHPY 257
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
351-513 |
7.59e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.94 E-value: 7.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSL---RSQM 427
Cdd:PRK11831 8 VDMRGVSFTRGNRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 428 GVMLQDTFIFSG-TIIENIRYGKLDATE--EEIIAAAKVVRAHDFisGLKDGyyteVKERGSTLSAGQRQLISFARALLA 504
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAYPLREHTQlpAPLLHSTVMMKLEAV--GLRGA----AKLMPSELSGGMARRAALARAIAL 160
|
....*....
gi 346645039 505 DPKILILDE 513
Cdd:PRK11831 161 EPDLIMFDE 169
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
367-591 |
1.11e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 65.25 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTiinLLSRFYNI--NSGEILVDGENVEEVTLRSLrSQMGVML--QDTFIFSGTII 442
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMAGLlpGQGEILLNGRPLSDWSAAEL-ARHRAYLsqQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYGKLDATEEEIIAAAKVVRAHDFisGLKDGYYTEVkergSTLSAGQRQLISFARALL-------ADPKILILDEAT 515
Cdd:COG4138 88 QYLALHQPAGASSEAVEQLLAQLAEAL--GLEDKLSRPL----TQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 516 SSID-TQteillQEGLERLLE-----GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELMAQHgyyyNL---YQS 585
Cdd:COG4138 162 NSLDvAQ-----QAALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPE----NLsevFGV 232
|
....*.
gi 346645039 586 QFDMLQ 591
Cdd:COG4138 233 KFRRLE 238
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
359-544 |
1.21e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.79 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 359 RYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGEnvEEVTLRSLRSQmgvmLQDTFifS 438
Cdd:NF040873 1 GYG-GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAYVPQRSE----VPDSL--P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 GTIIENIRYG---------KLDATEEEIIAAA-KVVRAHDFisglkdgyyteVKERGSTLSAGQRQLISFARALLADPKI 508
Cdd:NF040873 72 LTVRDLVAMGrwarrglwrRLTRDDRAAVDDAlERVGLADL-----------AGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190
....*....|....*....|....*....|....*..
gi 346645039 509 LILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAH 544
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTH 177
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
366-545 |
1.73e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDgenveevtlrslrsqmgvMLQDTFIFSGTIIENI 445
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 ryGKLDATEE--EIIAAAkvvrahdfisGLKDGYYteVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTE 523
Cdd:COG2401 107 --GRKGDFKDavELLNAV----------GLSDAVL--WLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180
....*....|....*....|....
gi 346645039 524 ILLQEGLERLL-EGRTSFIIA-HR 545
Cdd:COG2401 173 KRVARNLQKLArRAGITLVVAtHH 196
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
322-530 |
2.05e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.81 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 322 LERIFETMDV--EPDIK---DIPNAKKMPPIVgnvDFKDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINL 396
Cdd:PLN03073 478 LDRLGHVDAVvnDPDYKfefPTPDDRPGPPII---SFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKL 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 397 LsrfyninSGEIlvdgENVEEVTLRSLRSQMGVMLQ---DTFIFSGTIIENIRYGKLDATEEEIiaaakvvRAH--DF-I 470
Cdd:PLN03073 555 I-------SGEL----QPSSGTVFRSAKVRMAVFSQhhvDGLDLSSNPLLYMMRCFPGVPEQKL-------RAHlgSFgV 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 471 SG---LKDGYytevkergsTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGL 530
Cdd:PLN03073 617 TGnlaLQPMY---------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL 670
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
365-578 |
2.52e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 64.28 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 365 DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRF--YNINSGEILVDGENVEEVTlRSLRSQMGVML--QDTFIFSGT 440
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLGIFLafQYPIEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 -------IIENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTEVKERGstLSAGQRQLISFARALLADPKILILDE 513
Cdd:CHL00131 100 snadflrLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEG--FSGGEKKRNEILQMALLDSELAILDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 514 ATSSIDTQTEILLQEGLERLLEGRTSFI-IAH--RLSTIKNSSRIFYIDNGRIQEAGSHE--ELMAQHGY 578
Cdd:CHL00131 178 TDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKGY 247
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
64-258 |
2.84e-11 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 64.74 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 64 IPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINML 143
Cdd:cd18584 28 LEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 144 SDLLSNGLINLIsdiLSVIVT---LGFMLMIDPV---LTLYSLALIPVLFVIV-MVIKTAQRKAYQVLSNkqsnMNAYIH 216
Cdd:cd18584 108 DGYFARYLPQLV---LAAIVPlliLVAVFPLDWVsalILLVTAPLIPLFMILIgKAAQAASRRQWAALSR----LSGHFL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 346645039 217 ESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFL 258
Cdd:cd18584 181 DRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRVAFL 222
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
110-325 |
3.38e-11 |
|
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: 64.41 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 110 TAIFGHLQKLPFS--------YFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLA 181
Cdd:cd18589 65 SRIHSRLQGLVFAavlrqeiaFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 182 LIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTE-VSNEYRRSWMKAVKIQFLLW 260
Cdd:cd18589 145 GLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQrLQKTYRLNKKEAAAYAVSMW 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 261 PGVQNIAVMTTCLIYFVGIKGYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18589 225 TSSFSGLALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
355-549 |
3.87e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 355 DVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDT 434
Cdd:PRK15056 11 DVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 435 FIFSgTIIENI----RYGKL------DATEEEIIAAAkVVRAhdfisGLKDGYYTEVKErgstLSAGQRQLISFARALLA 504
Cdd:PRK15056 91 WSFP-VLVEDVvmmgRYGHMgwlrraKKRDRQIVTAA-LARV-----DMVEFRHRQIGE----LSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 346645039 505 DPKILILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTI 549
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
39-253 |
4.51e-11 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 64.03 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 39 LFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRyrirSITLIGQDILKDMRTAIFGHLQK 118
Cdd:cd18577 17 LMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTA----CWTITGERQARRIRKRYLKALLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 119 LPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQR 198
Cdd:cd18577 93 QDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 199 KAYQVLSNKQSNMNAYIHESIAGIKVTQSF---SREEENFEIFTEVSNEY--RRSWMKAV 253
Cdd:cd18577 173 KYTKKEQEAYAKAGSIAEEALSSIRTVKAFggeEKEIKRYSKALEKARKAgiKKGLVSGL 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
367-519 |
5.21e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.04 E-value: 5.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGEnveEVTLRSLRSQM--GVML------QDTFIFS 438
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK---PVRIRSPRDAIraGIAYvpedrkGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 439 GTIIENI---------RYGKLDATEEEIIAAakvvrahDFISGLK---DGYYTEVkergSTLSAGQRQLISFARALLADP 506
Cdd:COG1129 345 LSIRENItlasldrlsRGGLLDRRRERALAE-------EYIKRLRiktPSPEQPV----GNLSGGNQQKVVLAKWLATDP 413
|
170
....*....|...
