|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-567 |
1.27e-174 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 506.62 E-value: 1.27e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 7 KILNWMRPYKARMILGFSMSFLNAIFIALPIFLAAKIFNNVLSHKPiyMKDILNVVIIMVLLVIGRFITAYFKSKSHESI 86
Cdd:COG1132 11 RLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGD--LSALLLLLLLLLGLALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 87 AYEMSAKERLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSLLAC 166
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 167 IGVLLSFFAIQLLERKSRqnaPAYHNVQNQ---LVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTKIEMQYI 243
Cdd:COG1132 169 LVLPLLLLVLRLFGRRLR---KLFRRVQEAlaeLNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 244 PFNLLHLLSLKVVSIMIVLVACLLYMNHSIDLPTLIMISIFSFVIFDSVENINSAAHVLEMIDMTIDDIEKIKNAPEL-- 321
Cdd:COG1132 246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEip 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 322 -DENGKNLTIKNENIAFQNVNFSYD-DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIK 399
Cdd:COG1132 326 dPPGAVPLPPVRGEIEFENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 400 DMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRI 479
Cdd:COG1132 406 DLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRI 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 480 SIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARG 565
|
....*...
gi 613101153 560 GMYQDFIR 567
Cdd:COG1132 566 GLYARLYR 573
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-567 |
4.99e-119 |
|
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: 368.01 E-value: 4.99e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 8 ILNWMRPYKARMILGFSMSFLNAIF-IALPIFLAAkIFNNVLSHKpiyMKDILNV-VIIMVLLVIGRFITAYFKSKSHES 85
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLaLATPLFTQV-VIDRVLPNQ---DLSTLWVlAIGLLLALLFEGLLRLLRSYLLLR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 86 IAYEMSAKERLDIGDKLKNVRLGYFNSHHSNELTTIVTtDLTFLENFAMK-MVDVVVNG------------YIliivlil 152
Cdd:COG2274 223 LGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGsLLTALLDLlfvliflivlffYS------- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 153 sllvvsWQVSLLACIG----VLLSFFAIQLLERKSRQNAPAYHNVQNQLVEkvleVIRGIQVIKSFAKENTSLKSFNQSV 228
Cdd:COG2274 295 ------PPLALVVLLLiplyVLLGLLFQPRLRRLSREESEASAKRQSLLVE----TLRGIETIKALGAESRFRRRWENLL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 229 NESKRINTKIE-MQYIPFNLLHLLSlKVVSIMIVLVACLLYMNHSIDLPTLIMISIFSFVIFDSVENINSAAHVLEMIDM 307
Cdd:COG2274 365 AKYLNARFKLRrLSNLLSTLSGLLQ-QLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKI 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 308 TIDDIEKIKNAPELDENGKNLTIKNE---NIAFQNVNFSY--DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLR 382
Cdd:COG2274 444 ALERLDDILDLPPEREEGRSKLSLPRlkgDIELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 383 FYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQT 462
Cdd:COG2274 524 LYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDT 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 463 MLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLN 542
Cdd:COG2274 604 VVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLD 683
|
570 580
....*....|....*....|....*
gi 613101153 543 EGEIIQKGSHDELIRKPGMYQDFIR 567
Cdd:COG2274 684 KGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-560 |
1.52e-109 |
|
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: 339.04 E-value: 1.52e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 8 ILNWMRPYKARMILGFSMSFLNAIFIALPIFLAAKIFNNVLSHKPIYMkDILNVVIIMVLLVIGRFITAYFKskshESIA 87
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLS-ALLPLLGLLLAVLLLRALLAWLR----ERAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 88 YEMSAKERLDIGDKL--KNVRLG--YFNSHHSNELTTIVTTDLTFLENFAMK-------------MVDVVVngyiliivl 150
Cdd:COG4988 83 FRAAARVKRRLRRRLleKLLALGpaWLRGKSTGELATLLTEGVEALDGYFARylpqlflaalvplLILVAV--------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 151 ilslLVVSWQVSL-LACIGVLLSFFAI---QLLERKSRQNAPAYHNVQNQLvekvLEVIRGIqviksfakenTSLKSFNQ 226
Cdd:COG4988 154 ----FPLDWLSGLiLLVTAPLIPLFMIlvgKGAAKASRRQWRALARLSGHF----LDRLRGL----------TTLKLFGR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 227 SVNESKRINTKIE-----------MQyipfnllhLLSLKV------VSIMIVLV-ACLLYMNHSIDLPTLIMISIFSFVI 288
Cdd:COG4988 216 AKAEAERIAEASEdfrkrtmkvlrVA--------FLSSAVleffasLSIALVAVyIGFRLLGGSLTLFAALFVLLLAPEF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 289 F-----------DSVENINSAAHVLEMIDMtiddiekikNAPELDENGKNLTIKNEN-IAFQNVNFSYDD-KQVIKNVNF 355
Cdd:COG4988 288 FlplrdlgsfyhARANGIAAAEKIFALLDA---------PEPAAPAGTAPLPAAGPPsIELEDVSFSYPGgRPALDGLSL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 356 EIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGA 435
Cdd:COG4988 359 TIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 436 TKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINE 515
Cdd:COG4988 439 SDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 613101153 516 LSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPG 560
Cdd:COG4988 519 LAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
335-564 |
9.83e-105 |
|
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: 314.94 E-value: 9.83e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY--DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISA 412
Cdd:cd03251 1 VEFKNVTFRYpgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPII 492
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613101153 493 ILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPGMYQD 564
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
335-564 |
1.64e-104 |
|
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: 314.55 E-value: 1.64e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDD-KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAV 413
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 414 FQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIII 493
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 494 LDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPGMYQD 564
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
311-562 |
8.76e-101 |
|
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: 317.53 E-value: 8.76e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 311 DIEK----------IKNAPeldeNGKNLTIKNENIAFQNVNFSYD-DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHL 379
Cdd:COG5265 328 DMERmfdlldqppeVADAP----DAPPLVVGGGEVRFENVSFGYDpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 380 LLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEG 459
Cdd:COG5265 404 LFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDG 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 460 YQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQII 539
Cdd:COG5265 484 YDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEIL 563
|
250 260
....*....|....*....|...
gi 613101153 540 VLNEGEIIQKGSHDELIRKPGMY 562
Cdd:COG5265 564 VLEAGRIVERGTHAELLAQGGLY 586
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
334-560 |
3.97e-98 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 297.98 E-value: 3.97e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 334 NIAFQNVNFSYD-DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISA 412
Cdd:cd03254 2 EIEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPII 492
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 493 ILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPG 560
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-562 |
7.12e-97 |
|
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: 306.64 E-value: 7.12e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 6 FKILNWMRPYKARMILGFSMSFLNA----IFIALPIFLAAKIFNNVLSHKPIYMKdiLNVVIIMVLLVIGRFITAYFKSK 81
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAatesTLAALLKPLLDDGFGGRDRSVLWWVP--LVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 82 SHESIAYEMsakeRLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQV 161
Cdd:TIGR02203 81 VSNKVVRDI----RVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 162 SLLACIGVLLSFFAIQLLERKSRQNAPAYHNVQNQLVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTKIEMQ 241
Cdd:TIGR02203 157 TLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 242 ---YIPF-NLLHLLSLKVVsIMIVLVACLLYMNHSIDLPTLIMISIFSFVIFDSVENIN--------SAAHVLEMIDmti 309
Cdd:TIGR02203 237 gsiSSPItQLIASLALAVV-LFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNapmqrglaAAESLFTLLD--- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 310 ddiekikNAPELDENGKNLTIKNENIAFQNVNFSY--DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDID 387
Cdd:TIGR02203 313 -------SPPEKDTGTRAIERARGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 388 DGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPG-ATKEEIIRAAKQACCHDFIMSLPEGYQTMLNE 466
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 467 KGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEI 546
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
570
....*....|....*.
gi 613101153 547 IQKGSHDELIRKPGMY 562
Cdd:TIGR02203 546 VERGTHNELLARNGLY 561
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
335-567 |
9.21e-95 |
|
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: 289.44 E-value: 9.21e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYD---DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKIS 411
Cdd:cd03249 1 IEFKNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPI 491
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 492 IILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPGMYQDFIR 567
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
7-569 |
9.13e-89 |
|
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: 285.44 E-value: 9.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 7 KILNWMRPYKARMIL-GFSMSFLNAIFIALPIFLAAKIFNNVLSHKPIYMKDILNVVIIMVL-LVIGRFITAYFKSKSHE 84
Cdd:TIGR02204 8 ALWPFVRPYRGRVLAaLVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALvLALGTAARFYLVTWLGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 85 SIayemSAKERLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSLL 164
Cdd:TIGR02204 88 RV----VADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 165 ACIGVLLSFFAIQLLERKSRQNAPAYHNVQNQLVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNES-----KRINTKIe 239
Cdd:TIGR02204 164 VLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAyeaarQRIRTRA- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 240 mqyipfnllhLLSLKVVSIMIVLVACLLYMN-HSI--------DLPTLIMISIF---SFVIFDSVEN-INSAAHVLEMId 306
Cdd:TIGR02204 243 ----------LLTAIVIVLVFGAIVGVLWVGaHDViagkmsagTLGQFVFYAVMvagSIGTLSEVWGeLQRAAGAAERL- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 307 mtiddIEKIKNAPELDENGKNLTIKNE---NIAFQNVNFSYD---DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL 380
Cdd:TIGR02204 312 -----IELLQAEPDIKAPAHPKTLPVPlrgEIEFEQVNFAYParpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 381 LRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGY 460
Cdd:TIGR02204 387 LRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGY 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 461 QTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIV 540
Cdd:TIGR02204 467 DTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVV 546
|
570 580
....*....|....*....|....*....
gi 613101153 541 LNEGEIIQKGSHDELIRKPGMYQDFIRIK 569
Cdd:TIGR02204 547 MDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
164-568 |
1.42e-87 |
|
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: 282.04 E-value: 1.42e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 164 LACIGVLLSFFAIQLLERKSRQNAPAyhnvQNQLVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTKIEMQYI 243
Cdd:COG4987 165 LLLAGLLLPLLAARLGRRAGRRLAAA----RAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 244 PFNLLHLLSLKVVSIMIVLVACLLYMNHSIDLPTLIMISIFSFVIFDSV-----------ENINSAAHVLEMIDMTIDDI 312
Cdd:COG4987 241 LAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALaplpaaaqhlgRVRAAARRLNELLDAPPAVT 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 313 EKIKNAPELDENGknltiknenIAFQNVNFSYDD--KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGI 390
Cdd:COG4987 321 EPAEPAPAPGGPS---------LELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 391 IRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSN 470
Cdd:COG4987 392 ITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRR 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 471 LSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKG 550
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQG 551
|
410
....*....|....*...
gi 613101153 551 SHDELIRKPGMYQDFIRI 568
Cdd:COG4987 552 THEELLAQNGRYRQLYQR 569
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-562 |
2.80e-86 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 282.38 E-value: 2.80e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 6 FKILNWMRPYKARMILGFSMSFLNAIF-IALPiFLAAKIFNNVLSHKPIYmkDILNVVIIMVLLVIGRFITAYFKSKSHE 84
Cdd:TIGR00958 150 FRLLGLSGRDWPWLISAFVFLTLSSLGeMFIP-FYTGRVIDTLGGDKGPP--ALASAIFFMCLLSIASSVSAGLRGGSFN 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 85 sIAYE-MSAKERLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSL 163
Cdd:TIGR00958 227 -YTMArINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTM 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 164 LACIGVLLSFFA-------IQLLERKSrQNAPAYhnvQNQLVEkvlEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINT 236
Cdd:TIGR00958 306 VTLINLPLVFLAekvfgkrYQLLSEEL-QEAVAK---ANQVAE---EALSGMRTVRSFAAEEGEASRFKEALEETLQLNK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 237 KIEMQYIPFnllhlLSLKVVSIMIVLVACLLYMNHSIDLPTLIMISIFSFVIF----------------DSVENINSAAH 300
Cdd:TIGR00958 379 RKALAYAGY-----LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYqeqlgeavrvlsyvysGMMQAVGASEK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 301 VLEMIDMTiddiekiknaPELDENG----KNLtikNENIAFQNVNFSY---DDKQVIKNVNFEIPTQTSTAIIGPSGSGK 373
Cdd:TIGR00958 454 VFEYLDRK----------PNIPLTGtlapLNL---EGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGK 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 374 STLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFI 453
Cdd:TIGR00958 521 STVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFI 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 454 MSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINelSKGKTVITIAHKLETIK 533
Cdd:TIGR00958 601 MEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVE 678
|
570 580
....*....|....*....|....*....
gi 613101153 534 NADQIIVLNEGEIIQKGSHDELIRKPGMY 562
Cdd:TIGR00958 679 RADQILVLKKGSVVEMGTHKQLMEDQGCY 707
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
159-569 |
1.70e-83 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 271.89 E-value: 1.70e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 159 WQVSL-LACIGVLLSFfAIQLLERKSRQNAPAYHNVQNQLVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTK 237
Cdd:PRK11176 165 WQLSLiLIVIAPIVSI-AIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMK 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 238 I-EMQYIPFNLLHLLSlkvvSIMIVLVaclLYMNhsiDLPTLI-MISIFSF-VIFD----------SVENINS------- 297
Cdd:PRK11176 244 MvSASSISDPIIQLIA----SLALAFV---LYAA---SFPSVMdTLTAGTItVVFSsmialmrplkSLTNVNAqfqrgma 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 298 AAHVLemidMTIDDIEkiknaPELDENGKNLTIKNENIAFQNVNFSYD--DKQVIKNVNFEIPTQTSTAIIGPSGSGKST 375
Cdd:PRK11176 314 ACQTL----FAILDLE-----QEKDEGKRVIERAKGDIEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKST 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 376 LCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGA-TKEEIIRAAKQACCHDFIM 454
Cdd:PRK11176 385 IANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFIN 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 455 SLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKN 534
Cdd:PRK11176 465 KMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK 544
|
410 420 430
....*....|....*....|....*....|....*
gi 613101153 535 ADQIIVLNEGEIIQKGSHDELIRKPGMYQDFIRIK 569
Cdd:PRK11176 545 ADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
297-567 |
1.76e-82 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 269.14 E-value: 1.76e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 297 SAAHVLEMIDM--TIDDIEKIKNAPELdENGKNLtiknenIAFQNVNFSYDDK-QVIKNVNFEI-PTQTsTAIIGPSGSG 372
Cdd:PRK13657 302 AAPKLEEFFEVedAVPDVRDPPGAIDL-GRVKGA------VEFDDVSFSYDNSrQGVEDVSFEAkPGQT-VAIVGPTGAG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 373 KSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDF 452
Cdd:PRK13657 374 KSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDF 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 453 IMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETI 532
Cdd:PRK13657 454 IERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTV 533
|
250 260 270
....*....|....*....|....*....|....*
gi 613101153 533 KNADQIIVLNEGEIIQKGSHDELIRKPGMYQDFIR 567
Cdd:PRK13657 534 RNADRILVFDNGRVVESGSFDELVARGGRFAALLR 568
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
335-562 |
6.98e-76 |
|
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: 240.85 E-value: 6.98e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY--DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISA 412
Cdd:cd03252 1 ITFEHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPII 492
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 493 ILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPGMY 562
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLY 230
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-570 |
2.13e-72 |
|
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: 245.04 E-value: 2.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 18 RMILGFSMsFLNAIFIALPIFLAAkIFNNVLSHKPIYMKDILNVViiMVLLVIGRFITAYFKSK--SHES--IAYEMSAK 93
Cdd:TIGR01846 142 REVLLISL-ALQLFALVTPLLFQV-VIDKVLVHRGLSTLSVLALA--MLAVAIFEPALGGLRTYlfAHLTsrIDVELGAR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 94 erldIGDKLKNVRLGYFNSHHSNELTTIV---TTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSLLACIGVL 170
Cdd:TIGR01846 218 ----LYRHLLGLPLGYFESRRVGDTVARVrelEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYAL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 171 LSFFAIQLLERKSRQNAPAYHNVQNQLVEKVleviRGIQVIKSFAKE----NTSLKSFNQSVNESKRIntkIEMQYIPFN 246
Cdd:TIGR01846 294 LSVFVGPILRKRVEDKFERSAAATSFLVESV----TGIETIKATATEpqfqNRWDRQLAAYVAASFRV---TNLGNIAGQ 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 247 LLHLLSlKVVSIMIVLVACLLYMNHSIDLPTLIMISIFSFVIFDSVENINSAAHVLEMIDMTIDDIEKIKNAPEldENGK 326
Cdd:TIGR01846 367 AIELIQ-KLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPT--EPRS 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 327 N----LTIKNENIAFQNVNFSY--DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKD 400
Cdd:TIGR01846 444 AglaaLPELRGAITFENIRFRYapDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAI 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 401 MTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRIS 480
Cdd:TIGR01846 524 ADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIA 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 481 IARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPG 560
Cdd:TIGR01846 604 IARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQG 683
|
570
....*....|
gi 613101153 561 MYQDFIRIKS 570
Cdd:TIGR01846 684 LYARLWQQQS 693
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
335-545 |
2.36e-70 |
|
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: 223.80 E-value: 2.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDD--KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISA 412
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKVYLFNDTIENNIlfgnpgatkeeiiraakqacchdfimslpegyqtmlnekgsnLSGGEKQRISIARAILKDAPII 492
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 613101153 493 ILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGE 545
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
13-541 |
4.46e-69 |
|
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: 232.18 E-value: 4.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 13 RPYKARMILgfsMSFLNAIFIALPIFLAAKIFNNVLSHKPiYMKDILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMSA 92
Cdd:TIGR02857 2 RRALALLAL---LGVLGALLIIAQAWLLARVVDGLISAGE-PLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 93 KERLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSL-LACIGVLL 171
Cdd:TIGR02857 78 QLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLiLLLTAPLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 172 SFFAIQLL---ERKSRQNapayHNVQNQLVEKVLEVIRGIQVIKSFAKENTSLKSFNQSvNESKRINTkieMQYIPFNLL 248
Cdd:TIGR02857 158 PIFMILIGwaaQAAARKQ----WAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRS-SEEYRERT---MRVLRIAFL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 249 HLLSLKVV-SIMIVLVACLL---YMNHSIDLPTLIMISI-----------FSFVIFDSVENINSAAHVLEMIDmtiddie 313
Cdd:TIGR02857 230 SSAVLELFaTLSVALVAVYIgfrLLAGDLDLATGLFVLLlapefylplrqLGAQYHARADGVAAAEALFAVLD------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 314 kiKNAPELDENGKNLTIKNENIAFQNVNFSYDDK-QVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIR 392
Cdd:TIGR02857 303 --AAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 393 IDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLS 472
Cdd:TIGR02857 381 VNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLS 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 473 GGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVL 541
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
30-567 |
4.51e-67 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 228.06 E-value: 4.51e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 30 AIFIALPIFLAAKIFNNVlSHKPIYMKDILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMSAKERLDIGDKLKNVRLGY 109
Cdd:PRK10789 8 AMLQLIPPKVVGIIVDGV-TEQHMTTGQILMWIGTMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQLSRQHPEF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 110 FNSHHSNELTTIVTTD------------LTFLENFAMKMVDVVVngyiliivlilSLLVVSWQVSLLACI-----GVLLS 172
Cdd:PRK10789 87 YLRHRTGDLMARATNDvdrvvfaagegvLTLVDSLVMGCAVLIV-----------MSTQISWQLTLLALLpmpvmAIMIK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 173 FFAIQLLER-KSRQNAPAYHNVQNQlvekvlEVIRGIQVIKSFAKENTSLKSFNQSVNESKRIN---TKIEMQ-----YI 243
Cdd:PRK10789 156 RYGDQLHERfKLAQAAFSSLNDRTQ------ESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNmrvARIDARfdptiYI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 244 PFNLLHLLSLKVVSIMIVlvacllymNHSIDLPTLImisifSFVI---------------FDSVENiNSAAHvlEMIDMT 308
Cdd:PRK10789 230 AIGMANLLAIGGGSWMVV--------NGSLTLGQLT-----SFVMylglmiwpmlalawmFNIVER-GSAAY--SRIRAM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 309 IDDiekiknAPELDENGKNLTIKNENIAFQNVNFSY--DDKQVIKNVNFEI-PTQTsTAIIGPSGSGKSTLCHLLLRFYD 385
Cdd:PRK10789 294 LAE------APVVKDGSEPVPEGRGELDVNIRQFTYpqTDHPALENVNFTLkPGQM-LGICGPTGSGKSTLLSLIQRHFD 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 386 IDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLN 465
Cdd:PRK10789 367 VSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 466 EKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGE 545
Cdd:PRK10789 447 ERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGH 526
|
570 580
....*....|....*....|..