gi 346645039 507 KILILDEATSSID 519
Cdd:COG1129 414 KVLILDEPTRGID 426
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
351-545 |
1.02e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.50 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEvTLRSLRSQMGVM 430
Cdd:PRK13540 2 LDVIELDFDYHDQP-LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDTFIFSG-TIIENIRY------GKLDATeeEIIAAAKVVRAHDFISGLkdgyytevkergstLSAGQRQLISFARALL 503
Cdd:PRK13540 80 GHRSGINPYlTLRENCLYdihfspGAVGIT--ELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWM 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 346645039 504 ADPKILILDEATSSIDtqteillqeglERLLEGRTSFIIAHR 545
Cdd:PRK13540 144 SKAKLWLLDEPLVALD-----------ELSLLTIITKIQEHR 174
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
351-575 |
1.20e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.41 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVD-----ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDG-ENVEEVTLRSLR 424
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQ--DTFIFSGTIIENIRYG--KLDATEEEIiaaakvvRAHDFISGLKDGYYTEVKERGSTLSAGQRQLISFAR 500
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEI-------RERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 501 ALLADPKILILDEATSSIDTQTEILLQEGLERL--LEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
366-519 |
3.38e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGE---NVEEVTLRSLRSQMGVMLQDTfifsgTII 442
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatRGDRSRFMAYLGHLPGLKADL-----STL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYgkldateeeiIAAAKVVRAHDF------ISGLKDGYYTEVKErgstLSAGQRQLISFARALLADPKILILDEATS 516
Cdd:PRK13543 101 ENLHF----------LCGLHGRRAKQMpgsalaIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
...
gi 346645039 517 SID 519
Cdd:PRK13543 167 NLD 169
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
382-574 |
3.68e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.18 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 382 LVGPTGAGKTTIINLLSRFYNINSGEILVDG-------ENVEEVtlRSLRSQMGVMLQ--DTFIFSGTIIENIRYGKLDA 452
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEV--KRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 453 TEEEIIAAAKVVRAHDFISgLKDGYyteVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLER 532
Cdd:PRK13645 120 GENKQEAYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFER 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 346645039 533 L--LEGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGSHEELMA 574
Cdd:PRK13645 196 LnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
366-556 |
4.01e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.59 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINS--GEILVDGENVEEVTLRslrsQMGVMLQDTFIFSG-TII 442
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK----RTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 443 ENIRYGKLDATEEEIIAAAKVVRAHDFIS--GLKDGYYTEVKE---RGstLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVISelGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 346645039 518 IDTQTEILLQEGLERLLE-GRTSFIIAHrlstiKNSSRIF 556
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQkGKTIVTSMH-----QPSSRVY 271
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
321-559 |
4.66e-10 |
|
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: 62.46 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 321 YLERIFETMDV-------------EPDIKDIPNAKKMPPIV---GNVDFKDVYFRYE-------EGVDILKGINFHVDAG 377
Cdd:TIGR00954 399 FTARVDTLLQVlddvksgnfkrprVEEIESGREGGRNSNLVpgrGIVEYQDNGIKFEniplvtpNGDVLIESLSFEVPSG 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 378 ESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENV-------EEVTLRSLRSQMgvmlqdtfIFSGTIIENIRYGKL 450
Cdd:TIGR00954 479 NNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKlfyvpqrPYMTLGTLRDQI--------IYPDSSEDMKRRGLS 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 451 DATEEEIIaaaKVVRAHDFISglKDGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGL 530
Cdd:TIGR00954 551 DKDLEQIL---DNVQLTHILE--REGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
250 260
....*....|....*....|....*....
gi 346645039 531 ERLleGRTSFIIAHRLSTIKNSSRIFYID 559
Cdd:TIGR00954 626 REF--GITLFSVSHRKSLWKYHEYLLYMD 652
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
365-519 |
5.00e-10 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 58.98 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 365 DILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSL--------------RSQMGVM 430
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPrdairagiayvpedRKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQdtfifsGTIIENIrygkldateeeiiaaakVVRAHdfisglkdgyytevkergstLSAGQRQLISFARALLADPKILI 510
Cdd:cd03215 91 LD------LSVAENI-----------------ALSSL--------------------LSGGNQQKVVLARWLARDPRVLI 127
|
....*....
gi 346645039 511 LDEATSSID 519
Cdd:cd03215 128 LDEPTRGVD 136
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
37-312 |
5.80e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 60.76 E-value: 5.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 37 ITLFVILLANVATMIgpyLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGHL 116
Cdd:cd18561 3 LLGLLITALYIAQAW---LLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 117 QKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTA 196
Cdd:cd18561 80 LKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 197 QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQNIAVMTTCLIYF 276
Cdd:cd18561 160 AKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALG 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 346645039 277 VGIKGY---GVDVSTGTLIAFIGyvGNFWNPVINIGNFY 312
Cdd:cd18561 240 VGALRVlggQLTLSSLLLILFLS--REFFRPLRDLGAYW 276
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
366-522 |
9.89e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYN---INSGEILVDGENVEEVTLRSLrsqmG-VMLQDTFIFSGTI 441
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSSFQRSI----GyVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IENIRYGKLDATEEEIIAAAKVVRAHDFISGLKDGYYTE--VKERGSTLSAGQRQLISFARALLADPKILI-LDEATSSI 518
Cdd:TIGR00956 854 RESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADavVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
....
gi 346645039 519 DTQT 522
Cdd:TIGR00956 934 DSQT 937
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
35-250 |
1.16e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 59.83 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 35 IYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPvltlYSLALIPVLFVIVMVIk 194
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP----YFLIVLPPLLVVYYLL- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 195 taqRKAYQVLSNK--------QSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWM 250
Cdd:cd18580 156 ---QRYYLRTSRQlrrlesesRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFY 216
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
377-564 |
1.44e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.00 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 377 GESIALVGPTGAGKTTIINLLSRFYNINSGE-ILVDGENVEEVTLRSLRsqmgvmlqdtfifsgtiienirygkldatee 455
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 456 eiiaaakvvrahdfisglkdgyYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLE---- 531
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190
....*....|....*....|....*....|....*
gi 346645039 532 --RLLEGRTSFIIAHRLSTIKNSSRIFYIDNGRIQ 564
Cdd:smart00382 109 llLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
38-312 |
1.66e-09 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 59.05 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 38 TLFVILLANVATMIGPYLTKIVID--DTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFGH 115
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDalSAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRVFRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 116 LQKLPFSYFDSRPHGKiLIRVVNY-INMLSDLLSNGLINLISDILSVIVTLGFML-MIDPVLTLYSLALIpVLFVIVMVI 193
Cdd:cd18582 81 LHSLSLRFHLSRKTGA-LSRAIERgTRGIEFLLRFLLFNILPTILELLLVCGILWyLYGWSYALITLVTV-ALYVAFTIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 194 KTAQRKAYQVLSNKQSNM-NAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLwpgvqNI---AVM 269
Cdd:cd18582 159 VTEWRTKFRREMNEADNEaNAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALL-----NIgqaLII 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 346645039 270 TTCLIYFVGIKGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFY 312
Cdd:cd18582 234 SLGLTAIMLLAAQGVvagTLTVGDFVLVNTYLLQLYQPLNFLGFVY 279
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
367-581 |
4.43e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.52 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 367 LKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenveEVTLRSLRSQMGVMLqdtfifsgTIIENIR 446
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----EVSVIAISAGLSGQL--------TGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 447 YGKL--DATEEEIIA-AAKVVRahdfISGLKDGYYTEVKErgstLSAGQRQLISFARALLADPKILILDEATSSIDtQTe 523
Cdd:PRK13546 108 FKMLcmGFKRKEIKAmTPKIIE----FSELGEFIYQPVKK----YSSGMRAKLGFSINITVNPDILVIDEALSVGD-QT- 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346645039 524 iLLQEGLERLLE----GRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQHGYYYN 581
Cdd:PRK13546 178 -FAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYEAFLN 239
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
370-573 |
4.46e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.25 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTiinLLSRFYNI--NSGEILVDGENVEEVTLRSL--------RSQMGVMLQDTFifsg 439
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAAELarhraylsQQQTPPFAMPVF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 440 tiieniRYGKL---DATEEEIIAAAKVVRAHDFisGLKDGYYTEVkergSTLSAGQRQLISFARALL-----ADP--KIL 509
Cdd:PRK03695 88 ------QYLTLhqpDKTRTEAVASALNEVAEAL--GLDDKLGRSV----NQLSGGEWQRVRLAAVVLqvwpdINPagQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLLE-GRTSFIIAHRLS-TIKNSSRIFYIDNGRIQEAGSHEELM 573
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
366-519 |
5.24e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.65 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTI-INLLSRFYNIN-SGEILVDGEnveEVTLRSL--------------RSQMGV 429
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGK---EVDVSTVsdaidaglayvtedRKGYGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 430 MLQDTfifsgtIIENI---------RYGKLDATEEEIIA----AAKVVRAHDfisglkdgyyteVKERGSTLSAGQRQLI 496
Cdd:NF040905 352 NLIDD------IKRNItlanlgkvsRRGVIDENEEIKVAeeyrKKMNIKTPS------------VFQKVGNLSGGNQQKV 413
|
170 180
....*....|....*....|...
gi 346645039 497 SFARALLADPKILILDEATSSID 519
Cdd:NF040905 414 VLSKWLFTDPDVLILDEPTRGID 436
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
381-519 |
1.78e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.42 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 381 ALVGPTGAGKTTIINLLSRFYNINSGEI------LVDGENveEVTLRSLRSQMGVMLQDTFIFSG-TIIENIRYGkldat 453
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvLFDAEK--GICLPPEKRRIGYVFQDARLFPHyKVRGNLRYG----- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 454 eeeiiaAAKVVRAH-DFISGLKdGYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:PRK11144 101 ------MAKSMVAQfDKIVALL-GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
361-576 |
2.20e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.01 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 361 EEGVDILKGINFHVDAGESIALVGPTGAGKTTIIN-----LLSRFYNINSGEILVDGENVEEVTLRS-----------LR 424
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkeLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 425 SQMGVMLQ--DTFIFSGTIIENIRYGKLdATEEEIIAAAKVVRAHDFISGLKDGYYtevkERGS-TLSAGQRQLISFARA 501
Cdd:PRK13631 116 RRVSMVFQfpEYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLAKFYLNKMGLDDSYL----ERSPfGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 502 LLADPKILILDEATSSIDTQTE-ILLQEGLERLLEGRTSFIIAHRLSTI-KNSSRIFYIDNGRIQEAGS-HEELMAQH 576
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTpYEIFTDQH 268
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
363-524 |
2.25e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVE-EVTLRSLRSQMGVMLQD-TFIFSGT 440
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYGKLdATEEEIIAAAKVVRahDFISGLKD-GYYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSId 519
Cdd:PRK10982 90 VMDNMWLGRY-PTKGMFVDQDKMYR--DTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL- 165
|
....*
gi 346645039 520 TQTEI 524
Cdd:PRK10982 166 TEKEV 170
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
355-578 |
2.46e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 355 DVYFRYEEG-VDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFY-----NINSGEILVDGENVEEVTL-------- 420
Cdd:PRK10261 19 NIAFMQEQQkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLeqaggLVQCDKMLLRRRSRQVIELseqsaaqm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 421 RSLR-SQMGVMLQD-------TFIFSGTIIENIRYGKLDATEEEIIAAAKV---VRAHDFISGLkdGYYTEvkergsTLS 489
Cdd:PRK10261 99 RHVRgADMAMIFQEpmtslnpVFTVGEQIAESIRLHQGASREEAMVEAKRMldqVRIPEAQTIL--SRYPH------QLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 490 AGQRQLISFARALLADPKILILDEATSSIDT--QTEILlqeGLERLLEGRTSF---IIAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVtiQAQIL---QLIKVLQKEMSMgviFITHDMGVVAEiADRVLVMYQGEA 247
|
250
....*....|....*..