gi 613101153 546 IIQKGSHDELIRKPGMYQDFIR 567
Cdd:PRK10789 527 IAQRGNHDQLAQQSGWYRDMYR 548
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
159-567 |
3.64e-66 |
|
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: 225.92 E-value: 3.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 159 WQVSL-LACIGVLLSFFAIQLLERKSRQNAPAYHNVQNqLVEKVLEVIRGIQVIKSFAK---ENTSLKSFNQSVneskri 234
Cdd:TIGR01192 156 WRLSIvLMVLGILYILIAKLVMQRTKNGQAAVEHHYHN-VFKHVSDSISNVSVVHSYNRieaETSALKQFTNNL------ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 235 ntkIEMQYIPFNLLHLLS-----LKVVSIMIVLV-ACLLYMNHSIDLPTLIMISIFSFVIFDSVENIN--------SAAH 300
Cdd:TIGR01192 229 ---LSAQYPVLDWWALASglnrmASTISMMCILViGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSgfitqifeARAK 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 301 VLEMIDM--TIDDIEKIKNAPELDengknlTIKNEnIAFQNVNFSY-DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLC 377
Cdd:TIGR01192 306 LEDFFDLedSVFQREEPADAPELP------NVKGA-VEFRHITFEFaNSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLI 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 378 HLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLP 457
Cdd:TIGR01192 379 NLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRS 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 458 EGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQ 537
Cdd:TIGR01192 459 NGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADL 538
|
410 420 430
....*....|....*....|....*....|
gi 613101153 538 IIVLNEGEIIQKGSHDELIRKPGMYQDFIR 567
Cdd:TIGR01192 539 VLFLDQGRLIEKGSFQELIQKDGRFYKLLR 568
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
335-546 |
7.07e-63 |
|
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: 206.17 E-value: 7.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY---DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKIS 411
Cdd:cd03248 12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPI 491
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 492 IILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEI 546
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
334-551 |
2.26e-59 |
|
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: 196.95 E-value: 2.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 334 NIAFQNVNFSY--DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKIS 411
Cdd:cd03244 2 DIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKVYLFNDTIENNI-LFGNpgATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAP 490
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 491 IIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGS 551
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
295-567 |
3.34e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 206.98 E-value: 3.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 295 INSAAHVLEMIDMTIDdiekiknaPELDENGKnLTIKNENIAFQNVNFSYDDKQ--VIKNVNFEIPTQTSTAIIGPSGSG 372
Cdd:PRK11160 308 IASARRINEITEQKPE--------VTFPTTST-AAADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 373 KSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDF 452
Cdd:PRK11160 379 KSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 453 IMSlPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETI 532
Cdd:PRK11160 459 LED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGL 537
|
250 260 270
....*....|....*....|....*....|....*
gi 613101153 533 KNADQIIVLNEGEIIQKGSHDELIRKPGMYQDFIR 567
Cdd:PRK11160 538 EQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
334-550 |
2.38e-58 |
|
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: 194.35 E-value: 2.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 334 NIAFQNVNFSYDDKQ--VIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKIS 411
Cdd:cd03245 2 RIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPI 491
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 492 IILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKG 550
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
342-567 |
1.58e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 191.60 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 342 FSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRF--YDIDDGIIRidgVDIKDMTLSTLMSKISAVFQKVYL 419
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQGSLKING---IELRELDPESWRKHLSWVGQNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 420 FNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATS 499
Cdd:PRK11174 435 PHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 500 SIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPGMYQDFIR 567
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
201-566 |
2.02e-51 |
|
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: 188.02 E-value: 2.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 201 VLEVIRGIQVIKSFAKENTSLKS----FNQSVNESKRiNTKIEMQYIPFNLLHLLSLKVVsimIVLVACLLYMNHSIDLP 276
Cdd:TIGR01193 337 IIEDLNGIETIKSLTSEAERYSKidseFGDYLNKSFK-YQKADQGQQAIKAVTKLILNVV---ILWTGAYLVMRGKLTLG 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 277 TLIMISIFSFVIFDSVENINSAAHVLEMIDMTIDDIEKIKNAPELDENGKNLTIK---NENIAFQNVNFSYD-DKQVIKN 352
Cdd:TIGR01193 413 QLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELnnlNGDIVINDVSYSYGyGSNILSD 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 353 VNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGN 432
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGA 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 433 -PGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQT 511
Cdd:TIGR01193 573 kENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVN 652
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 512 AINELsKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPGMYQDFI 566
Cdd:TIGR01193 653 NLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
334-558 |
1.94e-49 |
|
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: 179.94 E-value: 1.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 334 NIAFQNVNFSY--DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLL----------RFydiddgiiriDGVDIKDM 401
Cdd:COG4618 330 RLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVgvwpptagsvRL----------DGADLSQW 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 402 TLSTLMSKISAVFQKVYLFNDTIENNI-LFGNPgaTKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRIS 480
Cdd:COG4618 400 DREELGRHIGYLPQDVELFDGTIAENIaRFGDA--DPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 481 IARAILKDAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRK 558
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
335-545 |
1.24e-46 |
|
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: 162.25 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQ-----VIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLrfydiddgiiridgvdiKDMTLS----T 405
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL-----------------GELEKLsgsvS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 406 LMSKISAVFQKVYLFNDTIENNILFGNPgaTKEEIIRAAKQACC--HDFIMsLPEGYQTMLNEKGSNLSGGEKQRISIAR 483
Cdd:cd03250 64 VPGSIAYVSQEPWIQNGTIRENILFGKP--FDEERYEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613101153 484 AILKDAPIIILDEATSSIDPE-NEQLIQTAIN-ELSKGKTVITIAHKLETIKNADQIIVLNEGE 545
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHvGRHIFENCILgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
203-563 |
1.68e-45 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 169.51 E-value: 1.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 203 EVIRGIQVIKSFAKEntslKSFNQSVNESKRINTKIEMQYIP---FNLLHLLSLkvvsiMIVLVACLLYMNHSIDLPTLI 279
Cdd:PRK10790 209 EVINGMSVIQQFRQQ----ARFGERMGEASRSHYMARMQTLRldgFLLRPLLSL-----FSALILCGLLMLFGFSASGTI 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 280 MISI-FSFVIFDSVEN-----INSAAHVLEMIDMTIDDIEKIKNAPELDENGKNLTIKNENIAFQNVNFSY-DDKQVIKN 352
Cdd:PRK10790 280 EVGVlYAFISYLGRLNeplieLTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRPLQSGRIDIDNVSFAYrDDNLVLQN 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 353 VNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGN 432
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 433 PgATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTA 512
Cdd:PRK10790 440 D-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQA 518
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 513 INELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPG----MYQ 563
Cdd:PRK10790 519 LAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGrywqMYQ 573
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-529 |
1.70e-44 |
|
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: 165.61 E-value: 1.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 9 LNWMRPY----KARMILGFSMSFLNAIFIALPIFLAAKIFNNVLSHKPIYMkdiLNVVIIMV-LLVIGRFITAYFKS-KS 82
Cdd:TIGR02868 1 LLRILPLlkprRRRLALAVLLGALALGSAVALLGVSAWLISRAAEMPPVLY---LSVAAVAVrAFGIGRAVFRYLERlVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 83 HEsIAYEMSAKERLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVS 162
Cdd:TIGR02868 78 HD-AALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 163 LLACIGVLLSFFAIQLLE-RKSRQNAPAYHNVQNQLVEKVLEVIRGIQVIKSFAKENTSLKSfnqsVNESKRINTKIEMQ 241
Cdd:TIGR02868 157 LILAAGLLLAGFVAPLVSlRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQ----VEEADRELTRAERR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 242 YIPFNLL----HLLSLKVVSIMIVLVACLLYMNHSIDLPTLIMISIFSFVIFDSVENINSAAHVLEMIDMTIDDIEKIKN 317
Cdd:TIGR02868 233 AAAATALgaalTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 318 APELDENG-----KNLTIKNENIAFQNVNFSYDDKQ-VIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGII 391
Cdd:TIGR02868 313 AAGPVAEGsapaaGAVGLGKPTLELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 392 RIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNL 471
Cdd:TIGR02868 393 TLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARL 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 472 SGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKL 529
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
335-559 |
1.08e-43 |
|
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: 155.18 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY-DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAV 413
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 414 FQ--KVYLFNDTIENNILFG--NPGATKEEIIRAAKQACcHDFimslpeGYQTMLNEKGSNLSGGEKQRISIARAILKDA 489
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpeNLGLPREEIRERVEEAL-ELV------GLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613101153 490 PIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETI-KNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
335-550 |
2.07e-42 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 150.16 E-value: 2.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYD--DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTlSTLMSKISA 412
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKVYLFNDTIENNIlfgnpgatkeeiiraakqacchdfimslpegyqtmlnekGSNLSGGEKQRISIARAILKDAPII 492
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 493 ILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKG 550
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
316-568 |
4.22e-42 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 162.89 E-value: 4.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 316 KNAPELDENGkNLTIKNEN-----IAFQNVNFSYDDKQ---VIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDID 387
Cdd:PTZ00265 1143 KSNIDVRDNG-GIRIKNKNdikgkIEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLK 1221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 388 DGIIRIDG------------------------------------------------------VDIKDMTLSTLMSKISAV 413
Cdd:PTZ00265 1222 NDHHIVFKnehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsgkilldgVDICDYNLKDLRNLFSIV 1301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 414 FQKVYLFNDTIENNILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIII 493
Cdd:PTZ00265 1302 SQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILL 1381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 494 LDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKNADQIIVLNE----GEIIQ-KGSHDELIR-KPGMYQDF 565
Cdd:PTZ00265 1382 LDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKY 1461
|
...
gi 613101153 566 IRI 568
Cdd:PTZ00265 1462 VKL 1464
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
347-558 |
1.05e-41 |
|
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: 157.89 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 347 KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIEN 426
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 427 NILFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENE 506
Cdd:TIGR01842 411 NIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGE 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 613101153 507 QLIQTAINELSK-GKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRK 558
Cdd:TIGR01842 491 QALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
335-555 |
4.98e-41 |
|
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: 148.10 E-value: 4.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDI-------KDMTLSTLM 407
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLdgkdiydLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 408 SKISAVFQKVYLFNDTIENNILFG------NPGATKEEIIRAAKQacchdfIMSLPEgyQTMLNEKGSNLSGGEKQRISI 481
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEALR------KAALWD--EVKDRLHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 482 ARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDEL 555
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
337-545 |
1.67e-40 |
|
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: 146.07 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 337 FQNVNFSYDD--KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVF 414
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 Q--KVYLFNDTIENNILFG--NPGATKEEIIRAAKQACchdFIMSLpegyQTMLNEKGSNLSGGEKQRISIARAILKDAP 490
Cdd:cd03225 82 QnpDDQFFGPTVEEEVAFGleNLGLPEEEIEERVEEAL---ELVGL----EGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 491 IIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETIKN-ADQIIVLNEGE 545
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
335-546 |
4.25e-40 |
|
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: 143.90 E-value: 4.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQ--VIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISA 412
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKVYLFNDTIENNILfgnpgatkeeiiraakqacchdfimslpegyqtmlnekgsnlSGGEKQRISIARAILKDAPII 492
Cdd:cd03246 81 LPQDDELFSGSIAENIL------------------------------------------SGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 493 ILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETIKNADQIIVLNEGEI 546
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-559 |
1.21e-39 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 155.57 E-value: 1.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 2 FQITFKILnwmrPYKARMILGfsMSFLNAIFI--ALPIFLAakIFNNVLSHKPIyMKDILNVVIIMVLLVIGRFITAYFK 79
Cdd:PTZ00265 47 FFLPFKCL----PASHRKLLG--VSFVCATISggTLPFFVS--VFGVIMKNMNL-GENVNDIIFSLVLIGIFQFILSFIS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 80 SKSHESIAYEMsakerldigdkLKNVRLGYFNS-------HHSNELTTIVTTDLTF-LENFAMKMVDVVVNGYILIIVLI 151
Cdd:PTZ00265 118 SFCMDVVTTKI-----------LKTLKLEFLKSvfyqdgqFHDNNPGSKLTSDLDFyLEQVNAGIGTKFITIFTYASAFL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 152 LSLLVVSWQ-VSLLACIGVLLSFFAI--QLLERKSRQNAPAYHNVQNQLVEKVLEVIRGIQVIKSFAKENTSLKSFNQSV 228
Cdd:PTZ00265 187 GLYIWSLFKnARLTLCITCVFPLIYIcgVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 229 N-ESKRINTKIEMQYIPFNLLHLLSLKVVSI-------MIVLVACLLYMNHSIDLPTLI------MISIFSFVIFdsVEN 294
Cdd:PTZ00265 267 KlYSKYILKANFMESLHIGMINGFILASYAFgfwygtrIIISDLSNQQPNNDFHGGSVIsillgvLISMFMLTII--LPN 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 295 INSAAHVLEMidmTIDDIEKIKNAPELDENGKNLTIKN-ENIAFQNVNFSYD---DKQVIKNVNFEIPTQTSTAIIGPSG 370
Cdd:PTZ00265 345 ITEYMKSLEA---TNSLYEIINRKPLVENNDDGKKLKDiKKIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 371 SGKSTLCHLLLRFYDIDDGIIRIDGV-DIKDMTLSTLMSKISAVFQKVYLFNDTIENNILFG----------------NP 433
Cdd:PTZ00265 422 CGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 434 GATKE-----------------------------------------EIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLS 472
Cdd:PTZ00265 502 NDSQEnknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLS 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 473 GGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL--SKGKTVITIAHKLETIKNADQIIVLNEGEIIQKG 550
Cdd:PTZ00265 582 GGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIRYANTIFVLSNRERGSTV 661
|
....*....
gi 613101153 551 SHDELIRKP 559
Cdd:PTZ00265 662 DVDIIGEDP 670
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
335-551 |
4.76e-39 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 142.17 E-value: 4.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY--DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISA 412
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKVYLFNDTIENNI-LFGNpgATKEEIIRAAKqacchdfimslpegyqtmLNEKGSNLSGGEKQRISIARAILKDAPI 491
Cdd:cd03369 87 IPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 492 IILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGS 551
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
335-546 |
3.74e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.87 E-value: 3.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVF 414
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKVYLFNDTIENNILFG----NPGATKEEIIRAAKQACchdfimsLPEGYqtmLNEKGSNLSGGEKQRISIARAILKDAP 490
Cdd:COG4619 81 QEPALWGGTVRDNLPFPfqlrERKFDRERALELLERLG-------LPPDI---LDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 491 IIILDEATSSIDPENEQLIQTAINEL--SKGKTVITIAHKLETIKN-ADQIIVLNEGEI 546
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
335-558 |
1.85e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 133.27 E-value: 1.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLStLMSKISAVF 414
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKVYLFND-TIENNI-----LFGNPGATKEEIIRAAKQACchdfimSLPEgyqtMLNEKGSNLSGGEKQRISIARAILKD 488
Cdd:COG1131 80 QEPALYPDlTVRENLrffarLYGLPRKEARERIDELLELF------GLTD----AADRKVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613101153 489 APIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETI-KNADQIIVLNEGEIIQKGSHDELIRK 558
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
337-545 |
4.27e-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: 129.29 E-value: 4.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 337 FQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQk 416
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 vylfndtiennilfgnpgatkeeiiraakqacchdfimslpegyqtmlnekgsnLSGGEKQRISIARAILKDAPIIILDE 496
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 613101153 497 ATSSIDPENEQLIQTAINELS-KGKTVITIAHKLETIKNA-DQIIVLNEGE 545
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
177-562 |
1.11e-33 |
|
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: 137.38 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 177 QLLERKSRQNAPAYHNVQnqlvekvlEVIRGIQVIKSFAKENTSLKSFNQSVNEskriNTKIEMQYIPFNLLHLLSLKVV 256
Cdd:TIGR00957 1131 QLKRLESVSRSPVYSHFN--------ETLLGVSVIRAFEEQERFIHQSDLKVDE----NQKAYYPSIVANRWLAVRLECV 1198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 257 SIMIVLVACLLYM--NHSIDlPTLIMISI-FSFVIfdsVENINSAAHVLEMIDMTIDDIEKIKnapELDENGKNLTIKNE 333
Cdd:TIGR00957 1199 GNCIVLFAALFAVisRHSLS-AGLVGLSVsYSLQV---TFYLNWLVRMSSEMETNIVAVERLK---EYSETEKEAPWQIQ 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 334 NIA------------FQNVNFSY--DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIK 399
Cdd:TIGR00957 1272 ETAppsgwpprgrveFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA 1351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 400 DMTLSTLMSKISAVFQKVYLFNDTIENNI-LFGNpgATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQR 478
Cdd:TIGR00957 1352 KIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQL 1429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 479 ISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRK 558
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
....
gi 613101153 559 PGMY 562
Cdd:TIGR00957 1510 RGIF 1513
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
335-560 |
1.30e-33 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 129.09 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDD--KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHL---LLrfydiddgIIRIDGVDIKDM------TL 403
Cdd:TIGR04520 1 IEVENVSFSYPEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLlngLL--------LPTSGKVTVDGLdtldeeNL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 404 STLMSKISAVFQkvylfN-D------TIENNILFG--NPGATKEEIIR----AAKQACCHDFIMSLPegyqtmlnekgSN 470
Cdd:TIGR04520 73 WEIRKKVGMVFQ-----NpDnqfvgaTVEDDVAFGleNLGVPREEMRKrvdeALKLVGMEDFRDREP-----------HL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 471 LSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKNADQIIVLNEGEIIQ 548
Cdd:TIGR04520 137 LSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVA 216
|
250
....*....|....*...
gi 613101153 549 KG------SHDELIRKPG 560
Cdd:TIGR04520 217 EGtpreifSQVELLKEIG 234
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
335-567 |
1.34e-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: 128.19 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY-DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAV 413
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 414 FQKVYLF-NDTIENNI-----LFGNPgatKEEIIRAAKQACChdfIMSLPEgyQTMLNEKGSNLSGGEKQRISIARAILK 487
Cdd:cd03295 81 IQQIGLFpHMTVEENIalvpkLLKWP---KEKIRERADELLA---LVGLDP--AEFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 488 DAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKL-ETIKNADQIIVLNEGEIIQKGSHDELIRKPGmyQD 564
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSPA--ND 230
|
...
gi 613101153 565 FIR 567
Cdd:cd03295 231 FVA 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-561 |
2.82e-33 |
|
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: 133.49 E-value: 2.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY--DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGV---DIKDMTLSTLMSK 409
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLdgrDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 410 ISAVFQ--KVYLFNDTIENNILFG--NPGATKEEIIRAAKQAcchdfimsLPE-GYQTMLNEKGSNLSGGEKQRISIARA 484
Cdd:COG1123 85 IGMVFQdpMTQLNPVTVGDQIAEAleNLGLSRAEARARVLEL--------LEAvGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 485 ILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKPGM 561
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
328-555 |
3.19e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.80 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 328 LTIKNENIAFQNVNFSY--DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLST 405
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 406 LMSKISAVFQKV--YLFNDTIENNILFG------NPGATKEEIIRAAKQACCHDFIMSLPEgyqtmlnekgsNLSGGEKQ 477
Cdd:PRK13632 81 IRKKIGIIFQNPdnQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 478 RISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDEL 555
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-557 |
7.55e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.97 E-value: 7.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiddGIIRIDGVDIKDMTLSTLMSKISAVF 414
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGL-----LPPTSGTVRLFGKPPRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QK----------VYlfnDTIENNI-----LFGNPGATKEEIIRAAkqacchdfimslpegyqtmLNEKG---------SN 470
Cdd:COG1121 82 QRaevdwdfpitVR---DVVLMGRygrrgLFRRPSRADREAVDEA-------------------LERVGledladrpiGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 471 LSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETI-KNADQIIVLNeGEIIQ 548
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVrEYFDRVLLLN-RGLVA 218
|
....*....