gi 346645039 564 QEAGSHEELM--AQHGY 578
Cdd:PRK10261 248 VETGSVEQIFhaPQHPY 264
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
39-297 |
5.89e-08 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 54.56 E-value: 5.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 39 LFVILLANVATMIGPYLTKIVID---------DTIPNKNMTQ-LFWIAVIFIVSVIVTGLcmryRIRSITLIGQDILKDM 108
Cdd:cd18780 2 TIALLVSSGTNLALPYFFGQVIDavtnhsgsgGEEALRALNQaVLILLGVVLIGSIATFL----RSWLFTLAGERVVARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 109 RTAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFV 188
Cdd:cd18780 78 RKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 189 IVMV----IKTAQRKAYQVLSNKQSnmnaYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLLWPGVQ 264
Cdd:cd18780 158 GAVIygkyVRKLSKKFQDALAAAST----VAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMG 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 346645039 265 NIAVMTTCLIYFVG----IKGygvDVSTGTLIAFIGY 297
Cdd:cd18780 234 AAAQLAIVLVLWYGgrlvIDG---ELTTGLLTSFLLY 267
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
72-280 |
6.58e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 54.38 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 72 LFWIAVIFIVSVI--VTGLCMRYrirSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPH--GKILIRVVNYINMLSDLL 147
Cdd:cd18578 52 NFWALMFLVLAIVagIAYFLQGY---LFGIAGERLTRRLRKLAFRAILRQDIAWFDDPENstGALTSRLSTDASDVRGLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 148 SNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQS 227
Cdd:cd18578 129 GDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVAS 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 228 FSREEENFEIFTE-VSNEYRRSWMKAVKIQFLLwpGV-QNIAVMTTCLIYFVGIK 280
Cdd:cd18578 209 LTLEDYFLEKYEEaLEEPLKKGLRRALISGLGF--GLsQSLTFFAYALAFWYGGR 261
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
354-573 |
7.25e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.02 E-value: 7.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQD 433
Cdd:PRK10575 15 RNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 TFIFSGTIIENI----RY------GKLDATEEEiiaaaKVVRAHDFIsGLKDGYYTEVkergSTLSAGQRQLISFARALL 503
Cdd:PRK10575 94 LPAAEGMTVRELvaigRYpwhgalGRFGAADRE-----KVEEAISLV-GLKPLAHRLV----DSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 504 ADPKILILDEATSSIDT--QTEILLQegLERLLEGRTSFIIAhRLSTIKNSSRifYID------NGRIQEAGSHEELM 573
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIahQVDVLAL--VHRLSQERGLTVIA-VLHDINMAAR--YCDylvalrGGEMIAQGTPAELM 236
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
352-565 |
8.42e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 8.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 352 DFKDVYFRYEeGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVdGENVEEVTLRSLRSQMgvml 431
Cdd:PRK11147 321 EMENVNYQID-GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHRAEL---- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 432 qDTfifSGTIIENIRYGKLDATeeeiiaaakvV--RAHDFISGLKDGYY------TEVKergsTLSAGQRQLISFARALL 503
Cdd:PRK11147 395 -DP---EKTVMDNLAEGKQEVM----------VngRPRHVLGYLQDFLFhpkramTPVK----ALSGGERNRLLLARLFL 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 504 ADPKILILDEATSSIDTQTeillQEGLERLLEGR--TSFIIAHRLSTIKN---SSRIFYiDNGRIQE 565
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVET----LELLEELLDSYqgTVLLVSHDRQFVDNtvtECWIFE-GNGKIGR 518
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
94-248 |
4.99e-07 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 51.78 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 94 IRSITLIGQDILKDMRTAIFGHLQKLPFSYFDSRPHGKILIRVVNYIN----MLSDLLSNGLINLISDILSVIVtlgfML 169
Cdd:cd18574 63 ISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQefksSFKQCVSQGLRSVTQTVGCVVS----LY 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346645039 170 MIDPVLTLYSLALIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRS 248
Cdd:cd18574 139 LISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKL 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
351-578 |
6.00e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVdGENveevtlrslrSQMGVM 430
Cdd:PRK15064 320 LEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-SEN----------ANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 LQDT---FIFSGTIIENIRYGKLDATEEEIIAAA--KVVRAHDfisglkdgyytEVKERGSTLSAGQRQLISFARALLAD 505
Cdd:PRK15064 388 AQDHaydFENDLTLFDWMSQWRQEGDDEQAVRGTlgRLLFSQD-----------DIKKSVKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 506 PKILILDEATSSIDTQTEILLQEGLErLLEGrTSFIIAH------RLSTiknssRIFYI-DNGRIQEAGSHEELMAQHGY 578
Cdd:PRK15064 457 PNVLVMDEPTNHMDMESIESLNMALE-KYEG-TLIFVSHdrefvsSLAT-----RIIEItPDGVVDFSGTYEEYLRSQGI 529
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
40-301 |
6.20e-07 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 51.19 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 40 FVIL-LANVATMIGPYLTKIVID----DTIPNKNMTQLFWIAVIFIVSVIVTGLcmryRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18590 2 FLFLtLAVICETFIPYYTGRVIDilggEYQHNAFTSAIGLMCLFSLGSSLSAGL----RGGLFMCTLSRLNLRLRHQLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIK 194
Cdd:cd18590 78 SLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 195 TAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEY-----RRSWMKAVKIQF--LLWPGVQniA 267
Cdd:cd18590 158 TYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTynlkdRRDTVRAVYLLVrrVLQLGVQ--V 235
|
250 260 270
....*....|....*....|....*....|....
gi 346645039 268 VMTTCLIYFVGiKGygvDVSTGTLIAFIGYVGNF 301
Cdd:cd18590 236 LMLYCGRQLIQ-SG---HLTTGSLVSFILYQKNL 265
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
372-563 |
6.40e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 372 FHVDAGESIALVGPTGAGKTTIINLLSrfyninsGEILVD-GENVEEVTLRSLRSQmgvmlQD----------TFIFSGt 440
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDdGRIIYEQDLIVARLQ-----QDpprnvegtvyDFVAEG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 iIENI-----RYGKL------DATEEEIIAAAKVVRAHDFISGLK-DGYYTEVKE--------RGSTLSAGQRQLISFAR 500
Cdd:PRK11147 91 -IEEQaeylkRYHDIshlvetDPSEKNLNELAKLQEQLDHHNLWQlENRINEVLAqlgldpdaALSSLSGGWLRKAALGR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346645039 501 ALLADPKILILDEATSSIDTQTeILLQEGLerLLEGRTSFI-IAHRLSTIKN-SSRIFYIDNGRI 563
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDIET-IEWLEGF--LKTFQGSIIfISHDRSFIRNmATRIVDLDRGKL 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
351-522 |
8.90e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 49.95 E-value: 8.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 351 VDFKDVYFRYEEGVD---ILKGINFHVDAGESIALVGPTGAGKTT----IINLLSRFYNINsGEILVDGENVEEVTLRSL 423
Cdd:cd03233 4 LSWRNISFTTGKGRSkipILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 424 RSQMGVMLQDTFIFSGTIIENIRYgkldateeeiiaAAKvVRAHDFISGlkdgyytevkergstLSAGQRQLISFARALL 503
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTVRETLDF------------ALR-CKGNEFVRG---------------ISGGERKRVSIAEALV 134
|
170
....*....|....*....
gi 346645039 504 ADPKILILDEATSSIDTQT 522
Cdd:cd03233 135 SRASVLCWDNSTRGLDSST 153
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
370-519 |
1.16e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTIINLLSRFY-NINSGEILVDGEnveEVTLRSLRSQMG---VML-----QDTFIFSGT 440
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpGRWEGEIFIDGK---PVKIRNPQQAIAqgiAMVpedrkRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 441 IIENIRYGKLD--ATEEEIIAAAKVVRAHDFISGLKdgyyteVKE-----RGSTLSAGQRQLISFARALLADPKILILDE 513
Cdd:PRK13549 358 VGKNITLAALDrfTGGSRIDDAAELKTILESIQRLK------VKTaspelAIARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
....*.
gi 346645039 514 ATSSID 519
Cdd:PRK13549 432 PTRGID 437
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
370-519 |
1.28e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRSQMGVMLQDTFIFSGTIIE------ 443
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSSGLYLDaplawn 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 346645039 444 --NIRYGKLDATEEEIIAAAKVVRAHDFIsGLKdgyYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:PRK15439 362 vcALTHNRRGFWIKPARENAVLERYRRAL-NIK---FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
362-569 |
2.44e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 362 EGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLS--RFYNINSGEILVDGENVEEVTLRSlRSQMGVMLQDTF---- 435
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIFMAFQYpvei 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 436 ------IFSGTIIENIR-YGKLDATE--------EEIIAAAKvvrahdfisgLKDGYYTEVKERGstLSAGQRQLISFAR 500
Cdd:PRK09580 91 pgvsnqFFLQTALNAVRsYRGQEPLDrfdfqdlmEEKIALLK----------MPEDLLTRSVNVG--FSGGEKKRNDILQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 346645039 501 ALLADPKILILDEATSSIDTQTEILLQEGLERLLEGRTSFIIAHRLSTIKNSSRIFYID---NGRIQEAGSH 569
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHvlyQGRIVKSGDF 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
328-574 |
2.67e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 328 TMDVEPDIKDIPNAkkMPPIVGNVDFKDVY-----FRYEEGVdiLKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYN 402
Cdd:PRK09700 239 RLMVGRELQNRFNA--MKENVSNLAHETVFevrnvTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 403 INSGEILVDGENVEEVT-LRSLRSQMGVMLQ---DTFIFSG-TIIENIR-------------YGKLDATEEEIIAAAkvv 464
Cdd:PRK09700 315 RAGGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFPNfSIAQNMAisrslkdggykgaMGLFHEVDEQRTAEN--- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 465 rAHDFISgLKdgyYTEVKERGSTLSAGQRQLISFARALLADPKILILDEATSSID--TQTEILlqeGLERLL--EGRTSF 540
Cdd:PRK09700 392 -QRELLA-LK---CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgAKAEIY---KVMRQLadDGKVIL 463
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 346645039 541 IIAHRLSTIKN-SSRIFYIDNGRI------QEAGSHEELMA 574
Cdd:PRK09700 464 MVSSELPEIITvCDRIAVFCEGRLtqiltnRDDMSEEEIMA 504
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
366-519 |
3.32e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLL---------SRFYNInSGEILVDGE---NVEEVTLRSLRSQMGVMLQD 433
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgggaPRGARV-TGDVTLNGEplaAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 434 TFIFS-------GTIIENIRYGKLDATEEEIIAAAkVVRAhdfisglkdGYYTEVKERGSTLSAGQRQLISFARAL---- 502
Cdd:PRK13547 95 AFAFSareivllGRYPHARRAGALTHRDGEIAWQA-LALA---------GATALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180
....*....|....*....|..
gi 346645039 503 -----LADPKILILDEATSSID 519
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALD 186
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
366-533 |
3.62e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.57 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 366 ILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILvdgenveevtlRSLRSQMGVMLQDTFIFSGTIIENI 445
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYVPQKLYLDTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 446 RYGKL--DATEEEIIAAAKVVRAHDFIsglkdgyytevKERGSTLSAGQRQLISFARALLADPKILILDEATSSIDTQTE 523
Cdd:PRK09544 88 RFLRLrpGTKKEDILPALKRVQAGHLI-----------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170
....*....|
gi 346645039 524 ILLQEGLERL 533
Cdd:PRK09544 157 VALYDLIDQL 166
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
370-519 |
7.06e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 7.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGenvEEVTLRSLRS--QMGVML------QDTFIFSGTI 441
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDaiRAGIMLcpedrkAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 442 IENI---------RYGKL--DATEEEIiaaakvvrAHDFISGLKdgyyteVKERGS-----TLSAGQRQLISFARALLAD 505
Cdd:PRK11288 349 ADNInisarrhhlRAGCLinNRWEAEN--------ADRFIRSLN------IKTPSReqlimNLSGGNQQKAILGRWLSED 414
|
170
....*....|....
gi 346645039 506 PKILILDEATSSID 519
Cdd:PRK11288 415 MKVILLDEPTRGID 428
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
38-293 |
7.64e-06 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 47.98 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 38 TLFVILLANVAtmigPYLTKIVIDDTIPNKNMTQLFWIAVIFIVSVIVTGLcMRYrIRSITL--IGQDILKDMRTAIFGH 115
Cdd:cd18586 11 SFFINLLALAP----PIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGL-LRQ-VRSRILqrVGLRLDVELGRRVFRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 116 LQKLPFsyfDSRPHGkilirvvNYINMLSDL------LSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVI 189
Cdd:cd18586 85 VLELPL---ESRPSG-------YWQQLLRDLdtlrnfLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 190 VMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREeenfeiftevsNEYRRSWMKAVKiQFLLWP-------- 261
Cdd:cd18586 155 AWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGML-----------GNLRRRWEARHA-ETLELQirasdlag 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 346645039 262 GVQNIA----VMTTCLIYFVG----IKGygvDVSTGTLIA 293
Cdd:cd18586 223 AISAIGktlrMALQSLILGVGaylvIDG---ELTIGALIA 259
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
354-515 |
7.70e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.87 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 354 KDVYFRYEEGVDILKGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGENVEEVTLRSLRsQMGVM--- 430
Cdd:COG3845 261 ENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR-RLGVAyip 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 431 ---LQDTFIFSGTIIEN----------------IRYGKLDATEEEIIAAAKvVRAHDfisglkdgyyteVKERGSTLSAG 491
Cdd:COG3845 340 edrLGRGLVPDMSVAENlilgryrrppfsrggfLDRKAIRAFAEELIEEFD-VRTPG------------PDTPARSLSGG 406
|
170 180
....*....|....*....|....*.