gi 613101153 549 KGSHDELIR 557
Cdd:COG1121 219 HGPPEEVLT 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
335-546 |
1.61e-32 |
|
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: 124.52 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDD----KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL----------LRFydiddgiiriDGVDIKD 400
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILggldrptsgeVRV----------DGTDISK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 401 MTLSTLMS----KISAVFQKVYLFND-TIENNILFgnP----GATKEEIIRAAKQACCHdfiMSLPEGyqtmLNEKGSNL 471
Cdd:cd03255 71 LSEKELAAfrrrHIGFVFQSFNLLPDlTALENVEL--PlllaGVPKKERRERAEELLER---VGLGDR----LNHYPSEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 472 SGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKNADQIIVLNEGEI 546
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
331-563 |
4.49e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 124.91 E-value: 4.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 331 KNENIAFQNVNFSYDD--KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMS 408
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 409 ---KISAVFQKV--YLFNDTIENNILFG--NPGATKEEIIRAAKQACCH----DFIMSLPegyqtmlnekgSNLSGGEKQ 477
Cdd:PRK13640 82 ireKVGIVFQNPdnQFVGATVGDDVAFGleNRAVPRPEMIKIVRDVLADvgmlDYIDSEP-----------ANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 478 RISIArAILKDAP-IIILDEATSSIDPENEQLIQTAINELSKGK--TVITIAHKLETIKNADQIIVLNEGEIIQKGSHDE 554
Cdd:PRK13640 151 RVAIA-GILAVEPkIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
....*....
gi 613101153 555 LIRKPGMYQ 563
Cdd:PRK13640 230 IFSKVEMLK 238
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
328-550 |
9.45e-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: 9.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 328 LTIKNENIAFQNVNFSyddKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMT---LS 404
Cdd:cd03257 2 LEVKNLSVSFPTGGGS---VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 405 TLMSKISAVFQKVYL-FN------DTIENNILFGNPGATKEEIIRAAKQACCHdfiMSLPEgyqTMLNEKGSNLSGGEKQ 477
Cdd:cd03257 79 IRRKEIQMVFQDPMSsLNprmtigEQIAEPLRIHGKLSKKEARKEAVLLLLVG---VGLPE---EVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 478 RISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKG 550
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
335-557 |
1.53e-31 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 122.23 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMS---KIS 411
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKVYLFND-TIENNILFgnP----GATKEEIIRAAKQACCHDFimslpeGYQTMLNEKGSNLSGGEKQRISIARAIL 486
Cdd:cd03261 81 MLFQSGALFDSlTVFENVAF--PlrehTRLSEEEIREIVLEKLEAV------GLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613101153 487 KDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETI-KNADQIIVLNEGEIIQKGSHDELIR 557
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
335-556 |
2.20e-31 |
|
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: 122.46 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVF 414
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKVYL-FNDTIENNIL---------FGNPGATKEEIIRAAKQAC-CHDFIMSLpegyqtmLNEkgsnLSGGEKQRISIAR 483
Cdd:COG1120 82 QEPPApFGLTVRELVAlgryphlglFGRPSAEDREAVEEALERTgLEHLADRP-------VDE----LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 484 AILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLE-TIKNADQIIVLNEGEIIQKGSHDELI 556
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
337-550 |
2.25e-31 |
|
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: 121.09 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 337 FQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiddGIIRIDGVDIKDMTLSTLMS---KISAV 413
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL-----ERPDSGEILIDGRDVTGVPPerrNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 414 FQKVYLF-NDTIENNILFG--NPGATKEEIIRAAKQACchdFIMSLPEgyqtMLNEKGSNLSGGEKQRISIARAILKDAP 490
Cdd:cd03259 78 FQDYALFpHLTVAENIAFGlkLRGVPKAEIRARVRELL---ELVGLEG----LLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613101153 491 IIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKL-ETIKNADQIIVLNEGEIIQKG 550
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
334-559 |
2.99e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.40 E-value: 2.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 334 NIAFQNVNFSYDDKqvIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiDDGIIRIDGVDIKDMTlSTLMSK--IS 411
Cdd:COG3840 1 MLRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGF---LPPDSGRILWNGQDLT-ALPPAErpVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKVYLFND-TIENNILFG-NPG-----ATKEEIIRAAKQAcchdfimslpeGYQTMLNEKGSNLSGGEKQRISIARA 484
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGlRPGlkltaEQRAQVEQALERV-----------GLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 485 ILKDAPIIILDEATSSIDP----ENEQLIQTAINELskGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPalrqEMLDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
337-550 |
3.70e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 120.33 E-value: 3.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 337 FQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiddGIIRIDGVDIKDMTLSTLMSKISAVFQK 416
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGL-----LKPTSGSIRVFGKPLEKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 VYL---FNDTIENNIL---------FGNPGATKEEIIRAAkqaccHDFImslpeGYQTMLNEKGSNLSGGEKQRISIARA 484
Cdd:cd03235 77 RSIdrdFPISVRDVVLmglyghkglFRRLSKADKAKVDEA-----LERV-----GLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 485 ILKDAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETI-KNADQIIVLNeGEIIQKG 550
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLN-RTVVASG 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
331-557 |
3.88e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.43 E-value: 3.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 331 KNENIAFQNVNFSYDD--KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHL---LLRFydiddgiiRIDGVDIKDMTLST 405
Cdd:PRK13635 2 KEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLlngLLLP--------EAGTITVGGMVLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 406 -----LMSKISAVFQkvylfN-------DTIENNILFG--NPGATKEEIIRAAKQAcchdfimsLPE-GYQTMLNEKGSN 470
Cdd:PRK13635 74 etvwdVRRQVGMVFQ-----NpdnqfvgATVQDDVAFGleNIGVPREEMVERVDQA--------LRQvGMEDFLNREPHR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 471 LSGGEKQRISIArAILKDAP-IIILDEATSSIDPENEQLIQTAINEL--SKGKTVITIAHKLETIKNADQIIVLNEGEII 547
Cdd:PRK13635 141 LSGGQKQRVAIA-GVLALQPdIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEIL 219
|
250
....*....|
gi 613101153 548 QKGSHDELIR 557
Cdd:PRK13635 220 EEGTPEEIFK 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
335-555 |
4.11e-31 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 121.24 E-value: 4.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMT---LSTLMSKIS 411
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKVYLFND-TIENNILFG---NPGATKEEIIRAAKQAcchdfimslpegyqtmLNEKG---------SNLSGGEKQR 478
Cdd:COG1127 86 MLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLEK----------------LELVGlpgaadkmpSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 479 ISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDEL 555
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
335-567 |
7.67e-31 |
|
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: 120.78 E-value: 7.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDD--KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISA 412
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKVYLFNDTIENNIlfgNP--GATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAP 490
Cdd:cd03288 100 ILQDPILFSGSIRFNL---DPecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 491 IIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELI-RKPGMYQDFIR 567
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVR 254
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
335-545 |
8.23e-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: 118.44 E-value: 8.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMS--KISA 412
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKVYLF-NDTIENNILFGnpgatkeeiiraakqacchdfimslpegyqtmlnekgsnLSGGEKQRISIARAILKDAPI 491
Cdd:cd03229 81 VFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 492 IILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKL-ETIKNADQIIVLNEGE 545
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLdEAARLADRVVVLRDGK 178
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
311-567 |
3.05e-30 |
|
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: 126.60 E-value: 3.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 311 DIEKIKNAPELDENGKNLTIKNENIAFqnvnfSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLrfydiDDGI 390
Cdd:TIGR00957 620 EPDSIERRTIKPGEGNSITVHNATFTW-----ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALL-----AEMD 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 391 IRIDGVDIKdmtlstlmSKISAVFQKVYLFNDTIENNILFGNPgaTKEEIIRAAKQACC--HDFIMsLPEGYQTMLNEKG 468
Cdd:TIGR00957 690 KVEGHVHMK--------GSVAYVPQQAWIQNDSLRENILFGKA--LNEKYYQQVLEACAllPDLEI-LPSGDRTEIGEKG 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 469 SNLSGGEKQRISIARAILKDAPIIILDEATSSIDPE-NEQLIQTAINE--LSKGKTVITIAHKLETIKNADQIIVLNEGE 545
Cdd:TIGR00957 759 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPegVLKNKTRILVTHGISYLPQVDVIIVMSGGK 838
|
250 260
....*....|....*....|..
gi 613101153 546 IIQKGSHDELIRKPGMYQDFIR 567
Cdd:TIGR00957 839 ISEMGSYQELLQRDGAFAEFLR 860
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
335-547 |
3.36e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 118.22 E-value: 3.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDK----QVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL----------LRFydiddgiiriDGVDIKD 400
Cdd:COG1136 5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrptsgeVLI----------DGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 401 MT---LSTL-MSKISAVFQKVYLFND-TIENNILFgnP----GATKEEIIRAAKQAcchdfIMSLpeGYQTMLNEKGSNL 471
Cdd:COG1136 75 LSereLARLrRRHIGFVFQFFNLLPElTALENVAL--PlllaGVSRKERRERAREL-----LERV--GLGDRLDHRPSQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 472 SGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKNADQIIVLNEGEII 547
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
338-550 |
3.98e-30 |
|
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: 116.38 E-value: 3.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKV 417
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 418 YLFNdtIENnilfgnpgatkeeiiraakqacchdfimslpegyqtmLNEKGSN-LSGGEKQRISIARAILKDAPIIILDE 496
Cdd:cd03214 83 ELLG--LAH-------------------------------------LADRPFNeLSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 497 ATSSIDPENEQLIQTAINELSK--GKTVITIAHKLE-TIKNADQIIVLNEGEIIQKG 550
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-559 |
5.31e-30 |
|
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: 123.86 E-value: 5.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY-----DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMT---LSTL 406
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 407 MSKISAVFQKVYL-FN--DTIENNILFG---NPGATKEEIIRAAKQAcchdfiMS---LPEGYqtmLNEKGSNLSGGEKQ 477
Cdd:COG1123 341 RRRVQMVFQDPYSsLNprMTVGDIIAEPlrlHGLLSRAERRERVAEL------LErvgLPPDL---ADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 478 RISIARAILKDAPIIILDEATSSIDPeneqLIQTAI----NELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKG 550
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDV----SVQAQIlnllRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
....*....
gi 613101153 551 SHDELIRKP 559
Cdd:COG1123 488 PTEEVFANP 496
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-559 |
1.53e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.06 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTL--C---------------HLLLRfydiddgiiridGVD 397
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLlrClnrmndlipgarvegEILLD------------GED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 398 I--KDMTLSTLMSKISAVFQKVYLFNDTIENNILFG------NPGATKEEIIRAA-KQAcchdfimSLPEGYQTMLNEKG 468
Cdd:COG1117 80 IydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESlRKA-------ALWDEVKDRLKKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 469 SNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHkletikN-------ADQIIVL 541
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTH------NmqqaarvSDYTAFF 226
|
250
....*....|....*...
gi 613101153 542 NEGEIIQKGSHDELIRKP 559
Cdd:COG1117 227 YLGELVEFGPTEQIFTNP 244
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
335-546 |
1.40e-28 |
|
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: 111.72 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLStLMSKISAVF 414
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKVYLFndtiennilfgnPGATKEEIIRaakqacchdfimslpegyqtmlnekgsnLSGGEKQRISIARAILKDAPIIIL 494
Cdd:cd03230 80 EEPSLY------------ENLTVRENLK----------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 613101153 495 DEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETIKN-ADQIIVLNEGEI 546
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
161-560 |
1.64e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 121.24 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 161 VSLLACIGVLLSFFAIQLLERKSRQNAPAYHNVQNQLVEKVL-EVIRGIQVIKSFakentslksfnQSVNESKRINTKIE 239
Cdd:PLN03232 1051 ISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFgEALNGLSSIRAY-----------KAYDRMAKINGKSM 1119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 240 MQYIPFNLLHL-----LSLKVVS---IMIVLVACLLYM------NHSIDLPTLIMISIFSFVIFDSVENINSAAHVLEMi 305
Cdd:PLN03232 1120 DNNIRFTLANTssnrwLTIRLETlggVMIWLTATFAVLrngnaeNQAGFASTMGLLLSYTLNITTLLSGVLRQASKAEN- 1198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 306 dmTIDDIEKIKN-------APELDENGKNLT--IKNENIAFQNVNFSYDDK--QVIKNVNFEIPTQTSTAIIGPSGSGKS 374
Cdd:PLN03232 1199 --SLNSVERVGNyidlpseATAIIENNRPVSgwPSRGSIKFEDVHLRYRPGlpPVLHGLSFFVSPSEKVGVVGRTGAGKS 1276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 375 TLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNIlfgNPGATKEE--IIRAAKQACCHDF 452
Cdd:PLN03232 1277 SMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDadLWEALERAHIKDV 1353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 453 IMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETI 532
Cdd:PLN03232 1354 IDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTI 1433
|
410 420
....*....|....*....|....*...
gi 613101153 533 KNADQIIVLNEGEIIQKGSHDELIRKPG 560
Cdd:PLN03232 1434 IDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
335-563 |
1.99e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 121.00 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYD---DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRfydiddgiiridgvDIKDMTLST--LMSK 409
Cdd:PLN03130 615 ISIKNGYFSWDskaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLG--------------ELPPRSDASvvIRGT 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 410 ISAVFQKVYLFNDTIENNILFGNP--GATKEEIIRAAkqACCHDfIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILK 487
Cdd:PLN03130 681 VAYVPQVSWIFNATVRDNILFGSPfdPERYERAIDVT--ALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 488 DAPIIILDEATSSIDPE-NEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPGMYQ 563
Cdd:PLN03130 758 NSDVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQ 834
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
335-560 |
3.86e-28 |
|
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: 112.67 E-value: 3.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDK----QVIKNVNFEIPTQTSTAIIGPSGSGKSTL--CHLLLRFYDIDDGIiridgVDIKDMT------ 402
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLirCINGLERPTSGSVL-----VDGTDLTllsgke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 403 LSTLMSKISAVFQKVYLFND-TIENNILFgnP----GATKEEIIRAAKQacchdfimsLPEgyQTMLNEKG----SNLSG 473
Cdd:cd03258 77 LRKARRRIGMIFQHFNLLSSrTVFENVAL--PleiaGVPKAEIEERVLE---------LLE--LVGLEDKAdaypAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 474 GEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKG 550
Cdd:cd03258 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEG 223
|
250
....*....|
gi 613101153 551 SHDELIRKPG 560
Cdd:cd03258 224 TVEEVFANPQ 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
335-559 |
6.39e-28 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 112.01 E-value: 6.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL----------LRFydiddgiiRIDGVDIKDMTLS 404
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlleepdsgtITV--------DGEDLTDSKKDIN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 405 TLMSKISAVFQKVYLFND-TIENNILFGnP----GATKEEiirAAKQAcchdfiMSLPE--GyqtmLNEKG----SNLSG 473
Cdd:COG1126 74 KLRRKVGMVFQQFNLFPHlTVLENVTLA-PikvkKMSKAE---AEERA------MELLErvG----LADKAdaypAQLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 474 GEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGS 551
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKeGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
....*...
gi 613101153 552 HDELIRKP 559
Cdd:COG1126 220 PEEFFENP 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
335-555 |
7.61e-28 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 111.89 E-value: 7.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY-DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDI---KDMTLSTLMSKI 410
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 411 SAVFQKVYLFND-TIENNILFGNPGA-----------TKEEIIRAAkqACCHDFIMSlpegyqTMLNEKGSNLSGGEKQR 478
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglfPKEEKQRAL--AALERVGLL------DKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 479 ISIARAILKDAPIIILDEATSSIDPEN-EQLIQT--AINElSKGKTVITIAHKLETIK-NADQIIVLNEGEIIQKGSHDE 554
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASsRQVMDLlkRINR-EEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAE 231
|
.
gi 613101153 555 L 555
Cdd:cd03256 232 L 232
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
349-559 |
8.43e-28 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 111.66 E-value: 8.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 349 VIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDmtLSTLMSKISAVFQKVYLF-NDTIENN 427
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 428 ILFG--NPGATKEEIIRAAKQacchdfiMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPen 505
Cdd:cd03299 92 IAYGlkKRKVDKKEIERKVLE-------IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV-- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 506 eQLIQTAINELSK-----GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:cd03299 163 -RTKEKLREELKKirkefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
350-499 |
8.67e-28 |
|
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: 108.89 E-value: 8.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 350 IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFND-TIENNI 428
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613101153 429 LFgnpGATKEEIIRAAKQACCHDFI--MSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATS 499
Cdd:pfam00005 81 RL---GLLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
335-546 |
5.01e-27 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 108.77 E-value: 5.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTL--CHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISA 412
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKVYLF-NDTIENNILFGnP----GATKEEIIRAAKQAC----CHDFIMSLPegyqtmlnekgSNLSGGEKQRISIAR 483
Cdd:cd03262 81 VFQQFNLFpHLTVLENITLA-PikvkGMSKAEAEERALELLekvgLADKADAYP-----------AQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 484 AILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETIKN-ADQIIVLNEGEI 546
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
334-571 |
9.43e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 110.10 E-value: 9.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 334 NIAFQNVNFSYDDK-----QVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHL----LLRFYDIDDGIIRIDGVDIKDMT-L 403
Cdd:PRK13645 6 DIILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtnglIISETGQTIVGDYAIPANLKKIKeV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 404 STLMSKISAVFQ--KVYLFNDTIENNILFG--NPGATKEEIIRAAKQACChdfIMSLPEGYqtmLNEKGSNLSGGEKQRI 479
Cdd:PRK13645 86 KRLRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYKKVPELLK---LVQLPEDY---VKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 480 SIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETI-KNADQIIVLNEGEIIQKG------ 550
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfeif 239
|
250 260
....*....|....*....|....*.
gi 613101153 551 SHDELIRK-----PGMYQDFIRIKSK 571
Cdd:PRK13645 240 SNQELLTKieidpPKLYQLMYKLKNK 265
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
328-557 |
1.42e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.75 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 328 LTIKNENIAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDI--KDMTLST 405
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 406 LMSKISAVFQ--KVYLFNDTIENNILFG--NPGATKEEIIRAAKQACChdfIMSLPegYQTMLNEKGSNLSGGEKQRISI 481
Cdd:PRK13637 81 IRKKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 482 ARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGK--TVITIAHKLETI-KNADQIIVLNEGEIIQKGSHDELIR 557
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
335-559 |
1.57e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.34 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYD-----DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLC-HL--LLRfydiddgiIRIDGVDIKDMT---- 402
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLqHLngLLQ--------PTSGTVTIGERVitag 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 403 -----LSTLMSKISAVFQ--KVYLFNDTIENNILFG--NPGATKEEIIRAAKQACchdFIMSLPEGYqtmLNEKGSNLSG 473
Cdd:PRK13634 75 kknkkLKPLRKKVGIVFQfpEHQLFEETVEKDICFGpmNFGVSEEDAKQKAREMI---ELVGLPEEL---LARSPFELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 474 GEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL--SKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKG 550
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQG 228
|
....*....
gi 613101153 551 SHDELIRKP 559
Cdd:PRK13634 229 TPREIFADP 237
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
339-547 |
3.04e-26 |
|
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: 106.19 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 339 NVNFSYDDKQ-VIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRidgVDIKDMTLSTLMSKISAVFQKV 417
Cdd:cd03226 4 NISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL---LNGKPIKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 418 --YLFNDTIENNILFGNPGATKE-EIIRAA-KQACCHDFIMSLPEgyqtmlnekgsNLSGGEKQRISIARAILKDAPIII 493
Cdd:cd03226 81 dyQLFTDSVREELLLGLKELDAGnEQAETVlKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 494 LDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETIKN-ADQIIVLNEGEII 547
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
350-567 |
3.27e-26 |
|
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: 108.11 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 350 IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMS----KISAVFQKVYLF-NDTI 424
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 425 ENNILFG--NPGATKEEIIRAAKQAcchdfiMSLPeGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSID 502
Cdd:cd03294 120 LENVAFGleVQGVPRAEREERAAEA------LELV-GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613101153 503 PeneqLI----QTAINELSK--GKTVITIAHKL-ETIKNADQIIVLNEGEIIQKGSHDELIRKPGmyQDFIR 567
Cdd:cd03294 193 P----LIrremQDELLRLQAelQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTNPA--NDYVR 258
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
350-544 |
4.63e-26 |
|
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: 106.26 E-value: 4.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 350 IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGII--RIDGVDIKDMTLSTLMSKISAVF--QKVYLFNDTIE 425
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwSNKNESEPSFEATRSRNRYSVAYaaQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 426 NNILFGNPgaTKEEIIRAAKQACC-HDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPE 504
Cdd:cd03290 97 ENITFGSP--FNKQRYKAVTDACSlQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 613101153 505 -NEQLIQTAINELSKG--KTVITIAHKLETIKNADQIIVLNEG 544
Cdd:cd03290 175 lSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
335-559 |
5.43e-26 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 106.55 E-value: 5.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiDDGIIRIDGVDIKDMT-LSTLMSKISAV 413
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF---ETPTSGEILLDGKDITnLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 414 FQKVYLFND-TIENNILFG--NPGATKEEIIRAAKQACchdFIMSLpEGYQtmlNEKGSNLSGGEKQRISIARAILKDAP 490
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlrLKKLPKAEIKERVAEAL---DLVQL-EGYA---NRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613101153 491 IIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAH-KLETIKNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
115-566 |
1.03e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 112.76 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 115 SNELTTIVTTDLTFLENFAMKMVDVvvngYILIIVLILSLLVVSWQVSLLACIGVLLSFFAI---QLLERKSRQNAPAYH 191
Cdd:PLN03232 397 SGKVTNMITTDANALQQIAEQLHGL----WSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIplqTLIVRKMRKLTKEGL 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 192 NVQNQLVEKVLEVIRGIQVIKSFAKENtSLKSFNQSV-NESKRINTKIEMQYiPFNLLHLLSLKVVsimIVLVACLLYMN 270
Cdd:PLN03232 473 QWTDKRVGIINEILASMDTVKCYAWEK-SFESRIQGIrNEELSWFRKAQLLS-AFNSFILNSIPVV---VTLVSFGVFVL 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 271 HSIDL-PTLIMISIFSFVIFDSVENI--NSAAHVLEMiDMTIDDIEKIKNAPE--LDENgKNLTIKNENIAFQNVNFSYD 345
Cdd:PLN03232 548 LGGDLtPARAFTSLSLFAVLRSPLNMlpNLLSQVVNA-NVSLQRIEELLLSEEriLAQN-PPLQPGAPAISIKNGYFSWD 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 346 ---DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLrfydIDDGIIRIDGVDIKdmtlstlmSKISAVFQKVYLFND 422
Cdd:PLN03232 626 sktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML----GELSHAETSSVVIR--------GSVAYVPQVSWIFNA 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 423 TIENNILFGNPGATKEEIIRAAKQACCHDFIMsLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSID 502
Cdd:PLN03232 694 TVRENILFGSDFESERYWRAIDVTALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 503 PE-NEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPGMYQDFI 566
Cdd:PLN03232 773 AHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-559 |
1.06e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGV-----DIKDMTLSTLMSK 409
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVyldgqDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 410 ISAVFQkvylFNDTIENNILFGNPG---------ATKEEIIRAAKQACCHdfiMSLPEGYQTMLNEKGSNLSGGEKQRIS 480
Cdd:PRK14247 84 VQMVFQ----IPNPIPNLSIFENVAlglklnrlvKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 481 IARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAH-KLETIKNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
335-559 |
1.28e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 108.24 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL----------LRFydiddgiiridgvDIKDMTls 404
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagledptsgeILI-------------GGRDVT-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 405 TLMSK---ISAVFQKVYLF-NDTIENNILFG--NPGATKEEIIR----AAKqacchdfIMSLpEGYqtmLNEKGSNLSGG 474
Cdd:COG3839 69 DLPPKdrnIAMVFQSYALYpHMTVYENIAFPlkLRKVPKAEIDRrvreAAE-------LLGL-EDL---LDRKPKQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 475 EKQRISIARAILKDAPIIILDEATSSIDPeneQLIQTAINELSK-----GKTVITIAHKLE---TIknADQIIVLNEGEI 546
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDA---KLRVEMRAEIKRlhrrlGTTTIYVTHDQVeamTL--ADRIAVMNDGRI 212
|
250
....*....|...
gi 613101153 547 IQKGSHDELIRKP 559
Cdd:COG3839 213 QQVGTPEELYDRP 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
335-547 |
2.13e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 104.36 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY-DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRfydidDGIIRIDGVDIKDMTLSTLMS----- 408
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG-----EERPTSGQVLVNGQDLSRLKRreipy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 409 ---KISAVFQKVYLFND-TIENNILFgnP----GATKEEIIRAAKQACCH----DFIMSLPEgyqtmlnekgsNLSGGEK 476
Cdd:COG2884 77 lrrRIGVVFQDFRLLPDrTVYENVAL--PlrvtGKSRKEIRRRVREVLDLvglsDKAKALPH-----------ELSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 477 QRISIARAILKDAPIIILDEATSSIDPEN-EQLIQ--TAINELskGKTVItIA-HKLETIKNADQ-IIVLNEGEII 547
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETsWEIMEllEEINRR--GTTVL-IAtHDLELVDRMPKrVLELEDGRLV 216
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
326-563 |
2.42e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.86 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 326 KNLTIKNENIAFQNVNFSYDDKQ-----VIKNVNFEIPTQTSTAIIGPSGSGKSTLC-HL--LLR----------FYDID 387
Cdd:PRK13631 13 PNPLSDDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVtHFngLIKskygtiqvgdIYIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 388 DGIIRIDGVD-----IKDmtLSTLMSKISAVFQ--KVYLFNDTIENNILFGnPGATKEEIIRAAKQACCHDFIMSLPEGY 460
Cdd:PRK13631 93 KKNNHELITNpyskkIKN--FKELRRRVSMVFQfpEYQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDDSY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 461 qtmLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETI-KNADQI 538
Cdd:PRK13631 170 ---LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVlEVADEV 246
|
250 260
....*....|....*....|....*
gi 613101153 539 IVLNEGEIIQKGSHDELIRKPGMYQ 563
Cdd:PRK13631 247 IVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
337-559 |
5.01e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 110.64 E-value: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 337 FQNVNFSYDD--KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLchlLLRFYDIDDGIIRIDGV---DIKDMTLSTLMSKIS 411
Cdd:PTZ00243 1311 FEGVQMRYREglPLVLRGVSFRIAPREKVGIVGRTGSGKSTL---LLTFMRMVEVCGGEIRVngrEIGAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKVYLFNDTIENNIlfgNP--GATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILK-D 488
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkG 1464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 489 APIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PTZ00243 1465 SGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
338-530 |
1.47e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 103.32 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLchllLRFYDIDDGIIRIDGVDIK-----------DMTLSTL 406
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTI----LRCFNRLNDLIPGFRVEGKvtfhgknlyapDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 407 MSKISAVFQKVYLFNDTIENNILFGN-----PGATKEEIIRAAKQACCHDFImslpegyQTMLNEKGSNLSGGEKQRISI 481
Cdd:PRK14243 90 RRRIGMVFQKPNPFPKSIYDNIAYGAringyKGDMDELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 613101153 482 ARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLE 530
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
363-550 |
1.72e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 101.42 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 363 TAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTlmSKISAVFQKVYLFND-TIENNILFG-NPG-----A 435
Cdd:cd03298 27 TAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNVGLGlSPGlkltaE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 436 TKEEIIRAAKQACCHDFIMSLPEgyqtmlnekgsNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINE 515
Cdd:cd03298 105 DRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 613101153 516 L--SKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKG 550
Cdd:cd03298 174 LhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
335-560 |
1.92e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 108.67 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY--DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISA 412
Cdd:PLN03130 1238 IKFEDVVLRYrpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKVYLFNDTIENNILFGNPgATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPII 492
Cdd:PLN03130 1318 IPQAPVLFSGTVRFNLDPFNE-HNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKIL 1396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 493 ILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPG 560
Cdd:PLN03130 1397 VLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
335-559 |
2.24e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.09 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISA-- 412
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKVYLFND-TIENNILFGnP----GATKEEiirAAKQAccHDFIMSLpeGYQTMLNEKGSNLSGGEKQRISIARAILK 487
Cdd:PRK09493 82 VFQQFYLFPHlTALENVMFG-PlrvrGASKEE---AEKQA--RELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613101153 488 DAPIIILDEATSSIDPENEQLIQTAINELS-KGKTVITIAHKLE-TIKNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
328-559 |
2.64e-24 |
|
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: 102.19 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 328 LTIKNENIAFQNvnfSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLM 407
Cdd:COG1124 2 LEVRNLSVSYGQ---GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 408 SKISAVFQKVYL-FN------DTIENNILFGNPGATKEEIIRAAKQacchdfiMSLPEGYqtmLNEKGSNLSGGEKQRIS 480
Cdd:COG1124 79 RRVQMVFQDPYAsLHprhtvdRILAEPLRIHGLPDREERIAELLEQ-------VGLPPSF---LDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 481 IARAILKDAPIIILDEATSSIDPeneqLIQTAI-NELSK-----GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHD 553
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDV----SVQAEIlNLLKDlreerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVA 224
|
....*.
gi 613101153 554 ELIRKP 559
Cdd:COG1124 225 DLLAGP 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
331-564 |
3.87e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.14 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 331 KNENIAFQNVNFSY--DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMS 408
Cdd:PRK13648 4 KNSIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 409 KISAVFQKV--YLFNDTIENNILFG--NPGATKEEIIRAAKQAcchdfimsLPEgyQTMLNEKGS---NLSGGEKQRISI 481
Cdd:PRK13648 84 HIGIVFQNPdnQFVGSIVKYDVAFGleNHAVPYDEMHRRVSEA--------LKQ--VDMLERADYepnALSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 482 ARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGK--TVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
....*
gi 613101153 560 GMYQD 564
Cdd:PRK13648 234 EELTR 238
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
256-544 |
1.27e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.89 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 256 VSIMI-VLVACLLYMNHSIDLPTLIMISI--------FSFVIfDSVENINSAAHVLEMIDMTIDDIEKIKNAPEldENGK 326
Cdd:COG4178 278 LAVIFpILVAAPRYFAGEITLGGLMQAASafgqvqgaLSWFV-DNYQSLAEWRATVDRLAGFEEALEAADALPE--AASR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 327 NLTIKNENIAFQNVN-FSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLchllLRfydiddgiiridgvdikdmTLS- 404
Cdd:COG4178 355 IETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL----LR-------------------AIAg 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 405 ---------TLMSKISAVF--QKVYLFNDTIENNILFGN-PGATKEEIIRAAKQACChdfimsLPEgYQTMLNEK---GS 469
Cdd:COG4178 412 lwpygsgriARPAGARVLFlpQRPYLPLGTLREALLYPAtAEAFSDAELREALEAVG------LGH-LAERLDEEadwDQ 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 470 NLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEG 544
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
335-550 |
3.72e-23 |
|
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: 97.65 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTsTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTlSTLMSKISAVF 414
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 Q--------KVYLFNDTIEnnILFG-NPGATKEEIIRAAKQACCHDFimslpegyqtmLNEKGSNLSGGEKQRISIARAI 485
Cdd:cd03264 79 QefgvypnfTVREFLDYIA--WLKGiPSKEVKARVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 486 LKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKG 550
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
335-560 |
4.55e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.54 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDK----QVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL----------LRfydiddgiiridgVDIKD 400
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInllerptsgsVL-------------VDGVD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 401 MT------LSTLMSKISAVFQKVYLFND-TIENNILFgnP----GATKEEIirAAKqacchdfIMSLPE--GyqtmLNEK 467
Cdd:COG1135 69 LTalsereLRAARRKIGMIFQHFNLLSSrTVAENVAL--PleiaGVPKAEI--RKR-------VAELLElvG----LSDK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 468 G----SNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQ----LIQTaIN-ELskGKTVITIAHKLETIKN-ADQ 537
Cdd:COG1135 134 AdaypSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRsildLLKD-INrEL--GLTIVLITHEMDVVRRiCDR 210
|
250 260
....*....|....*....|...
gi 613101153 538 IIVLNEGEIIQKGSHDELIRKPG 560
Cdd:COG1135 211 VAVLENGRIVEQGPVLDVFANPQ 233
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
312-555 |
4.64e-23 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 99.16 E-value: 4.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 312 IEKIKNapeldENGKNLTIKNENIAFQNvNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLrfydiddGII 391
Cdd:cd03291 21 LEKAKQ-----ENNDRKHSSDDNNLFFS-NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLIL-------GEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 392 RIDGVDIKDMtlstlmSKISAVFQKVYLFNDTIENNILFGNpgATKEEIIRAAKQAC-CHDFIMSLPEGYQTMLNEKGSN 470
Cdd:cd03291 88 EPSEGKIKHS------GRISFSSQFSWIMPGTIKENIIFGV--SYDEYRYKSVVKACqLEEDITKFPEKDNTVLGEGGIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 471 LSGGEKQRISIARAILKDAPIIILDEATSSIDPENE-QLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQK 549
Cdd:cd03291 160 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEkEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFY 239
|
....*.
gi 613101153 550 GSHDEL 555
Cdd:cd03291 240 GTFSEL 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
335-558 |
4.70e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.47 E-value: 4.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYD-----DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCH----LLLRFYDIDDGIIRIDGVDIKDMTLST 405
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQninaLLKPTTGTVTVDDITITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 406 LMSKISAVFQ--KVYLFNDTIENNILFG--NPGATKEEIIRAAkqaccHDFIMSLpeGY-QTMLNEKGSNLSGGEKQRIS 480
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEVKNYA-----HRLLMDL--GFsRDVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 481 IARAILKDAPIIILDEATSSIDPENEQLIQTAINELS--KGKTVITIAHKL-ETIKNADQIIVLNEGEIIQKGSHDELIR 557
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMnEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
.
gi 613101153 558 K 558
Cdd:PRK13646 236 D 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
335-558 |
8.69e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.27 E-value: 8.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY-DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTlchLLLRFYDIDDGIIRIDGVDIKDMTLST---LMSKI 410
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKST---LLLHLNGIYLPQRGRVKVMGREVNAENekwVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 411 SAVFQKV--YLFNDTIENNILFG--NPGATKEEIIRAAKQAC----CHDFIMSLPEgyqtmlnekgsNLSGGEKQRISIA 482
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERRVEEALkavrMWDFRDKPPY-----------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 483 RAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLE-TIKNADQIIVLNEGEIIQKGSHDELIRK 558
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
338-550 |
1.12e-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: 96.17 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYdidDGIIRIDGVDIKDMT-LSTLMSKISAVFQK 416
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE---EPTSGRIYIGGRDVTdLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 VYLF-NDTIENNILFG--NPGATKEEIIRAAKQACchdFIMSLPEgyqtMLNEKGSNLSGGEKQRISIARAILKDAPIII 493
Cdd:cd03301 81 YALYpHMTVYDNIAFGlkLRKVPKDEIDERVREVA---ELLQIEH----LLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 494 LDEATSSIDPENEQLIQTAINELSK--GKTVITIAH-KLETIKNADQIIVLNEGEIIQKG 550
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
335-555 |
1.57e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.88 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQ---VIKNVNFEIPTQTSTAIIGPSGSGKSTLCHL---LLrfydidDGIIRIDGVDIKDMTLST--- 405
Cdd:PRK13650 5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLidgLL------EAESGQIIIDGDLLTEENvwd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 406 LMSKISAVFQKV--YLFNDTIENNILFG--NPGATKEEIIRAAKQAcchdfiMSLPeGYQTMLNEKGSNLSGGEKQRISI 481
Cdd:PRK13650 79 IRHKIGMVFQNPdnQFVGATVEDDVAFGleNKGIPHEEMKERVNEA------LELV-GMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 482 ARAILKDAPIIILDEATSSIDPENEQ-LIQT--AINElSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDEL 555
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLeLIKTikGIRD-DYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
335-550 |
2.24e-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: 94.93 E-value: 2.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYD------DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLchllLRF---YDIDDGIIRIDGVDIKDMTLST 405
Cdd:cd03213 4 LSFRNLTVTVKsspsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTL----LNAlagRRTGLGVSGEVLINGRPLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 406 LMSKISAVFQKVYLF-NDTIENNILFgnpgatkeeiiraakQACChdfimslpegyqtmlnekgSNLSGGEKQRISIARA 484
Cdd:cd03213 80 FRKIIGYVPQDDILHpTLTVRETLMF---------------AAKL-------------------RGLSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 485 ILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKL--ETIKNADQIIVLNEGEIIQKG 550
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
335-559 |
3.34e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.82 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYD-----DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCH----LLLRFYDIDDGIIRIDGVDIKDMTLST 405
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQhfnaLLKPSSGTITIAGYHITPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 406 LMSKISAVFQ--KVYLFNDTIENNILFG--NPGATKEEIIRAAKQACCHdfiMSLPEgyqTMLNEKGSNLSGGEKQRISI 481
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDEAKEKALKWLKK---VGLSE---DLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 482 ARAILKDAPIIILDEATSSIDPEN-EQLIQTAINELSKGKTVITIAHKLETI-KNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
335-559 |
1.09e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 96.71 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL----------LRFydiddgiiridgvDIKDMTlS 404
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagfetpdsgrILL-------------DGRDVT-G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 405 TLMSK--ISAVFQKVYLF-NDTIENNILFG--NPGATKEEIIRAAKQACchdFIMSLPEgyqtMLNEKGSNLSGGEKQRI 479
Cdd:COG3842 72 LPPEKrnVGMVFQDYALFpHLTVAENVAFGlrMRGVPKAEIRARVAELL---ELVGLEG----LADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 480 SIARAILKDAPIIILDEATSSIDPEN-EQLiQTAINELSK--GKTVITIAHKLE---TIknADQIIVLNEGEIIQKGSHD 553
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLrEEM-REELRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPE 221
|
....*.
gi 613101153 554 ELIRKP 559
Cdd:COG3842 222 EIYERP 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
334-553 |
1.71e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.92 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 334 NIAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHL--LLRFYDIDDGIIRIDGVD----IKDMTLSTLM 407
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVlnLLETPDSGQLNIAGHQFDfsqkPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 408 SKISAVFQKVYLF-NDTIENNiLFGNP----GATKEEIIRAAKQacchdfIMSlpegyQTMLNEKGS----NLSGGEKQR 478
Cdd:COG4161 82 QKVGMVFQQYNLWpHLTVMEN-LIEAPckvlGLSKEQAREKAMK------LLA-----RLRLTDKADrfplHLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 479 ISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETI-KNADQIIVLNEGEIIQKGSHD 553
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGDAS 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
331-559 |
2.32e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 93.75 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 331 KNENIAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDI-------KDMTL 403
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLfgrniysPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 404 STLMSKISAVFQKVYLF-NDTIENNILFG----NPGATKEEIIR----AAKQAcchdfimSLPEGYQTMLNEKGSNLSGG 474
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFpHLTIYDNVAIGvklnGLVKSKKELDErvewALKKA-------ALWDEVKDRLNDYPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 475 EKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHK-LETIKNADQIIVLNEGEIIQKGSHD 553
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTR 233
|
....*.