gi 346645039 492 --QRQLIsfARALLADPKILILDEAT 515
Cdd:COG3845 407 nqQKVIL--ARELSRDPKLLIAAQPT 430
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
39-324 |
1.05e-05 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 47.52 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 39 LFVILLA----NVATmigPYLTKIVIDDTIPNKnmTQLFWIAVIF-----------IVSVIVTGLCMRyrirsitlIGQD 103
Cdd:cd18583 1 CFLCLLAervlNVLV---PRQLGIIVDSLSGGS--GKSPWKEIGLyvllrflqsggGLGLLRSWLWIP--------VEQY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 104 ILKDMRTAIFGHLQKLPFSYFDSRPHGKIlIRVVNYINMLSDLLSNGLINLISDILSVIVTLG-FMLMIDPVLTLYsLAL 182
Cdd:cd18583 68 SYRALSTAAFNHVMNLSMDFHDSKKSGEV-LKAIEQGSSINDLLEQILFQIVPMIIDLVIAIVyLYYLFDPYMGLI-VAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 183 IPVLFVIVMVIKTA-QRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSwMKAVKIQFLLWP 261
Cdd:cd18583 146 VMVLYVWSTIKLTSwRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKA-ERKYLFSLNLLN 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 262 GVQNiAVMTTCLIYFVGIKGYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLER 324
Cdd:cd18583 225 AVQS-LILTLGLLAGCFLAAYQVsqgQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAER 289
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
32-192 |
1.14e-05 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 47.44 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 32 QKSIYITLFVILLANVATMIGPYLTKIVIDDTIPNKNMT--------QLFWI----AVIFIVSVIVTGLCMRYrirSITL 99
Cdd:cd18571 1 KKLILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNfiyliliaQLVLFlgstSIEFIRSWILLHISSRI---NISI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 100 IGQDILKDMRtaifghlqkLPFSYFDSRPHGKILIRVVNYiNMLSDLLSNGLINLISDILSVIVTLGfmlmidpVLTLYS 179
Cdd:cd18571 78 ISDFLIKLMR---------LPISFFDTKMTGDILQRINDH-SRIESFLTSSSLSILFSLLNLIVFSI-------VLAYYN 140
|
170
....*....|...
gi 346645039 180 laliPVLFVIVMV 192
Cdd:cd18571 141 ----LTIFLIFLI 149
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
37-325 |
1.66e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 47.10 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 37 ITLFVILLANVATMIGPYLTKIVID--DTIPNKNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTAIFG 114
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISylSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 115 HLQKLPFSYFDSRPHGKIlirvvnyINMLS------DLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFV 188
Cdd:cd18579 81 KALRLSSSARQETSTGEI-------VNLMSvdvqriEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 189 IVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREeenfEIFTEVSNEYRRSWMKAVK-------IQFLLWP 261
Cdd:cd18579 154 LQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWE----KPFLKRIEELRKKELKALRkfgylraLNSFLFF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 262 GVQNIAVMTTCLIYFVgikgYGVDVSTGTLIAFIGYVGNFWNPVINIGNFYNSLITATTYLERI 325
Cdd:cd18579 230 STPVLVSLATFATYVL----LGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
370-564 |
2.54e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.13 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFHVDAGESIALVGPTGAGKTTIINLLSRFY-NINSGEILVDGENVEEVT-LRSLRSQMGVMLQDT----FIFSGTIIE 443
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkrhgIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 444 NI------RYGKL----DATEEEIIAAA----KVVRAHDFISglkdgyytevkerGSTLSAGQRQLISFARALLADPKIL 509
Cdd:TIGR02633 359 NItlsvlkSFCFKmridAAAELQIIGSAiqrlKVKTASPFLP-------------IGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 346645039 510 ILDEATSSIDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQ 564
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLGlSDRVLVIGEGKLK 482
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
333-551 |
2.76e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 333 PDIKDIPNAKKMPPIVGNVDFKDVYFRYEEGVdILKGINFHVDAGESIALVGPTGAGKTTiinLLSrfyninsgeiLVDG 412
Cdd:PRK10938 243 PEPDEPSARHALPANEPRIVLNNGVVSYNDRP-ILHNLSWQVNPGEHWQIVGPNGAGKST---LLS----------LITG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 413 ENVE----EVTLRSLRSQMGVMLQDtfifsgtIIENIRY--------GKLDATEEEIIaaakvvrahdfISGLKD--GYY 478
Cdd:PRK10938 309 DHPQgysnDLTLFGRRRGSGETIWD-------IKKHIGYvssslhldYRVSTSVRNVI-----------LSGFFDsiGIY 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 479 TEVKERGS----------------------TLSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLL-E 535
Cdd:PRK10938 371 QAVSDRQQklaqqwldilgidkrtadapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsE 450
|
250 260
....*....|....*....|....*...
gi 346645039 536 GRTSFI------------IAHRLSTIKN 551
Cdd:PRK10938 451 GETQLLfvshhaedapacITHRLEFVPD 478
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
374-531 |
5.07e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 374 VDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGE------NVEEVTL------------RSLRSQMGVMLQDTF 435
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvNQETPALpqpaleyvidgdREYRQLEAQLHDANE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 436 IFSGTIIENIrYGKLDATEEEIIAAakvvRAHDFISGLkdGYYTEVKERG-STLSAGQRQLISFARALLADPKILILDEA 514
Cdd:PRK10636 104 RNDGHAIATI-HGKLDAIDAWTIRS----RAASLLHGL--GFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170
....*....|....*..
gi 346645039 515 TSSIDTQTEILLQEGLE 531
Cdd:PRK10636 177 TNHLDLDAVIWLEKWLK 193
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
363-574 |
1.79e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 363 GVDilkGINFHVDAGESIALVGPTGAGKTTIINLLSRFYNINSGEILVDGEnveEVTLRSLRSQM--GVML------QDT 434
Cdd:PRK10762 267 GVN---DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGH---EVVTRSPQDGLanGIVYisedrkRDG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 435 FIFSGTIIEN-----IRY-----GKLDAtEEEIIAAAKVVRA-------HDFISGLkdgyytevkergstLSAGQRQLIS 497
Cdd:PRK10762 341 LVLGMSVKENmsltaLRYfsragGSLKH-ADEQQAVSDFIRLfniktpsMEQAIGL--------------LSGGNQQKVA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 498 FARALLADPKILILDEATSSID--TQTEI------LLQEGLERLLegrtsfIIAHRLSTIKNSSRIFYIDNGRIQ----- 564
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVDvgAKKEIyqlinqFKAEGLSIIL------VSSEMPEVLGMSDRILVMHEGRISgeftr 479
|
250
....*....|
gi 346645039 565 EAGSHEELMA 574
Cdd:PRK10762 480 EQATQEKLMA 489
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
371-575 |
3.03e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 371 NFHVDAGESIALVGPTGAGKTTIINLLSrfyninsGE-ILVDGE---NVEEVTLRSLRsQMGVMLQDTFIFSGTiiENIR 446
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALA-------GElPLLSGErqsQFSHITRLSFE-QLQKLVSDEWQRNNT--DMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 447 YGKLDA--TEEEII------AAAKVVRAHDF-ISGLKDgyytevkERGSTLSAGQRQLISFARALLADPKILILDEATSS 517
Cdd:PRK10938 93 PGEDDTgrTTAEIIqdevkdPARCEQLAQQFgITALLD-------RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 518 IDTQTEILLQEGLERLL-EGRTSFIIAHRLSTIKN-SSRIFYIDNGRIQEAGSHEELMAQ 575
Cdd:PRK10938 166 LDVASRQQLAELLASLHqSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
370-544 |
5.15e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.87 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 370 INFH-VDAGESIALVGPTGAGKTTIINLLS-RFYninsGEILVDGENVEEVTLRSLRSQ-MGVMLqdTFIFSGTIIENIR 446
Cdd:cd03279 20 IDFTgLDNNGLFLICGPTGAGKSTILDAITyALY----GKTPRYGRQENLRSVFAPGEDtAEVSF--TFQLGGKKYRVER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 447 YGKLDATeeeiiaaakvvrahDFISG--LKDGYYTEVKERG-STLSAGQRQLISFARAL-LADP---------KILILDE 513
Cdd:cd03279 94 SRGLDYD--------------QFTRIvlLPQGEFDRFLARPvSTLSGGETFLASLSLALaLSEVlqnrggarlEALFIDE 159
|
170 180 190
....*....|....*....|....*....|..