gi 613101153 554 ELIRKP 559
Cdd:PRK14267 234 KVFENP 239
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
345-559 |
3.41e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.19 E-value: 3.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 345 DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRI------DGVDIKDMTLSTLMSKISAVFQKVY 418
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkvlyFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 419 LF-NDTIENNILF--GNPGATKEEIIRAAKQACCHDfiMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILD 495
Cdd:PRK14246 101 PFpHLSIYDNIAYplKSHGIKEKREIKKIVEECLRK--VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 496 EATSSIDPENEQLIQTAINELSKGKTVITIAHKLETI-KNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
342-559 |
3.44e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 98.31 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 342 FSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYdiddgiiridgvDIKDMTLSTLMSkISAVFQKVYLFN 421
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF------------EISEGRVWAERS-IAYVPQQAWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 422 DTIENNILFGNPgatkEEIIRAAKQA-CCH---DfIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEA 497
Cdd:PTZ00243 735 ATVRGNILFFDE----EDAARLADAVrVSQleaD-LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613101153 498 TSSIDPE-NEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PTZ00243 810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
349-559 |
3.99e-21 |
|
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: 92.50 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 349 VIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTlstlMSKISA-----VFQKVYLFND- 422
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP----PHEIARlgigrTFQIPRLFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 423 TIENNILFGNPGATKEEII---RAAKQACCHDFIMSLPE--GYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEA 497
Cdd:cd03219 91 TVLENVMVAAQARTGSGLLlarARREEREARERAEELLErvGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 498 TSSIDP-ENEQLIQTaINELS-KGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:cd03219 171 AAGLNPeETEELAEL-IRELReRGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
335-547 |
4.70e-21 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 90.18 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLchlllrfydiddgiiridgvdikdmtlstlMSKISAVF 414
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTL------------------------------MKILSGLY 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 Q----KVYLFNDTIEnnilFGNPgatkeeiiRAAKQAcchdfimslpeG----YQtmlnekgsnLSGGEKQRISIARAIL 486
Cdd:cd03216 51 KpdsgEILVDGKEVS----FASP--------RDARRA-----------GiamvYQ---------LSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613101153 487 KDAPIIILDEATSSIDP-ENEQLIQTaINEL-SKGKTVITIAHKLETIKN-ADQIIVLNEGEII 547
Cdd:cd03216 99 RNARLLILDEPTAALTPaEVERLFKV-IRRLrAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
338-564 |
5.46e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.77 E-value: 5.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQkV 417
Cdd:PRK11231 6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ-H 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 418 YLFNDTIE-----------NNILFGNPGATKEEIIRAAKQACchdfimslpeGYQTMLNEKGSNLSGGEKQRISIARAIL 486
Cdd:PRK11231 85 HLTPEGITvrelvaygrspWLSLWGRLSAEDNARVNQAMEQT----------RINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 487 KDAPIIILDEATSSIDPENEQLIQTAINELS-KGKTVITIAHKL-ETIKNADQIIVLNEGEIIQKGSHDELIrKPGMYQD 564
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVM-TPGLLRT 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
332-555 |
5.75e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.23 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 332 NENIAFQNVNFSYD---DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMS 408
Cdd:PRK13642 2 NKILEVENLVFKYEkesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 409 KISAVFQKV--YLFNDTIENNILFG--NPGATKEEIIRAAKQACchdfimsLPEGYQTMLNEKGSNLSGGEKQRISIARA 484
Cdd:PRK13642 82 KIGMVFQNPdnQFVGATVEDDVAFGmeNQGIPREEMIKRVDEAL-------LAVNMLDFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613101153 485 ILKDAPIIILDEATSSIDPENEQLIQTAINELSKGK--TVITIAHKLETIKNADQIIVLNEGEIIQKGSHDEL 555
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
340-566 |
6.54e-21 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 93.00 E-value: 6.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 340 VNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFyDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYL 419
Cdd:cd03289 10 AKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 420 FNDTIENNiLFGNPGATKEEIIRAAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATS 499
Cdd:cd03289 89 FSGTFRKN-LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 500 SIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPGMYQDFI 566
Cdd:cd03289 168 HLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
335-542 |
8.57e-21 |
|
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: 90.99 E-value: 8.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQ----VIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiddGIIRIDGVDIKDMTLSTLMSKI 410
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGL-----ERPTSGEVLVDGEPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 411 SAVFQKVYLFN-DTIENNILFG--NPGATKEEIIRAAKQacchdfimslpegyqtMLNEKG---------SNLSGGEKQR 478
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGleLQGVPKAEARERAEE----------------LLELVGlsgfenaypHQLSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 479 ISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKL-ETIKNADQIIVLN 542
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIdEAVFLADRVVVLS 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
313-555 |
9.47e-21 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 96.90 E-value: 9.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 313 EKIKnapeldENGKNLTIKNENIAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLrfydiddGIIR 392
Cdd:TIGR01271 411 EKIK------QNNKARKQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM-------GELE 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 393 IDGVDIKDMtlstlmSKISAVFQKVYLFNDTIENNILFGNpgATKEEIIRAAKQAC-CHDFIMSLPEGYQTMLNEKGSNL 471
Cdd:TIGR01271 478 PSEGKIKHS------GRISFSPQTSWIMPGTIKDNIIFGL--SYDEYRYTSVIKACqLEEDIALFPEKDKTVLGEGGITL 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 472 SGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLI-QTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEIIQKG 550
Cdd:TIGR01271 550 SGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYG 629
|
....*
gi 613101153 551 SHDEL 555
Cdd:TIGR01271 630 TFSEL 634
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
352-550 |
1.55e-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: 90.05 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 352 NVNFEIPTQTsTAIIGPSGSGKSTLCHL---LLRFYDIDDGIIRIDGVDI-KDMTLSTLMSKISAVFQKVYLF-NDTIEN 426
Cdd:cd03297 16 KIDFDLNEEV-TGIFGASGAGKSTLLRCiagLEKPDGGTIVLNGTVLFDSrKKINLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 427 NILFGNPG-ATKEEIIRAAKqacchdfiMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPEN 505
Cdd:cd03297 95 NLAFGLKRkRNREDRISVDE--------LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 613101153 506 EQLIQTAINELSK--GKTVITIAHKLETI-KNADQIIVLNEGEIIQKG 550
Cdd:cd03297 167 RLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
335-546 |
1.76e-20 |
|
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: 90.16 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY-DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDI---KDMTLSTLMSKI 410
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 411 SAVFQKVYLFND-TIENNILF-----GNPGATKEEIIRAA-KQACCHDFIMSLPEGyqtmlnekgsnLSGGEKQRISIAR 483
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFalevtGVPPREIRKRVPAAlELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 484 AILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETIKN-ADQIIVLNEGEI 546
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
335-550 |
3.09e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 91.69 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDK-----QVIKNVNFEIPTQTSTAIIGPSGSGKSTLC-HL-------------LLRFYDIDDGIIRIDG 395
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIeHLnalllpdtgtiewIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 396 VDIKDMTLSTLMSKIS----------AVFQ--KVYLFNDTIENNILFG--NPGATKEEiirAAKQACCHDFIMSLPEGYq 461
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKkikeirrrvgVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEE---AKKRAAKYIELVGLDESY- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 462 tmLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETI-KNADQII 539
Cdd:PRK13651 159 --LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVlEWTKRTI 236
|
250
....*....|.
gi 613101153 540 VLNEGEIIQKG 550
Cdd:PRK13651 237 FFKDGKIIKDG 247
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
331-558 |
3.25e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.92 E-value: 3.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 331 KNENIAFQNVNFSYDD------KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDM-TL 403
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 404 STLMSKISAVFQKV--YLFNDTIENNILFG--NPGATKEEIiRAAKQACCHDFIMSLPEGYQTMLnekgsnLSGGEKQRI 479
Cdd:PRK13633 81 WDIRNKAGMVFQNPdnQIVATIVEEDVAFGpeNLGIPPEEI-RERVDESLKKVGMYEYRRHAPHL------LSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 480 SIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIR 557
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
.
gi 613101153 558 K 558
Cdd:PRK13633 234 E 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
335-556 |
3.69e-20 |
|
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: 90.14 E-value: 3.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRI------DGVDIKDmtlstLMS 408
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrGGEDVWE-----LRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 409 KI---SAVFQKVYLFNDTIENNIL---FGNPG----ATKEEIIRAAKqacchdfimslpegyqtMLNEKG---------S 469
Cdd:COG1119 79 RIglvSPALQLRFPRDETVLDVVLsgfFDSIGlyrePTDEQRERARE-----------------LLELLGlahladrpfG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 470 NLSGGEKQRISIARAILKDAPIIILDEATSSIDPEN-EQLIQTaINELSK--GKTVITIAHKLETIKNA-DQIIVLNEGE 545
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArELLLAL-LDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
250
....*....|.
gi 613101153 546 IIQKGSHDELI 556
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
348-558 |
4.19e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.54 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 348 QVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL----------LRFydiddgiiridgvDIKDMTLST----LMSKISAV 413
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILsgvyqpdsgeILL-------------DGEPVRFRSprdaQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 414 FQKVYLFND-TIENNILFGNPGATK-----EEIIRAAKQACcHDFIMSLPegyqtmLNEKGSNLSGGEKQRISIARAILK 487
Cdd:COG1129 85 HQELNLVPNlSVAENIFLGREPRRGglidwRAMRRRARELL-ARLGLDID------PDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 488 DAPIIILDEATSSIDP-ENEQLIQTaINEL-SKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKG-----SHDELIRK 558
Cdd:COG1129 158 DARVLILDEPTASLTErEVERLFRI-IRRLkAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVRL 235
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
335-559 |
5.67e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 91.36 E-value: 5.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL----------LRFydiddgiiridgvDIKDMT-- 402
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagletpdsgrIVL-------------NGRDLFtn 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 403 LSTLMSKISAVFQKVYLF-NDTIENNILFGnpgATKEEIIRAAKQACCHDFI--MSLPEgyqtMLNEKGSNLSGGEKQRI 479
Cdd:COG1118 70 LPPRERRVGFVFQHYALFpHMTVAENIAFG---LRVRPPSKAEIRARVEELLelVQLEG----LADRYPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 480 SIARAILKDAPIIILDEATSSID----PENEQLIQTAINELskGKTVITIAHKLE---TIknADQIIVLNEGEIIQKGSH 552
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL--GGTTVFVTHDQEealEL--ADRVVVMNQGRIEQVGTP 218
|
....*..
gi 613101153 553 DELIRKP 559
Cdd:COG1118 219 DEVYDRP 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
335-560 |
6.72e-20 |
|
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: 88.94 E-value: 6.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTlmSKISAVF 414
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKVYLFND-TIENNILFG---NPGATKEEiiRAAKQACCHDFI--MSLpEGYQtmlNEKGSNLSGGEKQRISIARAILKD 488
Cdd:cd03296 81 QHYALFRHmTVFDNVAFGlrvKPRSERPP--EAEIRAKVHELLklVQL-DWLA---DRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 489 APIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAH-KLETIKNADQIIVLNEGEIIQKGSHDELIRKPG 560
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
335-553 |
7.36e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.92 E-value: 7.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHL--LLRFYDIDDGIIRIDGVD----IKDMTLSTLMS 408
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVlnLLEMPRSGTLNIAGNHFDfsktPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 409 KISAVFQKVYLF-NDTIENNiLFGNP----GATKEEiirAAKQAcchdfiMSLPEGYQtmLNEKGS----NLSGGEKQRI 479
Cdd:PRK11124 83 NVGMVFQQYNLWpHLTVQQN-LIEAPcrvlGLSKDQ---ALARA------EKLLERLR--LKPYADrfplHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 480 SIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETI-KNADQIIVLNEGEIIQKGSHD 553
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDAS 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
339-559 |
8.26e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 89.75 E-value: 8.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 339 NVNFSY-DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLchlLLRFYDIDDGIIRIDGVDIKDM-----TLSTLMSKISA 412
Cdd:PRK13639 6 DLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTL---FLHFNGILKPTSGEVLIKGEPIkydkkSLLEVRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKV--YLFNDTIENNILFG--NPGATKEEIIRAAKQACcHDFIMslpEGYQtmlNEKGSNLSGGEKQRISIARAILKD 488
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEAL-KAVGM---EGFE---NKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613101153 489 APIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETI-KNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
335-558 |
1.13e-19 |
|
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: 92.56 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL--LRFYD--------------------------- 385
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEptsgriiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 386 ------IDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLF--NDTIENNIL-----FGNPGatKEEIIRAAkqacchDF 452
Cdd:TIGR03269 81 pcpvcgGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLealeeIGYEG--KEAVGRAV------DL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 453 IMSLPEGYQTMlnEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLE 530
Cdd:TIGR03269 153 IEMVQLSHRIT--HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*....
gi 613101153 531 TIKN-ADQIIVLNEGEIIQKGSHDELIRK 558
Cdd:TIGR03269 231 VIEDlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
364-556 |
1.31e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.10 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 364 AIIGPSGSGKSTLCHLLLRFydiDDGIIRIDGVDIKDMTlSTLMSK--ISAVFQKVYLFND-TIENNILFG-NPG----- 434
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGF---LTPASGSLTLNGQDHT-TTPPSRrpVSMLFQENNLFSHlTVAQNIGLGlNPGlklna 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 435 ATKEEIIRAAKQACCHDFIMSLPegyqtmlnekgSNLSGGEKQRISIARAILKDAPIIILDEATSSIDP----ENEQLIQ 510
Cdd:PRK10771 105 AQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPalrqEMLTLVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 613101153 511 TAINElsKGKTVITIAHKLE-TIKNADQIIVLNEGEIIQKGSHDELI 556
Cdd:PRK10771 174 QVCQE--RQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
335-559 |
1.77e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 88.71 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYD-DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAV 413
Cdd:PRK13652 4 IETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 414 FQKV--YLFNDTIENNILFG--NPGATKEEIIRAAKQAcchdfIMSLpeGYQTMLNEKGSNLSGGEKQRISIARAILKDA 489
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFGpiNLGLDEETVAHRVSSA-----LHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613101153 490 PIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-548 |
1.77e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.56 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDI-------KDMTLSTLM 407
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFfnqniyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 408 SKISAVFQKVYLFNDTIENNILFG------NPGATKEEIIRAAKQACchdfimSLPEGYQTMLNEKGSNLSGGEKQRISI 481
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKDA------DLWDEIKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613101153 482 ARAILKDAPIIILDEATSSIDP----ENEQLIQTAinELSKGKTVITIAHKLETIKNADQIIVL---NEGEIIQ 548
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSL--RLRSELTMVIVSHNLHQVSRLSDFTAFfkgNENRIGQ 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
335-541 |
2.85e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 86.69 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVF 414
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKVYLFNDTIENNILFgnPGATKEEIIRAAKQAcchDFIM--SLPEgyqTMLNEKGSNLSGGEKQRISIARAILKDAPII 492
Cdd:PRK10247 88 QTPTLFGDTVYDNLIF--PWQIRNQQPDPAIFL---DDLErfALPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 613101153 493 ILDEATSSIDPENEQLIQTAINEL--SKGKTVITIAHKLETIKNADQIIVL 541
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITL 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
335-551 |
3.11e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.09 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVN--FSYDDKQVI--KNVNFEIPTQTSTAIIGPSGSGKSTL--C-HLLLRfydiddGIIRIDGVDIKDMT----- 402
Cdd:PRK11153 2 IELKNISkvFPQGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLirCiNLLER------PTSGRVLVDGQDLTalsek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 403 -LSTLMSKISAVFQKVYLFND-TIENNILFgnP----GATKEEIIR-----------AAKqaccHDFimslpegYQtmln 465
Cdd:PRK11153 76 eLRKARRQIGMIFQHFNLLSSrTVFDNVAL--PlelaGTPKAEIKArvtellelvglSDK----ADR-------YP---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 466 ekgSNLSGGEKQRISIARAiLKDAPIIIL-DEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKN-ADQIIVL 541
Cdd:PRK11153 139 ---AQLSGGQKQRVAIARA-LASNPKVLLcDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVI 214
|
250
....*....|
gi 613101153 542 NEGEIIQKGS 551
Cdd:PRK11153 215 DAGRLVEQGT 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
335-574 |
3.13e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.88 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYD-----DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDI----KDMTLST 405
Cdd:PRK13649 3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 406 LMSKISAVFQ--KVYLFNDTIENNILFG--NPGATKEEIIRAAKQAcchdfiMSLPEGYQTMLNEKGSNLSGGEKQRISI 481
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAREK------LALVGISESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 482 ARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELirkp 559
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI---- 232
|
250
....*....|....*
gi 613101153 560 gmYQDFIRIKSKSAG 574
Cdd:PRK13649 233 --FQDVDFLEEKQLG 245
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
338-555 |
3.55e-19 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 86.81 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSK-ISAVFQK 416
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 VYLFND-TIENNILFG--NPGATKEEIIraakqacchDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIII 493
Cdd:TIGR03410 84 REIFPRlTVEENLLTGlaALPRRSRKIP---------DEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 494 LDEATSSIDPENEQLIQTAINEL--SKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDEL 555
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
335-561 |
4.29e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.74 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY-DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMT-LSTLMSKISA 412
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQ--KVYLFNDTIENNILFG--NPGATKEEIIRAAKQAcchdfimsLPE-GYQTMLNEKGSNLSGGEKQRISIARAILK 487
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRA--------LAEiGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 488 DAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPGM 561
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
297-566 |
6.92e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 91.13 E-value: 6.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 297 SAAHVLEMIDMTIDDiEKIKNAPELDENGKNLTIKNENIA----------FQNVNFSY--DDKQVIKNVNFEIPTQTSTA 364
Cdd:TIGR01271 1171 SVSRVFKFIDLPQEE-PRPSGGGGKYQLSTVLVIENPHAQkcwpsggqmdVQGLTAKYteAGRAVLQDLSFSVEGGQRVG 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 365 IIGPSGSGKSTLCHLLLRFyDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNIlfgNPGA--TKEEIIR 442
Cdd:TIGR01271 1250 LLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEqwSDEEIWK 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 443 AAKQACCHDFIMSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTV 522
Cdd:TIGR01271 1326 VAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTV 1405
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 613101153 523 ITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKPGMYQDFI 566
Cdd:TIGR01271 1406 ILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
335-559 |
7.14e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 88.47 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDmtLSTLMSKISAVF 414
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH--VPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKVYLF-NDTIENNILFG-----NPgatKEEIIRAAKQAcchdFIMSLPEGyqtMLNEKGSNLSGGEKQRISIARAILKD 488
Cdd:PRK09452 93 QSYALFpHMTVFENVAFGlrmqkTP---AAEITPRVMEA----LRMVQLEE---FAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613101153 489 APIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAH-KLETIKNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
331-559 |
1.44e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.47 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 331 KNENIAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiDDGIIRIDGVDIKDMTLSTLMSK- 409
Cdd:PRK11432 3 QKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL---EKPTEGQIFIDGEDVTHRSIQQRd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 410 ISAVFQKVYLF-NDTIENNILFG--NPGATKEEIIRAAKQACChdfIMSLpEGYQTMLNEKgsnLSGGEKQRISIARAIL 486
Cdd:PRK11432 80 ICMVFQSYALFpHMSLGENVGYGlkMLGVPKEERKQRVKEALE---LVDL-AGFEDRYVDQ---ISGGQQQRVALARALI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 487 KDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAH-KLETIKNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
344-559 |
1.90e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.21 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 344 YDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLST-------LMSKISAVFQK 416
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSprtdtvdLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 VYLFNDTIENNILFG--NPGATKEEIIRAA-----KQAcchdfimSLPEGYQTMLNEKGSNLSGGEKQRISIARAILKDA 489
Cdd:PRK14239 95 PNPFPMSIYENVVYGlrLKGIKDKQVLDEAvekslKGA-------SIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 490 PIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
334-559 |
2.64e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 86.68 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 334 NIAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL----------LRFYDiddgiiridgvdiKDMT- 402
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIaglehqtsghIRFHG-------------TDVSr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 403 LSTLMSKISAVFQKVYLFND-TIENNILFG--------NPGAtkeEIIRAAkqacchdfIMSLPEGYQT--MLNEKGSNL 471
Cdd:PRK10851 69 LHARDRKVGFVFQHYALFRHmTVFDNIAFGltvlprreRPNA---AAIKAK--------VTQLLEMVQLahLADRYPAQL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 472 SGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELS---KGKTVITIAHKLETIKNADQIIVLNEGEIIQ 548
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHeelKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQ 217
|
250
....*....|.
gi 613101153 549 KGSHDELIRKP 559
Cdd:PRK10851 218 AGTPDQVWREP 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
350-567 |
3.78e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 86.63 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 350 IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMS----KISAVFQKVYLF-NDTI 424
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 425 ENNILFGNPGA------TKEEIIRAAKQACCHDFIMSLPEgyqtmlnekgsNLSGGEKQRISIARAILKDAPIIILDEAT 498
Cdd:PRK10070 124 LDNTAFGMELAginaeeRREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 499 SSIDPeneqLIQTAI-NELSK-----GKTVITIAHKL-ETIKNADQIIVLNEGEIIQKGSHDELIRKPGmyQDFIR 567
Cdd:PRK10070 193 SALDP----LIRTEMqDELVKlqakhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA--NDYVR 262
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
335-541 |
3.82e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 84.37 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY----DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHL---LLRFYdiddgiirIDGVDIKDMTLSTLM 407
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLiagLEKPT--------SGEVLVDGKPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 408 SKISAVFQKVYLFN-DTIENNILFG--NPGATKEEIIRAAKQ-------AcchDFIMSLPegyqtmlnekgSNLSGGEKQ 477
Cdd:COG1116 80 PDRGVVFQEPALLPwLTVLDNVALGleLRGVPKAERRERAREllelvglA---GFEDAYP-----------HQLSGGMRQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 478 RISIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL--SKGKTVITIAHKL-ETIKNADQIIVL 541
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVdEAVFLADRVVVL 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
335-550 |
4.10e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 83.10 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRidgVDIKDMTLSTlMSKISAVF 414
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL---FDGKPLDIAA-RNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKVYLFNDT--IENNILFGN-PGATKEEIIRAAKqacchDFIMSLP-EGYQtmlNEKGSNLSGGEKQRISIARAILKDAP 490
Cdd:cd03269 77 EERGLYPKMkvIDQLVYLAQlKGLKKEEARRRID-----EWLERLElSEYA---NKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613101153 491 IIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKG 550
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
335-566 |
6.62e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.90 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTL---CHLLLRfYDIDDGIIRIDGVDIKDMTLSTLMSKIS 411
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLfmnLSGLLR-PQKGAVLWQGKPLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQ--KVYLFNDTIENNILFG--NPGATKEEIIRAAKQAcchdfiMSLPEGyQTMLNEKGSNLSGGEKQRISIARAILK 487
Cdd:PRK13638 81 TVFQdpEQQIFYTDIDSDIAFSlrNLGVPEAEITRRVDEA------LTLVDA-QHFRHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 488 DAPIIILDEATSSIDPENE-QLIQTAINELSKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKG------SHDELIRKP 559
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRtQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGapgevfACTEAMEQA 233
|
....*..
gi 613101153 560 GMYQDFI 566
Cdd:PRK13638 234 GLTQPWL 240
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
335-557 |
7.35e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 7.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIiridgVDIKDMTLSTLMSKISA-- 412
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGT-----ITINNINYNKLDHKLAAql 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 ----VFQKVYLFND-TIENNILFG----------NPGATKEEIIRAAkqacchdfIMSLPEGYQTMLNEKGSNLSGGEKQ 477
Cdd:PRK09700 81 gigiIYQELSVIDElTVLENLYIGrhltkkvcgvNIIDWREMRVRAA--------MMLLRVGLKVDLDEKVANLSISHKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 478 RISIARAILKDAPIIILDEATSSI-DPENEQLIqTAINELSK-GKTVITIAHKLETIKN-ADQIIVLNEGE-----IIQK 549
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLF-LIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDGSsvcsgMVSD 231
|
....*...
gi 613101153 550 GSHDELIR 557
Cdd:PRK09700 232 VSNDDIVR 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
335-559 |
1.34e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.49 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTL--CHLLLRfydiddgIIRIDGVDIKDMTLST------- 405
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLE-------QPEAGTIRVGDITIDTarslsqq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 406 ------LMSKISAVFQKVYLF-NDTIENNILFGnP----GATKEEIIRAAKQACCHDFIMSLPEGYQtmlnekgSNLSGG 474
Cdd:PRK11264 77 kglirqLRQHVGFVFQNFNLFpHRTVLENIIEG-PvivkGEPKEEATARARELLAKVGLAGKETSYP-------RRLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 475 EKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGK-TVITIAHKLETIKN-ADQIIVLNEGEIIQKGSH 552
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPA 228
|
....*..
gi 613101153 553 DELIRKP 559
Cdd:PRK11264 229 KALFADP 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
335-556 |
1.37e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.11 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMsKISAV- 413
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA-RIGVVp 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 414 -FQKVYLFNDTIENNILFGNPGATKEEIIRAAkqacchdfIMSLPE--GYQTMLNEKGSNLSGGEKQRISIARAILKDAP 490
Cdd:PRK13536 121 qFDNLDLEFTVRENLLVFGRYFGMSTREIEAV--------IPSLLEfaRLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 491 IIILDEATSSIDPENEQLIQTAINE-LSKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELI 556
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
334-559 |
1.48e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 84.70 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 334 NIAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLchllLRFydiddgiiridGVDIKDMTLSTLM------ 407
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTL----LRM-----------IAGLEDITSGDLFigekrm 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 408 -----SK--ISAVFQKVYLF-NDTIENNILFGN--PGATKEEIIRAAKQACchdFIMSLPEgyqtMLNEKGSNLSGGEKQ 477
Cdd:PRK11000 68 ndvppAErgVGMVFQSYALYpHLSVAENMSFGLklAGAKKEEINQRVNQVA---EVLQLAH----LLDRKPKALSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 478 RISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAH-KLETIKNADQIIVLNEGEIIQKGSHDE 554
Cdd:PRK11000 141 RVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
....*
gi 613101153 555 LIRKP 559
Cdd:PRK11000 221 LYHYP 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
338-558 |
1.50e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.51 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL---LRFYdiddgiirIDGVDIKDMTLSTL----MSKI 410
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsgeLSPD--------SGEVRLNGRPLADWspaeLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 411 SAVF-QKVYL-FNDTIENNILFG-----NPGATKEEIIRAAKQAC-CHDFimslpEG--YQTmlnekgsnLSGGEKQRIS 480
Cdd:PRK13548 78 RAVLpQHSSLsFPFTVEEVVAMGraphgLSRAEDDALVAAALAQVdLAHL-----AGrdYPQ--------LSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 481 IARAIL------KDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLetikN-----ADQIIVLNEGEII 547
Cdd:PRK13548 145 LARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHerGLAVIVVLHDL----NlaaryADRIVLLHQGRLV 220
|
250
....*....|....*.
gi 613101153 548 QKGS-----HDELIRK 558
Cdd:PRK13548 221 ADGTpaevlTPETLRR 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
338-550 |
1.61e-17 |
|
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: 81.49 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRidgVDIKDMT-LSTLMSKISAVfqk 416
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT---FDGKSYQkNIEALRRIGAL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 vylfndtIENNILFGNpgATKEEIIRAAkqACCHDF----IMSLPE--GYQTMLNEKGSNLSGGEKQRISIARAILKDAP 490
Cdd:cd03268 78 -------IEAPGFYPN--LTARENLRLL--ARLLGIrkkrIDEVLDvvGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613101153 491 IIILDEATSSIDPEN-EQLIQTAINELSKGKTVITIAHKLETI-KNADQIIVLNEGEIIQKG 550
Cdd:cd03268 147 LLILDEPTNGLDPDGiKELRELILSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
353-561 |
1.76e-17 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 84.01 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 353 VNFEIPTQTSTAIIGPSGSGKSTLCHL---LLRFYDIDDGIIRIDGVDI-KDMTLSTLMSKISAVFQKVYLFND-TIENN 427
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLiagLTRPDEGEIVLNGRTLFDSrKGIFLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 428 ILFGNPGAT-KEEIIRAAKqacchdfIMSLpEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENE 506
Cdd:TIGR02142 96 LRYGMKRARpSERRISFER-------VIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 507 QLIQTAINELSK--GKTVITIAHKL-ETIKNADQIIVLNEGEIIQKGSHDELIRKPGM 561
Cdd:TIGR02142 168 YEILPYLERLHAefGIPILYVSHSLqEVLRLADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
320-559 |
2.41e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.68 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 320 ELDENgKNLTIKNENIAFQNvnfsyDDKQV--IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRI---- 393
Cdd:PRK10261 6 ELDAR-DVLAVENLNIAFMQ-----EQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkml 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 394 ------DGVDIKDMTLSTLM----SKISAVFQK-------VYLFNDTIENNILFgNPGATKEEIIRAAKQACCHdfiMSL 456
Cdd:PRK10261 80 lrrrsrQVIELSEQSAAQMRhvrgADMAMIFQEpmtslnpVFTVGEQIAESIRL-HQGASREEAMVEAKRMLDQ---VRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 457 PEGyQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENE----QLIQTAINELSKGktVITIAHKLETI 532
Cdd:PRK10261 156 PEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilQLIKVLQKEMSMG--VIFITHDMGVV 232
|
250 260
....*....|....*....|....*...
gi 613101153 533 KN-ADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK10261 233 AEiADRVLVMYQGEAVETGSVEQIFHAP 260
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
335-541 |
2.99e-17 |
|
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: 80.60 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLchllLRfydiddgiiridgvdikdmTLSTLM------- 407
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTL----LR-------------------ILAGLLppsagev 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 408 --------SKISAVFQKV-YLFND-------TIENNILF----GNPGATKEEIIRAAKQacchdfiMSLpEGYqtmLNEK 467
Cdd:COG4133 60 lwngepirDAREDYRRRLaYLGHAdglkpelTVRENLRFwaalYGLRADREAIDEALEA-------VGL-AGL---ADLP 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 468 GSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINE-LSKGKTVITIAHKLETIkNADQIIVL 541
Cdd:COG4133 129 VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLEL-AAARVLDL 202
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
338-559 |
4.22e-17 |
|
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: 80.66 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLchlllrFYDIDDGIIRID-GVDIKDMTLSTL-MSK-----I 410
Cdd:cd03218 4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTT------FYMIVGLVKPDSgKILLDGQDITKLpMHKrarlgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 411 SAVFQKVYLFND-TIENNIL-----FGNPGATKEEIIraakQACCHDFimslpeGYQTMLNEKGSNLSGGEKQRISIARA 484
Cdd:cd03218 78 GYLPQEASIFRKlTVEENILavleiRGLSKKEREEKL----EELLEEF------HITHLRKSKASSLSGGERRRVEIARA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 485 ILKDAPIIILDEATSSIDPENEQLIQTAINELS-KGKTV-ITIAHKLETIKNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKdRGIGVlITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
335-559 |
6.07e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 80.51 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVF 414
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKvylfND-----TIENNILFG-------NPGATKEEIIRAAKQAcchdfiMSLPEGYQTMLNEkgsnLSGGEKQRISIA 482
Cdd:COG4604 82 QE----NHinsrlTVRELVAFGrfpyskgRLTAEDREIIDEAIAY------LDLEDLADRYLDE----LSGGQRQRAFIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 483 RAILKDAPIIILDEATSSIDPENE----QLIQTAINELskGKTVITIAHKLetikN-----ADQIIVLNEGEIIQKGSHD 553
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSvqmmKLLRRLADEL--GKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPE 221
|
....*.
gi 613101153 554 ELIRKP 559
Cdd:COG4604 222 EIITPE 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
338-559 |
9.63e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.19 E-value: 9.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMtlSTLMSKISAVFQKV 417
Cdd:PRK11607 23 RNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 418 YLF-NDTIENNILFgnpGATKEEIIRAAKQACCHDfIMSLPEgYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDE 496
Cdd:PRK11607 101 ALFpHMTVEQNIAF---GLKQDKLPKAEIASRVNE-MLGLVH-MQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 497 ATSSIDPENEQLIQTAINELSK--GKTVITIAH-KLETIKNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
19-302 |
1.04e-16 |
|
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: 80.67 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 19 MILGFSMSFLNAIFIALPIFLAAKIFNNVLSHKPIYMkdILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMSAKERLDI 98
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSL--LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 99 GDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSLLACIGVLLSFFAIQL 178
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 179 LERKSRqnaPAYHNVQNQ---LVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTKIEM-QYIPFNLLHLLSLk 254
Cdd:cd07346 159 FRRRIR---KASREVRESlaeLSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARlSALFSPLIGLLTA- 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 613101153 255 VVSIMIVLVACLLYMNHSIDLPTLIMISIFSFVIFDSVENINSAAHVL 302
Cdd:cd07346 235 LGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQL 282
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
335-551 |
1.07e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.44 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTL---------------CHLLLrfYDIDDGIIRIDGVDIK 399
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlsglitgdksagSHIEL--LGRTVQREGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 400 DMTLSTlmskiSAVFQKVYLFND-TIENNILFGNPGATK--EEIIRAAKQACCHDFIMSLPE-GYQTMLNEKGSNLSGGE 475
Cdd:PRK09984 83 KSRANT-----GYIFQQFNLVNRlSVLENVLIGALGSTPfwRTCFSWFTREQKQRALQALTRvGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 476 KQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLE-TIKNADQIIVLNEGEIIQKGS 551
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
346-550 |
1.65e-16 |
|
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: 78.85 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 346 DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLF-NDTI 424
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLpGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 425 ENNILFGNPGATKEEIIRAAKQAccHDFIMSLPEGYQTML-NEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDP 503
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKK--RVEDVLLRDLALTRIgGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 613101153 504 ENE-QLIQTAINELSKGKTVITIAHK--LETIKNADQIIVLNEGEIIQKG 550
Cdd:cd03234 177 FTAlNLVSTLSQLARRNRIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
342-555 |
2.28e-16 |
|
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: 78.32 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 342 FSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLlrfydiddgiiridgVDIKDMTLSTLM-------------- 407
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML---------------TGELRPTSGTAYingysirtdrkaar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 408 SKISAVFQKVYLFND-TIENNILFGNP--GATKEEIIRAAKQACCHdfiMSLpEGYQtmlNEKGSNLSGGEKQRISIARA 484
Cdd:cd03263 75 QSLGYCPQFDALFDElTVREHLRFYARlkGLPKSEIKEEVELLLRV---LGL-TDKA---NKRARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613101153 485 ILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDEL 555
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
338-555 |
2.49e-16 |
|
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: 78.24 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSK-ISAVFQK 416
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 VYLFND-TIENNILFG---NPGATKEEIIraakqacchDFIMSL-PEGYQtMLNEKGSNLSGGEKQRISIARAILKDAPI 491
Cdd:cd03224 84 RRIFPElTVEENLLLGayaRRRAKRKARL---------ERVYELfPRLKE-RRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 492 IILDEATSSIDPENEQLIQTAINELSK-GKTVITI---AHKLETIknADQIIVLNEGEIIQKGSHDEL 555
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDeGVTILLVeqnARFALEI--ADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-559 |
2.83e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.37 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRF--------YDIDDGIIRIDGVDIKDMTlsTL 406
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgyrYSGDVLLGGRSIFNYRDVL--EF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 407 MSKISAVFQKVYLFNDTIENNILFG---NPGATKEEIiRAAKQACCHDfiMSLPEGYQTMLNEKGSNLSGGEKQRISIAR 483
Cdd:PRK14271 100 RRRVGMLFQRPNPFPMSIMDNVLAGvraHKLVPRKEF-RGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 484 AILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKL-ETIKNADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
338-556 |
5.36e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.10 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKV 417
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 418 YLFND-TIENNILFG----NPGATK-----EEIIRAAKQAcchdfimslpEGYQTMLNEKGSNLSGGEKQRISIARAILK 487
Cdd:PRK10253 91 TTPGDiTVQELVARGryphQPLFTRwrkedEEAVTKAMQA----------TGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613101153 488 DAPIIILDEATSSIDPENEQLIQTAINELS--KGKTVITIAHKL-ETIKNADQIIVLNEGEIIQKGSHDELI 556
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNreKGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
345-567 |
6.67e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.52 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 345 DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiddgIIRIDGVDIKDMTLSTLMSK--------ISAVFQK 416
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL------INSQGEIWFDGQPLHNLNRRqllpvrhrIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 vylfndtiENNILfgNPGATKEEIIRAAKQAccHDFIMSLPEGYQ---TMLNEKG----------SNLSGGEKQRISIAR 483
Cdd:PRK15134 371 --------PNSSL--NPRLNVLQIIEEGLRV--HQPTLSAAQREQqviAVMEEVGldpetrhrypAEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 484 AILKDAPIIILDEATSSIDpeneQLIQTAINELSKGK------TVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELI 556
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLD----KTVQAQILALLKSLqqkhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVF 514
|
250
....*....|.
gi 613101153 557 RKPGmyQDFIR 567
Cdd:PRK15134 515 AAPQ--QEYTR 523
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
335-558 |
7.04e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.24 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDK-----QVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDI----KDMTLST 405
Cdd:PRK13643 2 IKFEKVNYTYQPNspfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 406 LMSKISAVFQ--KVYLFNDTIENNILFG--NPGATKEEIIRAAKQAcchdfiMSLPEGYQTMLNEKGSNLSGGEKQRISI 481
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKEKAEKIAAEK------LEMVGLADEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 482 ARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRK 558
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
338-558 |
8.35e-16 |
|
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: 76.03 E-value: 8.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRF--YDIDDGIIRIDGVDIKDMTlstlMSKISavfq 415
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP----PEERA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 416 KVYLFndtiennILFGNPgatkEEI--IRAAkqacchDFIMSLPEGyqtmlnekgsnLSGGEKQRISIARAILKDAPIII 493
Cdd:cd03217 76 RLGIF-------LAFQYP----PEIpgVKNA------DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 494 LDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHK---LETIKnADQIIVLNEGEIIQKGShDELIRK 558
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLrEEGKSVLIITHYqrlLDYIK-PDRVHVLYDGRIVKSGD-KELALE 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
339-559 |
8.96e-16 |
|
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: 78.56 E-value: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 339 NVNFSYDDKQV--IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGII---RIDGVDIKDMTLSTLMS----K 409
Cdd:COG0444 8 KVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSgeiLFDGEDLLKLSEKELRKirgrE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 410 ISAVFQkvylfnD---------TIENNI---LFGNPGATKEEIIRAAKQAcchdfiMSL-----PEGYqtmLNEKGSNLS 472
Cdd:COG0444 88 IQMIFQ------DpmtslnpvmTVGDQIaepLRIHGGLSKAEARERAIEL------LERvglpdPERR---LDRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 473 GGEKQRISIARAILKDAPIIILDEATSSIDPeneqLIQTAI----NELSK--GKTVITIAHKLETIKN-ADQIIVLNEGE 545
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQIlnllKDLQRelGLAILFITHDLGVVAEiADRVAVMYAGR 228
|
250
....*....|....