gi 346645039 514 ATSSIDTQTEILLQEGLERL-LEGRTSFIIAH 544
Cdd:cd03279 160 GFGTLDPEALEAVATALELIrTENRMVGVISH 191
|
|
| AAA_17 |
pfam13207 |
AAA domain; |
383-539 |
6.52e-04 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 40.30 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 383 VGPTGAGKTTIINLLSRFYN---INSGEIlvdgenveevtLRSLRSQMGvmlqdtfifSGTIIENIRYGKLDATEEEIIA 459
Cdd:pfam13207 1 TGVPGSGKTTQLKKLAEKLGfphISAGDL-----------LREEAKERG---------LVEDRDEMRKLPLEPQKELQKL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 460 AAKVVRAHDFISG-LKDGYYTEVKERGstlsAGQRQLISFARALlaDPKILILdeatssIDTQTEILlqegLERLLEGRT 538
Cdd:pfam13207 61 AAERIAEEAGEGGvIVDGHPRIKTPAG----YLPGLPVEVLREL--KPDAIIL------LEADPEEI----LERRLKDRT 124
|
.
gi 346645039 539 S 539
Cdd:pfam13207 125 R 125
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
35-315 |
1.03e-03 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 41.47 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 35 IYITLFVILLANVATMIGP-YLTKIV--IDDTIPNkNMTQLFWIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDMRTA 111
Cdd:cd18556 4 FFSILFISLLSSILISISPvILAKITdlLTSSSSD-SYNYIVVLAALYVITISATKLLGFLSLYLQSSLRVELIISISSS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 112 IFGHLQKLPFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVM 191
Cdd:cd18556 83 YFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIVVILSSGDYFVAALFLLYAVLFVINN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 192 VIKT------------AQRKAYQVLSNKQSNMNAyihesiagIKVTQSFSREEENFEIF-TEVSNEYRRSWMKAVKIQFL 258
Cdd:cd18556 163 TIFTkkivslrndlmdAGRKSYSLLTDSVKNIVA--------AKQNNAFDFLFKRYEATlTNDRNSQKRYWKLTFKMLIL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 259 lwPGVQNIAVMTTCLIYFVgikgYGV---DVSTGTLIAFIGYVGNFWNPVINIGNFYNSL 315
Cdd:cd18556 235 --NSLLNVILFGLSFFYSL----YGVvngQVSIGHFVLITSYILLLSTPIESLGNMLSEL 288
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
455-519 |
1.23e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 1.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 346645039 455 EEIIAAAKVVRAHDFISGLKdgYYTEVKERGS-TLSAGQRQLISFARALLADPKILILDEATSSID 519
Cdd:PLN03073 313 ELIDAYTAEARAASILAGLS--FTPEMQVKATkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
361-424 |
1.46e-03 |
|
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443988 [Multi-domain] Cd Length: 386 Bit Score: 41.30 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 361 EEGVDILKGInfhVDAGESIALVGPTGAGKTTIINLLSRFynINSGEILV-----------------------DGENVEE 417
Cdd:COG4962 169 PEMAEFLRAA---VRARLNILVSGGTGSGKTTLLNALSGF--IPPDERIVtiedaaelqlqhphvvrletrppNVEGAGE 243
|
90
....*....|..
gi 346645039 418 VTLR-----SLR 424
Cdd:COG4962 244 VTLRdlvrnALR 255
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
358-535 |
2.10e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 358 FRYEEGVDILKGINfhvdagesiALVGPTGAGKTTIIN---------------LLSRFYNINSGEILVDGE-NVEEVTLR 421
Cdd:COG0419 13 YRDTETIDFDDGLN---------LIVGPNGAGKSTILEairyalygkarsrskLRSDLINVGSEEASVELEfEHGGKRYR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 422 SLRSQ-------------MGVMLQDtfIFSGTIIENIRyGKLDATEEEIIAAAKVVRAhdfISGLKDGYYTEVKERGS-- 486
Cdd:COG0419 84 IERRQgefaefleakpseRKEALKR--LLGLEIYEELK-ERLKELEEALESALEELAE---LQKLKQEILAQLSGLDPie 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 346645039 487 TLSAGQRQLISFARALLadpkiLILDeaTSSIDtqteillQEGLERLLE 535
Cdd:COG0419 158 TLSGGERLRLALADLLS-----LILD--FGSLD-------EERLERLLD 192
|
|
| PRK12727 |
PRK12727 |
flagellar biosynthesis protein FlhF; |
377-400 |
2.14e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 237182 [Multi-domain] Cd Length: 559 Bit Score: 41.13 E-value: 2.14e-03
10 20
....*....|....*....|....*
gi 346645039 377 GESIALVGPTGAGKTTII-NLLSRF 400
Cdd:PRK12727 350 GGVIALVGPTGAGKTTTIaKLAQRF 374
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
488-577 |
2.15e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 488 LSAGQRQLISFARALLADPKILILDEATSSIDTQT-----EILLQegLERlLEGRTSFIIAHRLSTIKNSSRIFYIDNGR 562
Cdd:NF033858 398 LPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVArdmfwRLLIE--LSR-EDGVTIFISTHFMNEAERCDRISLMHAGR 474
|
90
....*....|....*
gi 346645039 563 IQEAGSHEELMAQHG 577
Cdd:NF033858 475 VLASDTPAALVAARG 489
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
120-326 |
2.29e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 40.21 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 120 PFSYFDSRPHGKILIRVVNYINMLSDLLSNglinlisdILSVIVTLGFMLMIDPVLTLYSLALIPVLFVIVMVIKTAQRK 199
Cdd:cd18605 89 KMSFFDKTPVGRILNRFSSDVYTIDDSLPF--------ILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 200 AYQVLS--------NKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRS---------WMkAVKIQFLlwpg 262
Cdd:cd18605 161 YYRATSrelkrlnsVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAqlasqaasqWL-SIRLQLL---- 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 346645039 263 vqNIAVMTTCLIYFVGIKGYGVDVSTGTLIAFIGYvgnfwnpVINIGNFYNSLITATTYLERIF 326
Cdd:cd18605 236 --GVLIVTFVALTAVVQHFFGLSIDAGLIGLALSY-------ALPITGLLSGLLNSFTETEKEM 290
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
487-572 |
2.41e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 487 TLSAGQRQLISFARALLAD---PKILILDEATSSIDTQTEILLQEGLERLLE-GRTSFIIAHRLSTIKNSSRIfyID--- 559
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVIKTADYI--IDlgp 906
|
90
....*....|....*...