gi 613101153 546 IIQKGSHDELIRKP 559
Cdd:COG0444 229 IVEEGPVEELFENP 242
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
335-542 |
1.67e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 74.50 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNF-SYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLchllLRfydiddgiiridgvdikdmTLSTL------- 406
Cdd:cd03223 1 IELENLSLaTPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FR-------------------ALAGLwpwgsgr 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 407 --MSKISAVF---QKVYLfndtiennilfgNPGATKEEIIRAAKQAcchdfimslpegyqtmlnekgsnLSGGEKQRISI 481
Cdd:cd03223 58 igMPEGEDLLflpQRPYL------------PLGTLREQLIYPWDDV-----------------------LSGGEQQRLAF 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 482 ARAILKDAPIIILDEATSSIDPENEQLIQTAINELskGKTVITIAHKLETIKNADQIIVLN 542
Cdd:cd03223 103 ARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHRPSLWKFHDRVLDLD 161
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
335-555 |
1.90e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 76.73 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMS---KIS 411
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrkRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKVYLFND-TIENNILFGNPGATK--EEIIRAAkqacchdFIMSLPE-GYQTMLNEKGSNLSGGEKQRISIARAILK 487
Cdd:PRK11831 88 MLFQSGALFTDmNVFDNVAYPLREHTQlpAPLLHST-------VMMKLEAvGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 488 DAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKL-ETIKNADQIIVLNEGEIIQKGSHDEL 555
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
343-541 |
1.91e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.96 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 343 SYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL---LRfydiddgiIRIDGVDIKDMTLSTLMSKISAVfqkVYL 419
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLagvLR--------PTSGTVRRAGGARVAYVPQRSEV---PDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 420 FNDTIENNI---LFGNPGATKEeiIRAAKQACCHDFIMSLpeGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDE 496
Cdd:NF040873 70 LPLTVRDLVamgRWARRGLWRR--LTRDDRAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 613101153 497 ATSSIDPENEQLIQTAINELS-KGKTVITIAHKLETIKNADQIIVL 541
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
348-558 |
3.21e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 75.85 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 348 QVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTlstlMSKISAV-----FQKVYLFND 422
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP----PHRIARLgiartFQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 423 --TIEN--------------NILFGNPGATKEEiiRAAKQACCH--DFImslpeGYQTMLNEKGSNLSGGEKQRISIARA 484
Cdd:COG0411 94 ltVLENvlvaaharlgrgllAALLRLPRARREE--REARERAEEllERV-----GLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 485 ILKDAPIIILDEATSSIDP-ENEQLIQTaINELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDElIRK 558
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPeETEELAEL-IRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE-VRA 242
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
337-549 |
3.22e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.24 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 337 FQNVNFSYDdkqVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLlrfydIDDGIIRIDGVDIKDMTLSTLMSKISA---- 412
Cdd:PRK11629 15 YQEGSVQTD---VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLL-----GGLDTPTSGDVIFNGQPMSKLSSAAKAelrn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 -----VFQKVYLFND--TIEN---NILFGnpGATKEEIIRAAKQacchdfiMSLPEGYQTMLNEKGSNLSGGEKQRISIA 482
Cdd:PRK11629 87 qklgfIYQFHHLLPDftALENvamPLLIG--KKKPAEINSRALE-------MLAAVGLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 483 RAILKDAPIIILDEATSSIDPENEQLIQTAINEL--SKGKTVITIAHKLETIKNADQIIVLNEGEIIQK 549
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
335-556 |
3.97e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.38 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMsKISAVF 414
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQ-RVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKVYLFND--TIENNILFGNPGATKEEIIRAAkqacchdfIMSLPE--GYQTMLNEKGSNLSGGEKQRISIARAILKDAP 490
Cdd:PRK13537 87 QFDNLDPDftVRENLLVFGRYFGLSAAAARAL--------VPPLLEfaKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 491 IIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELI 556
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
338-547 |
8.73e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.46 E-value: 8.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSY----DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDM---TLSTLMSK- 409
Cdd:PRK10535 8 KDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 410 ISAVFQKVYLFND-TIENNILFGNPGATKEeiiRAAKQACCHDFIMSLpeGYQTMLNEKGSNLSGGEKQRISIARAILKD 488
Cdd:PRK10535 88 FGFIFQRYHLLSHlTAAQNVEVPAVYAGLE---RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 489 APIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETIKNADQIIVLNEGEII 547
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
335-555 |
1.06e-14 |
|
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: 73.56 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDI-KDMTlsTLMSKISAV 413
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREPR--EVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 414 FQKVYLFND-TIENNI-----LFGNPGATKEEIIRAAKQAcchdfiMSLPEgyqtMLNEKGSNLSGGEKQRISIARAILK 487
Cdd:cd03265 79 FQDLSVDDElTGWENLyiharLYGVPGAERRERIDELLDF------VGLLE----AADRLVKTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 488 DAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETI-KNADQIIVLNEGEIIQKGSHDEL 555
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
344-559 |
1.32e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.85 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 344 YDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIK-------------DMTLSTLMSKI 410
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 411 SAVFQKVYLFND-TIENNILFGnP----GATKEEiirAAKQACCHDFIMSLPEGYQtmlNEKGSNLSGGEKQRISIARAI 485
Cdd:PRK10619 95 TMVFQHFNLWSHmTVLENVMEA-PiqvlGLSKQE---ARERAVKYLAKVGIDERAQ---GKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 486 LKDAPIIILDEATSSIDPENEQLIQTAINELS-KGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
335-545 |
1.73e-14 |
|
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: 70.56 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLrfydiddgiiridgvdikdmtlstlmskisavf 414
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 qkvylfndtiennilfGNPGATKEEIIRAAKqacchdfimsLPEGY--QtmlnekgsnLSGGEKQRISIARAILKDAPII 492
Cdd:cd03221 48 ----------------GELEPDEGIVTWGST----------VKIGYfeQ---------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 613101153 493 ILDEATSSIDPENEQLIQTAINELSkgKTVITIAHKLETIKN-ADQIIVLNEGE 545
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEYP--GTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
338-555 |
2.19e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 73.99 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRidgVDIKDMTLST------------ 405
Cdd:COG4152 5 KGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVL---WDGEPLDPEDrrrigylpeerg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 406 LMSKISAVFQKVYL--FNdtiennilfgnpGATKEEIIRAAkqacchDFIMS---LPEgyqtMLNEKGSNLSGGEKQRIS 480
Cdd:COG4152 82 LYPKMKVGEQLVYLarLK------------GLSKAEAKRRA------DEWLErlgLGD----RANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 481 IARAILKDAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETI-KNADQIIVLNEGEIIQKGSHDEL 555
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
338-558 |
2.83e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.79 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLL------------RFYDiddgiiridgVDIKDMT--- 402
Cdd:COG0396 4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghpkyevtsgsiLLDG----------EDILELSpde 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 403 -------LStlmskisavFQkvylfnDTIEnnIlfgnPGATKEEIIRAAKQACcHDFIMSLPEgYQTMLNEKGSNL---- 471
Cdd:COG0396 74 raragifLA---------FQ------YPVE--I----PGVSVSNFLRTALNAR-RGEELSARE-FLKLLKEKMKELglde 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 472 -----------SGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHK---LETIKnAD 536
Cdd:COG0396 131 dfldryvnegfSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrSPDRGILIITHYqriLDYIK-PD 209
|
250 260
....*....|....*....|..
gi 613101153 537 QIIVLNEGEIIQKGSHdELIRK 558
Cdd:COG0396 210 FVHVLVDGRIVKSGGK-ELALE 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-567 |
5.47e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.72 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRfydiddgiiridgvDIK----DMTL-STLmsK 409
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG--------------ELEpdsgTVKLgETV--K 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 410 IsAVF-QKVYLF--NDTIENNILFGNPGATKEEIIraakqACCHDFIMSlPEgyqtMLNEKGSNLSGGEKQRISIARAIL 486
Cdd:COG0488 380 I-GYFdQHQEELdpDKTVLDELRDGAPGGTEQEVR-----GYLGRFLFS-GD----DAFKPVGVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 487 KDAPIIILDEATSSIDPENEQLIQTAINELsKGkTVITIAHK---LETIknADQIIVLNEGEIIQkgshdelirKPGMYQ 563
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHDryfLDRV--ATRILEFEDGGVRE---------YPGGYD 515
|
....
gi 613101153 564 DFIR 567
Cdd:COG0488 516 DYLE 519
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
350-539 |
6.32e-14 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 70.04 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 350 IKNVNFEIPTQTSTAIIGPSGSGKSTLCHlllrfydiddgiiridgvdikdMTLSTLMSKISAVFQKVYLFNDTIENNIL 429
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN----------------------EGLYASGKARLISFLPKFSRNKLIFIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 430 fgnpgatkeeiiraakqacchDFIMSLPEGYQTmLNEKGSNLSGGEKQRISIARAILKDAP--IIILDEATSSIDPE-NE 506
Cdd:cd03238 69 ---------------------QFLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQdIN 126
|
170 180 190
....*....|....*....|....*....|....
gi 613101153 507 QLIQTaINEL-SKGKTVITIAHKLETIKNADQII 539
Cdd:cd03238 127 QLLEV-IKGLiDLGNTVILIEHNLDVLSSADWII 159
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
19-238 |
6.33e-14 |
|
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: 72.45 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 19 MILGFSMSFLNAIFIALPIFLAAKIFNNVLSHKPIYMkdILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMSAKERLDI 98
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEA--LLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 99 GDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSLLACIGVLLSFFAIQL 178
Cdd:cd18552 79 FDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613101153 179 LERKSRQNApayHNVQNQ---LVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTKI 238
Cdd:cd18552 159 IGKRLRKIS---RRSQESmgdLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKI 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
347-559 |
7.47e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 71.76 E-value: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 347 KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMS---KISAVFQKVY-LFND 422
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQDSPsAVNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 423 TIENNILFGNPGATKEEIIRAAKQACCHDFI--MSLPEgyqTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSS 500
Cdd:TIGR02769 104 RMTVRQIIGEPLRHLTSLDESEQKARIAELLdmVGLRS---EDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613101153 501 IDPENEQLIQTAINELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEII--QKGSHDELIRKP 559
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVeeCDVAQLLSFKHP 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
338-556 |
8.55e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 8.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLlrfydIDDGIIRIDGVDIKDMTLSTLMSK------IS 411
Cdd:PRK15439 15 RSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKII-----AGIVPPDSGTLEIGGNPCARLTPAkahqlgIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKVYLF-NDTIENNILFGNPG--ATKEEIIRAAKQACCHdfimslpegyqTMLNEKGSNLSGGEKQRISIARAILKD 488
Cdd:PRK15439 90 LVPQEPLLFpNLSVKENILFGLPKrqASMQKMKQLLAALGCQ-----------LDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 489 APIIILDEATSSIDP-ENEQLIQTaINEL-SKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKG-----SHDELI 556
Cdd:PRK15439 159 SRILILDEPTASLTPaETERLFSR-IRELlAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGktadlSTDDII 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
347-555 |
8.72e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.31 E-value: 8.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 347 KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTlMSKISAVFQKVYLF--NDTI 424
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKE-MRAISAYVQQDDLFipTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 425 ENNILF------GNPGATKE------EIIRAAKQACCHDFIMSLPEgyqtmlNEKGsnLSGGEKQRISIARAILKDAPII 492
Cdd:TIGR00955 117 REHLMFqahlrmPRRVTKKEkrervdEVLQALGLRKCANTRIGVPG------RVKG--LSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 493 ILDEATSSIDP-ENEQLIQTAINELSKGKTVITIAHK--LETIKNADQIIVLNEGEIIQKGSHDEL 555
Cdd:TIGR00955 189 FCDEPTSGLDSfMAYSVVQVLKGLAQKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
334-559 |
1.06e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.57 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 334 NIAFQNVNFSYDDK-QVIKNVNFEIPTQTSTAIIGPSGSGKSTLchllLRfydiddgiiridGV-----------DIKDM 401
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTL----LR------------MVagleritsgeiWIGGR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 402 TLSTLMSK---ISAVFQKVYLF-NDTIENNILFG--NPGATKEEIIR----AAKqacchdfIMSLpegyQTMLNEKGSNL 471
Cdd:PRK11650 67 VVNELEPAdrdIAMVFQNYALYpHMSVRENMAYGlkIRGMPKAEIEErvaeAAR-------ILEL----EPLLDRKPREL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 472 SGGEKQRISIARAILKDAPIIILDEATSSIDPeneQL-IQTAInELSK-----GKTVITIAH-KLETIKNADQIIVLNEG 544
Cdd:PRK11650 136 SGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA---KLrVQMRL-EIQRlhrrlKTTSLYVTHdQVEAMTLADRVVVMNGG 211
|
250
....*....|....*
gi 613101153 545 EIIQKGSHDELIRKP 559
Cdd:PRK11650 212 VAEQIGTPVEVYEKP 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
472-544 |
1.09e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 70.54 E-value: 1.09e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 472 SGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETIKN-ADQIIVLNEG 544
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
338-543 |
1.43e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.82 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMT-LSTLMSKISAVFQK 416
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRRLTaLPAEQRRIGILFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 VYLF-NDTIENNILFGNPGATKeeiiRAAKQACChdfimslpegyQTMLNEKG---------SNLSGGEKQRISIARAIL 486
Cdd:COG4136 85 DLLFpHLSVGENLAFALPPTIG----RAQRRARV-----------EQALEEAGlagfadrdpATLSGGQRARVALLRALL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 487 KDAPIIILDEATSSIDPE-NEQLIQTAINEL-SKGKTVITIAHKLETIKNADQIIVLNE 543
Cdd:COG4136 150 AEPRALLLDEPFSKLDAAlRAQFREFVFEQIrQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
335-550 |
1.72e-13 |
|
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: 69.70 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDK----QVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLmSKI 410
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR-RRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 411 SAVFQK--VYLFNDTIENNILFGNPGATKeeiiRAAKQACCHDFIMSLpeGYQTMLNEKGSNLSGGEKQRISIARAILKD 488
Cdd:cd03266 81 GFVSDStgLYDRLTARENLEYFAGLYGLK----GDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613101153 489 APIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKG 550
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
335-561 |
2.03e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.03 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDD-KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL--LRFYDIDDGIIRIDGVDIKDMTLSTLMSKIS 411
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLngILKPSSGRILFDGKPIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKV--YLFNDTIENNILFG--NPGATKEEIIRAAKQACCHdfimslpEGYQTMLNEKGSNLSGGEKQRISIARAILK 487
Cdd:PRK13636 86 MVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKR-------TGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 488 DAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIK-NADQIIVLNEGEIIQKGSHDELIRKPGM 561
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
352-551 |
2.34e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.44 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 352 NVNFEIPTQTSTAIIGPSGSGKSTLCHL---LLRFYDIDDGIIRIDGVDI-KDMTLSTLMSKISAVFQKVYLF-NDTIEN 426
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAisgLTRPQKGRIVLNGRVLFDAeKGICLPPEKRRIGYVFQDARLFpHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 427 NILFGNPGATKEEIiraakqacchDFIMSLPeGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSID-PEN 505
Cdd:PRK11144 96 NLRYGMAKSMVAQF----------DKIVALL-GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 613101153 506 EQLIQTaINELSKG-KT-VITIAHKL-ETIKNADQIIVLNEGEIIQKGS 551
Cdd:PRK11144 165 RELLPY-LERLAREiNIpILYVSHSLdEILRLADRVVVLEQGKVKAFGP 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
351-559 |
3.77e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 72.02 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 351 KNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiddgIIRIDGVDIKDMTLSTLMSK--------ISAVFQKVY-LFN 421
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRL------IPSEGEIRFDGQDLDGLSRRalrplrrrMQVVFQDPFgSLS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 422 ------DTIENNILFGNPGATKEEIIRAAKQAcchdfiMS---LPEGyqtMLN----EkgsnLSGGEKQRISIARA-ILK 487
Cdd:COG4172 377 prmtvgQIIAEGLRVHGPGLSAAERRARVAEA------LEevgLDPA---ARHryphE----FSGGQRQRIAIARAlILE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 488 daP-IIILDEATSSIDpeneQLIQTAINELSK------GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:COG4172 444 --PkLLVLDEPTSALD----VSVQAQILDLLRdlqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
469-547 |
6.77e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.21 E-value: 6.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 469 SNLSGGEKQRISIARAILKDAPIIILDEATSSIDP-ENEQLIQTaINEL-SKGKTVITIAHKLETIK-NADQIIVLNEGE 545
Cdd:COG3845 140 EDLSVGEQQRVEILKALYRGARILILDEPTAVLTPqEADELFEI-LRRLaAEGKSIIFITHKLREVMaIADRVTVLRRGK 218
|
..
gi 613101153 546 II 547
Cdd:COG3845 219 VV 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
338-548 |
9.07e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 9.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQ--VIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRidgVDIKDMTLSTLMSKISAVFQ 415
Cdd:COG2401 32 EAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC---VDVPDNQFGREASLIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 416 KvylfndtiennilfGNPGATKEeIIRAAKqacchdfimslpegyqtmLNE------KGSNLSGGEKQRISIARAILKDA 489
Cdd:COG2401 109 K--------------GDFKDAVE-LLNAVG------------------LSDavlwlrRFKELSTGQKFRFRLALLLAERP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613101153 490 PIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIK--NADQIIVLNEGEIIQ 548
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQKLARraGITLVVATHHYDVIDdlQPDLLIFVGYGGVPE 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
471-546 |
1.77e-12 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 65.92 E-value: 1.77e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 471 LSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELS-KGKTVITIAHKL-ETIKNADQIIVLNEGEI 546
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdAGKAVLLISSELdELLGLCDRILVMYEGRI 182
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
342-559 |
2.14e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 67.56 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 342 FSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLlrfydIDDGIIRIDGVDIKDMTL-----STLMSKISAVFQK 416
Cdd:COG4167 21 FRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKML-----AGIIEPTSGEILINGHKLeygdyKYRCKHIRMIFQD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 VylfndtieNNILfgNPGATKEEIiraakqacchdfiMSLPEGYQTMLNEKGSN-----------------------LSG 473
Cdd:COG4167 96 P--------NTSL--NPRLNIGQI-------------LEEPLRLNTDLTAEEREerifatlrlvgllpehanfyphmLSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 474 GEKQRISIARAILKDAPIIILDEATSSIDPE-NEQLiqtaIN---ELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEI 546
Cdd:COG4167 153 GQKQRVALARALILQPKIIIADEALAALDMSvRSQI----INlmlELQEklGISYIYVSQHLGIVKHiSDKVLVMHQGEV 228
|
250
....*....|...
gi 613101153 547 IQKGSHDELIRKP 559
Cdd:COG4167 229 VEYGKTAEVFANP 241
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
350-541 |
2.38e-12 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 67.25 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 350 IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLrfYDIDDGIIRIDGVDIKDMTLSTLMSKIS------------------ 411
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTL--YPALARRLHLKKEQPGNHDRIEGLEHIDkvividqspigrtprsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKVY-----LFND----------TIEnnILFgnPGATKEEIIR-AAKQAccHDFIMSLPE-------------GYQT 462
Cdd:cd03271 89 ATYTGVFdeireLFCEvckgkrynreTLE--VRY--KGKSIADVLDmTVEEA--LEFFENIPKiarklqtlcdvglGYIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 463 mLNEKGSNLSGGEKQRISIARAILKDAP---IIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETIKNADQI 538
Cdd:cd03271 163 -LGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIEHNLDVIKCADWI 241
|
...