gi 346645039 560 -----NGRIQEAGSHEEL 572
Cdd:TIGR00630 907 eggdgGGTVVASGTPEEV 924
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
104-295 |
2.99e-03 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 39.77 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 104 ILKDMRTAIFGHLQKLP---FSYFDSrphGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYSL 180
Cdd:cd18585 66 LLSNLRVWFYRKLEPLAparLQKYRS---GDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 181 A-LIPVLFVIVMVIKTAQRKAYQVLSNKQSNMNAYIHESIAGIKVTQSFSREEENFEIFTEVSNEYRRSWMKAVKIQFLL 259
Cdd:cd18585 143 AgLLLAGVVIPLLFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLS 222
|
170 180 190
....*....|....*....|....*....|....*.
gi 346645039 260 WPGVQNIAVMTTCLIYFVGIKGYGVDVSTGTLIAFI 295
Cdd:cd18585 223 QALMILLSGLTVWLVLWLGAPLVQNGALDGALLAML 258
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
361-397 |
3.46e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.92 E-value: 3.46e-03
10 20 30
....*....|....*....|....*....|....*..
gi 346645039 361 EEGVDILKGinfHVDAGESIALVGPTGAGKTTIINLL 397
Cdd:PRK01889 182 GEGLDVLAA---WLSGGKTVALLGSSGVGKSTLVNAL 215
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
120-232 |
3.74e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 39.77 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 120 PFSYFDSRPHGKILIRVVNYINMLSDLLSNGLINLISDILSVIVTLGFMLMIDPVLtlySLALIPVLFVIVMVIKTAQRK 199
Cdd:cd18606 82 PMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWF---AIALPPLLVLYYFIANYYRAS 158
|
90 100 110
....*....|....*....|....*....|....*.
gi 346645039 200 AYQVL---SNKQSNMNAYIHESIAGIKVTQSFSREE 232
Cdd:cd18606 159 SRELKrleSILRSFVYANFSESLSGLSTIRAYGAQD 194
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
488-593 |
4.04e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.79 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 488 LSAGQRQLISFARALLADPKILILDEATSSIDTQTEILLQEGLERLLE--GRTSFIIAHRLSTI-KNSSRIFYIDNGRIQ 564
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQTV 238
|
90 100 110
....*....|....*....|....*....|.
gi 346645039 565 EAGSHEELMA--QHGYYYNLYQSQFDMLQAL 593
Cdd:PRK15093 239 ETAPSKELVTtpHHPYTQALIRAIPDFGSAM 269
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
65-240 |
4.50e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 39.47 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 65 PNKNMTQLfwIAVIFIVSVIVTGLCMRYRIRSITLIGQDILKDmrtAIFGHLQKLPFSYFDSRPHGKILIRVVNYINMLS 144
Cdd:cd18599 55 PDLNFYQL--VYGGSILVILLLSLIRGFVFVKVTLRASSRLHN---KLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 145 DLLSNGLINLISDILSVIVTLGFMLMIDPVLTLYsLALIPVLFVIVMVI-KTAQRKAYQVLSNKQSNMNAYIHESIAGIK 223
Cdd:cd18599 130 VRLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIA-LIPLAIIFVFLSKIfRRAIRELKRLENISRSPLFSHLTATIQGLS 208
|
170
....*....|....*..
gi 346645039 224 VTQSFSREEENFEIFTE 240
Cdd:cd18599 209 TIHAFNKEKEFLSKFKK 225
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
43-293 |
5.82e-03 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 38.96 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 43 LLANVATMIGPYLTKIVIDDTIPNKNMTQLfWIAVIFIVSVIVTGLCMRY-RIRSITLIGQDILKDMRTAIFGHLQKLPF 121
Cdd:cd18587 12 LLINLFALASPLFVMNVYDRVVPNNAIETL-WVLAIGVLIALLFDFILKLlRAYFIDVAGKRADVILSSRLFERVLGLRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 122 SyfdSRPhgkilIRVVNYINMLS------DLLSNGLINLISDILSVIVTLGFMLMIDPVLtlyslALIPVLFVIVMVI-- 193
Cdd:cd18587 91 E---ARP-----ASVGSFANNLRefesvrDFFTSATLTALIDLPFVLLFLAVIALIGGPL-----ALVPLVAIPLVLLyg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 194 -------KTAQRKAYQVLSNKqsnmNAYIHESIAGIKVTQSFSREeenfeiftevsNEYRRSWMKAV--------KIQFL 258
Cdd:cd18587 158 lllqkplRRLVEESMRESAQK----NALLVESLSGLETIKALGAE-----------GRMQRRWEEAVaalarsslKSRLL 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 346645039 259 lwpgvQNIAVMTTCLIY---FVGIKGYGV------DVSTGTLIA 293
Cdd:cd18587 223 -----SSSATNFAQFVQqlvTVAIVIVGVylisdgELTMGGLIA 261
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
374-422 |
7.53e-03 |
|
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.
Pssm-ID: 410874 [Multi-domain] Cd Length: 177 Bit Score: 37.90 E-value: 7.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 346645039 374 VDAGESIALVGPTGAGKTTIINLLSRFynINSGEILVDGENVEEVTLRS 422
Cdd:cd01130 9 VRARKNILISGGTGSGKTTLLNALLSF--IPPDERIVTIEDTRELQLPH 55
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
39-210 |
9.73e-03 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 38.38 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 39 LFVILLANVATMIGPYLTKIVIDD-TIPNKNMTQLFWIAVIFIVSVIV---------TGLCMRYRIRSITLIGQDILKDM 108
Cdd:cd18581 2 LLLLAAGRVVNVLVPILYKKIVDSlTPDSADSPLAFPWALILLYVFLKflqgggsgsVGLLSNLRSFLWIPVQQFTTREI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346645039 109 RTAIFGHLQKLPFSYFDSRPHGKILiRVVNY-INMLSDLLSNGLINLISDILSVIVTLGFML-MIDPVLTLYSLALIpVL 186
Cdd:cd18581 82 SVKLFAHLHSLSLRWHLSRKTGEVL-RVMDRgTSSINSLLSYVLFNIGPTIADIIIAIIYFAiAFNPWFGLIVFVTM-AL 159
|
170 180
....*....|....*....|....
gi 346645039 187 FVIVMVIKTAQRKAYQVLSNKQSN 210
Cdd:cd18581 160 YLILTIIITEWRTKFRREMNKLDN 183
|
|
| |