gi 613101153 539 IVL 541
Cdd:cd03271 242 IDL 244
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
335-546 |
3.26e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.01 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVdikdmTLSTLMSKISAVF 414
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-----PLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKVYLFN-DTIENNILFGNPGATKEEIIRAAKQAcchdfimslpeGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIII 493
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGLKGQWRDAALQALAAV-----------GLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 494 LDEATSSIDP----ENEQLIQTAINElsKGKTVITIAHKL-ETIKNADQIIVLNEGEI 546
Cdd:PRK11247 157 LDEPLGALDAltriEMQDLIESLWQQ--HGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
352-561 |
1.61e-11 |
|
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: 65.89 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 352 NVNFEIPTQTSTAIIGPSGSGKSTLCHL---LLRfydiddgiIRIDGVDIKDMTL--STLMS-------KISAVFQKVYL 419
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER--------PDSGRIRLGGEVLqdSARGIflpphrrRIGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 420 FND-TIENNILFG-------NPGATKEEIIRAakqacchdfimsLpeGYQTMLNEKGSNLSGGEKQRISIARAILKDAPI 491
Cdd:COG4148 89 FPHlSVRGNLLYGrkrapraERRISFDEVVEL------------L--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 492 IILDEATSSID--------PENEQLIQ-TAInelskgkTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKPGM 561
Cdd:COG4148 155 LLMDEPLAALDlarkaeilPYLERLRDeLDI-------PILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSRPDL 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
352-557 |
1.67e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 64.63 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 352 NVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTlSTLMSKISAV--FQKVYLFND--TIEN- 426
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVVrtFQHVRLFREmtVIENl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 427 ----------NI---LFGNPG---ATKEEIIRAAKQAcchDFImslpeGYQTMLNEKGSNLSGGEKQRISIARAILKDAP 490
Cdd:PRK11300 102 lvaqhqqlktGLfsgLLKTPAfrrAESEALDRAATWL---ERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 491 IIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDElIR 557
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEE-IR 242
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
20-279 |
2.19e-11 |
|
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: 64.74 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 20 ILGFSMSFL-NAIFIALPIFLaaKIFNNVLSHKPIYMKDILNVVIIMVLLV----IGRFITAYFKSKSHESIAYEMsake 94
Cdd:cd18541 2 LLGILFLILvDLLQLLIPRII--GRAIDALTAGTLTASQLLRYALLILLLAlligIFRFLWRYLIFGASRRIEYDL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 95 RLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFA----MKMVDVVVNGyiliIVLILSLLVVSWQVSLLACIGVL 170
Cdd:cd18541 76 RNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALgpgiLYLVDALFLG----VLVLVMMFTISPKLTLIALLPLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 171 LSFFAIQLLERKSRQnapAYHNVQNQ---LVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRIN---TKIEMQYIP 244
Cdd:cd18541 152 LLALLVYRLGKKIHK---RFRKVQEAfsdLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNlrlARVDALFFP 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 613101153 245 fnLLHLLSlkVVSIMIVLVAC-LLYMNHSIDLPTLI 279
Cdd:cd18541 229 --LIGLLI--GLSFLIVLWYGgRLVIRGTITLGDLV 260
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
335-553 |
2.30e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.74 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSY-DDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDI---KDMTLSTLMSKI 410
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 411 SAVFQKVYLFND-TIENNILFgnP----GATKEEIIRAAKQACchdfimslpegYQTMLNEKGSN----LSGGEKQRISI 481
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAI--PliiaGASGDDIRRRVSAAL-----------DKVGLLDKAKNfpiqLSGGEQQRVGI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613101153 482 ARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETIKNAD-QIIVLNEGEIIqkGSHD 553
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSyRMLTLSDGHLH--GGVG 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
338-559 |
2.48e-11 |
|
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: 63.85 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCH----LL------LRFydiddgiiriDGVDIKDMTLSTLM 407
Cdd:COG0410 7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaisgLLpprsgsIRF----------DGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 408 SK-ISAVFQKVYLFND-TIENNILFGNPGATKEEIIRAAKqacchDFIMSL-PEGYQtMLNEKGSNLSGGEKQRISIARA 484
Cdd:COG0410 77 RLgIGYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADL-----ERVYELfPRLKE-RRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 485 ILKDAPIIILDEATSSIDPeneQLIQT---AINEL-SKGKTVI------TIAHKLetiknADQIIVLNEGEIIQKGSHDE 554
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAP---LIVEEifeIIRRLnREGVTILlveqnaRFALEI-----ADRAYVLERGRIVLEGTAAE 222
|
....*
gi 613101153 555 LIRKP 559
Cdd:COG0410 223 LLADP 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
335-550 |
2.97e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 65.63 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVF 414
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKVYL-FNDTIENNI---------LFGNPGATKEEIIRAAKQACchdfimslpeGYQTMLNEKGSNLSGGEKQRISIARA 484
Cdd:PRK09536 84 QDTSLsFEFDVRQVVemgrtphrsRFDTWTETDRAAVERAMERT----------GVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 485 ILKDAPIIILDEATSSIDPeNEQlIQT--AINELSK-GKTVITIAHKLE-TIKNADQIIVLNEGEIIQKG 550
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDI-NHQ-VRTleLVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
350-550 |
4.01e-11 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 63.05 E-value: 4.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 350 IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLL-----RFYDIDDGI---IRIDGVDIKDMTLSTLMSKISAVFQKvylfn 421
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIyaegqRRYVESLSAyarQFLGQMDKPDVDSIEGLSPAIAIDQK----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 422 dTIENN----------------ILFGNPGatkeeiIRAAKQacchdFIMSLPEGYQTMLNEKGSnLSGGEKQRISIARAI 485
Cdd:cd03270 86 -TTSRNprstvgtvteiydylrLLFARVG------IRERLG-----FLVDVGLGYLTLSRSAPT-LSGGEAQRIRLATQI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 486 ---LKDApIIILDEATSSIDP-ENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVL------NEGEIIQKG 550
Cdd:cd03270 153 gsgLTGV-LYVLDEPSIGLHPrDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
336-563 |
4.14e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 336 AFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIiridgVDIKDMTLSTLMSKISAvfQ 415
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGE-----ILLDAQPLESWSSKAFA--R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 416 KV-YLFNDtienniLFGNPGATKEEII--------------RAAKQACCHDFIMSLpeGYQTMLNEKGSNLSGGEKQRIS 480
Cdd:PRK10575 86 KVaYLPQQ------LPAAEGMTVRELVaigrypwhgalgrfGAADREKVEEAISLV--GLKPLAHRLVDSLSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 481 IARAILKDAPIIILDEATSSIDPENEQLIQTAINELS--KGKTVITIAHKLE-TIKNADQIIVLNEGEIIQKGSHDELIR 557
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqeRGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMR 237
|
....*.
gi 613101153 558 KPGMYQ 563
Cdd:PRK10575 238 GETLEQ 243
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
347-548 |
8.22e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.78 E-value: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 347 KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiddGIIRIDGVDIKDMTLSTLMSKISAVFQK-VYL-FNDTI 424
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-----ESPSQGNVSWRGEPLAKLNRAQRKAFRRdIQMvFQDSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 425 ENNilfgNPGATKEEIIR-----------AAKQACCHDFI--MSLPEgyqTMLNEKGSNLSGGEKQRISIARAILKDAPI 491
Cdd:PRK10419 100 SAV----NPRKTVREIIReplrhllsldkAERLARASEMLraVDLDD---SVLDKRPPQLSGGQLQRVCLARALAVEPKL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613101153 492 IILDEATSSIDpeneQLIQTAINELSK------GKTVITIAHKLETIKN-ADQIIVLNEGEIIQ 548
Cdd:PRK10419 173 LILDEAVSNLD----LVLQAGVIRLLKklqqqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-547 |
8.43e-11 |
|
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: 64.43 E-value: 8.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 13 RPYKARMILGFSMSFLNAIFIALpifLAAKIfNNVLSHKP-IYMKDILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMs 91
Cdd:COG4615 9 RESRWLLLLALLLGLLSGLANAG---LIALI-NQALNATGaALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 92 akeRLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVN--------GYILIIVlilsllvvsWQVSL 163
Cdd:COG4615 84 ---RLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSvalvlgclAYLAWLS---------PPLFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 164 LACIGVLLSFFAIQLLERKSRQNAPAYHNVQNQLVEKVLEVIRGIQVIK-------SFAKENtslksFNQSVNESKRINT 236
Cdd:COG4615 152 LTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKlnrrrrrAFFDED-----LQPTAERYRDLRI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 237 KIEMQyipFNLLHLLSLKVVSIMIVLVACLLYMNHSIDLPTLimiSIFSFVI---FDSVENINSAAHVLEMIDMTIDDIE 313
Cdd:COG4615 227 RADTI---FALANNWGNLLFFALIGLILFLLPALGWADPAVL---SGFVLVLlflRGPLSQLVGALPTLSRANVALRKIE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 314 KIKNAPELDENGKNLTIKN------ENIAFQNVNFSYDDKQ-----VIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLR 382
Cdd:COG4615 301 ELELALAAAEPAAADAAAPpapadfQTLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 383 FYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDtienniLFGNPGATKEEIIRAakqacchdfimslpegYQT 462
Cdd:COG4615 381 LYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR------LLGLDGEADPARARE----------------LLE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 463 MLN-------EKGS----NLSGGEKQRISIARAILKDAPIIILDEATSSIDPEN-----EQLIQtainEL-SKGKTVITI 525
Cdd:COG4615 439 RLEldhkvsvEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFrrvfyTELLP----ELkARGKTVIAI 514
|
570 580
....*....|....*....|....*..
gi 613101153 526 AH-----KLetiknADQIIVLNEGEII 547
Cdd:COG4615 515 SHddryfDL-----ADRVLKMDYGKLV 536
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
338-556 |
8.76e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLrfyDIDDGIIRIDGVDIKDMTLSTLMSKI------- 410
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVV---GIVPRDAGNIIIDDEDISLLPLHARArrgigyl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 411 ---SAVFQKVYLFNDTIEnnILFGNPGATKEEIIRAAKQaCCHDFIMSlpegyqTMLNEKGSNLSGGEKQRISIARAILK 487
Cdd:PRK10895 84 pqeASIFRRLSVYDNLMA--VLQIRDDLSAEQREDRANE-LMEEFHIE------HLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 488 DAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKL-ETIKNADQIIVLNEGEIIQKGSHDELI 556
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLrDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
335-543 |
1.02e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.44 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiddgIIRIDGVDIKDMTLstlmsKISAVF 414
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGL------VAPDEGVIKRNGKL-----RIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKVYL---FNDTIENNILFgNPGATKEEIIRAAK--QAcchdfimslpegyQTMLNEKGSNLSGGEKQRISIARAILKDA 489
Cdd:PRK09544 74 QKLYLdttLPLTVNRFLRL-RPGTKKEDILPALKrvQA-------------GHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 490 PIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETI-KNADQIIVLNE 543
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCLNH 196
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
335-548 |
1.08e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.22 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQV-IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAV 413
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 414 FQKVYLFNDtienniLFGNPGATKEEiirAAKQACCHDFIM----SLPEGyqTMLNEKgsnLSGGEKQRISIARAILKDA 489
Cdd:PRK10522 403 FTDFHLFDQ------LLGPEGKPANP---ALVEKWLERLKMahklELEDG--RISNLK---LSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 490 PIIILDEATSSIDPENEQLI-QTAINEL-SKGKTVITIAHKLETIKNADQIIVLNEGEIIQ 548
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFyQVLLPLLqEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
338-547 |
1.35e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFY-------DIDDGIIRIDGVDIKDmtlsTLMSKI 410
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgtyegEIIFEGEELQASNIRD----TERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 411 SAVFQKVYLFND-TIENNILFGNpgatkeEIIRAAkqacchdfIMSLPEGY---QTMLNE---------KGSNLSGGEKQ 477
Cdd:PRK13549 85 AIIHQELALVKElSVLENIFLGN------EITPGG--------IMDYDAMYlraQKLLAQlkldinpatPVGNLGLGQQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613101153 478 RISIARAILKDAPIIILDEATSSI-DPENEQLIqTAINEL-SKGKTVITIAHKLETIKN-ADQIIVLNEGEII 547
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLtESETAVLL-DIIRDLkAHGIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
335-548 |
1.60e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 61.30 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDK----QVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLL--LrfydiddGIIRIDGVDIKDMTLSTL-- 406
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLagL-------DRPTSGTVRLAGQDLFALde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 407 -------MSKISAVFQKVYLF-NDTIENNI-----LFGNPGATKeeiiRAAKqacchdfimslpegyqtMLNEKG----- 468
Cdd:COG4181 82 dararlrARHVGFVFQSFQLLpTLTALENVmlpleLAGRRDARA----RARA-----------------LLERVGlghrl 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 469 ----SNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKNADQIIVLN 542
Cdd:COG4181 141 dhypAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTHDPALAARCDRVLRLR 220
|
....*.
gi 613101153 543 EGEIIQ 548
Cdd:COG4181 221 AGRLVE 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
350-550 |
1.72e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.82 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 350 IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFNDTIENNIL 429
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 430 FGNPGATKeeIIRAAK---QACCHDFIMSLpeGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENE 506
Cdd:PRK15056 103 MGRYGHMG--WLRRAKkrdRQIVTAALARV--DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 613101153 507 QLIQTAINEL-SKGKTVITIAHKLETIKNADQIIVLNEGEIIQKG 550
Cdd:PRK15056 179 ARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
336-557 |
1.88e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 336 AFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRidgVDIKDMTLSTLMSKISA--- 412
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL---IDGQEMRFASTTAALAAgva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 -VFQKVYLFND-TIENNILFGN-PGA----TKEEIIRAAKQACCH---DFIMSLPEGYqtmlnekgsnLSGGEKQRISIA 482
Cdd:PRK11288 83 iIYQELHLVPEmTVAENLYLGQlPHKggivNRRLLNYEAREQLEHlgvDIDPDTPLKY----------LSIGQRQMVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 483 RAILKDAPIIILDEATSSID-PENEQLIQTaINEL-SKGKTVITIAHKLETI-KNADQIIVLNEG------EIIQKGSHD 553
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSaREIEQLFRV-IRELrAEGRVILYVSHRMEEIfALCDAITVFKDGryvatfDDMAQVDRD 231
|
....
gi 613101153 554 ELIR 557
Cdd:PRK11288 232 QLVQ 235
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
471-556 |
1.91e-10 |
|
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: 63.88 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 471 LSGGEKQRISIARAILKDA---PIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETIKNADQIIVL----- 541
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVLQRLvDKGNTVVVIEHNLDVIKTADYIIDLgpegg 909
|
90
....*....|....*.
gi 613101153 542 -NEGEIIQKGSHDELI 556
Cdd:TIGR00630 910 dGGGTVVASGTPEEVA 925
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
352-559 |
2.38e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.06 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 352 NVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMS---KISAVFQ----------KVY 418
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQdpyaslnprmTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 419 lfnDTIE-----NNILfgnPGATKEEIIRAakqacchdfIMSL----PEGYQTMLNEkgsnLSGGEKQRISIARAILKDA 489
Cdd:COG4608 116 ---DIIAeplriHGLA---SKAERRERVAE---------LLELvglrPEHADRYPHE----FSGGQRQRIGIARALALNP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 490 PIIILDEATSSIDPEneqlIQTAI----NELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:COG4608 177 KLIVCDEPVSALDVS----IQAQVlnllEDLQDelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
469-565 |
2.77e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.10 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 469 SNLSGGEKQRISIARAILKDAPII-------ILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKL-ETIKNADQII 539
Cdd:PRK03695 125 NQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLnHTLRHADRVW 204
|
90 100
....*....|....*....|....*.
gi 613101153 540 VLNEGEIIQKGSHDELIRKPGMYQDF 565
Cdd:PRK03695 205 LLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
338-551 |
3.18e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRF--YDIDDGIIRIDGVDIKDMTlSTLMSKISavfq 415
Cdd:CHL00131 11 KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLG---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 416 kVYL-FNDTIENnilfgnPGATKEEIIRAAKQACcHDFiMSLPE----GYQTMLNEK---------------GSNLSGGE 475
Cdd:CHL00131 86 -IFLaFQYPIEI------PGVSNADFLRLAYNSK-RKF-QGLPEldplEFLEIINEKlklvgmdpsflsrnvNEGFSGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 476 KQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELS-KGKTVITIAHK---LETIKnADQIIVLNEGEIIQKGS 551
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHYqrlLDYIK-PDYVHVMQNGKIIKTGD 235
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
23-297 |
4.44e-10 |
|
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: 61.04 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 23 FSMSFLNAIFIALPiFLAAKIFNNVLshKPIYMKDILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMSAKERLDIGDKL 102
Cdd:cd18557 3 LFLLISSAAQLLLP-YLIGRLIDTII--KGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 103 KNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSLLACIGVLLSFFAIQLLERK 182
Cdd:cd18557 80 LRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 183 SRQNAPAYHNVQNQLVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTKIEMQYIPFNLLHLLSLKVVSIMIVL 262
Cdd:cd18557 160 IRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLW 239
|
250 260 270
....*....|....*....|....*....|....*
gi 613101153 263 VACLLYMNHSIDLPTLIMISIFSFVIFDSVENINS 297
Cdd:cd18557 240 YGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSS 274
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
346-538 |
5.79e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 59.12 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 346 DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMskisavfqkVYL-----F 420
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAC---------HYLghrnaM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 421 ND--TIENNILF-GNPGATKEEIIRAAkqACCHDF--IMSLPEGYqtmlnekgsnLSGGEKQRISIARAILKDAPIIILD 495
Cdd:PRK13539 85 KPalTVAENLEFwAAFLGGEELDIAAA--LEAVGLapLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 613101153 496 EATSSIDPENEQLIQTAINE-LSKGKTVITIAHKLETIKNADQI 538
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAhLAQGGIVIAATHIPLGLPGAREL 196
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
19-298 |
6.61e-10 |
|
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: 60.52 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 19 MILGFSMSFLNAIF-IALPIFlAAKIFNNVLSHKPIYmkdiLNVVIIMVLLVIGRFITA---YFKSKSHESIAYEMsake 94
Cdd:cd18551 1 LILALLLSLLGTAAsLAQPLL-VKNLIDALSAGGSSG----GLLALLVALFLLQAVLSAlssYLLGRTGERVVLDL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 95 RLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSLLACIGVLLSFF 174
Cdd:cd18551 72 RRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 175 AIQLLerkSRQNAPAYHNVQNQLVE---KVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRIN---TKIEMQYIPFNLL 248
Cdd:cd18551 152 IILPL---GRRIRKASKRAQDALGElsaALERALSAIRTVKASNAEERETKRGGEAAERLYRAGlkaAKIEALIGPLMGL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 249 hllslkvvSIMIVLVACLLY-----MNHSIDLPTLIMISIFSFVIFDSVENINSA 298
Cdd:cd18551 229 --------AVQLALLVVLGVggarvASGALTVGTLVAFLLYLFQLITPLSQLSSF 275
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
363-551 |
6.78e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.34 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 363 TAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIkDMTLSTLMSKISAVFQKVYLFND-TIENNILFGN--PGATKEE 439
Cdd:TIGR01257 959 TAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFYAqlKGRSWEE 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 440 IiRAAKQACCHDfimslpEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKG 519
Cdd:TIGR01257 1038 A-QLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
170 180 190
....*....|....*....|....*....|...
gi 613101153 520 KTVITIAHKL-ETIKNADQIIVLNEGEIIQKGS 551
Cdd:TIGR01257 1111 RTIIMSTHHMdEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
324-550 |
1.13e-09 |
|
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: 58.70 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 324 NGKNLTIKNENIAFQNVNfsYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIridgvdikdmtl 403
Cdd:cd03220 14 KGGSSSLKKLGILGRKGE--VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 404 sTLMSKISAVFQKVYLFND--TIENNILFGNP--GATKEEIirAAKQACCHDFimSLPEGYqtmLNEKGSNLSGGEKQRI 479
Cdd:cd03220 80 -TVRGRVSSLLGLGGGFNPelTGRENIYLNGRllGLSRKEI--DEKIDEIIEF--SELGDF---IDLPVKTYSSGMKARL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613101153 480 SIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKG 550
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELlKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
338-550 |
1.15e-09 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 59.20 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYdiddgiiridgvdikdmtlSTLMSKISAVFQKV 417
Cdd:TIGR01978 4 KDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHP-------------------SYEVTSGTILFKGQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 418 YLFN---DTIENNILFGN-------PGATKEEIIRAAKQAC---CHDFIMSLPEgYQTMLNEKGSNL------------- 471
Cdd:TIGR01978 65 DLLElepDERARAGLFLAfqypeeiPGVSNLEFLRSALNARrsaRGEEPLDLLD-FEKLLKEKLALLdmdeeflnrsvne 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 472 --SGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETIK--NADQIIVLNEGEI 546
Cdd:TIGR01978 144 gfSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrEPDRSFLIITHYQRLLNyiKPDYVHVLLDGRI 223
|
....
gi 613101153 547 IQKG 550
Cdd:TIGR01978 224 VKSG 227
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
343-539 |
1.35e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 57.37 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 343 SYDDKQVIknvnfEIPTQTSTAIIGPSGSGKSTLchlllrfydiddgiiridgvdIKDMTLSTLMskisavfqkvylfnd 422
Cdd:cd03227 9 SYFVPNDV-----TFGEGSLTIITGPNGSGKSTI---------------------LDAIGLALGG--------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 423 tieNNILFGNPGATKEEIIRAAKQACchdFIMSLPEgyqtmlnekgsnLSGGEKQRISIARAI----LKDAPIIILDEAT 498
Cdd:cd03227 48 ---AQSATRRRSGVKAGCIVAAVSAE---LIFTRLQ------------LSGGEKELSALALILalasLKPRPLYILDEID 109
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 613101153 499 SSIDPENEQLIQTAINELSKGK-TVITIAHKLETIKNADQII 539
Cdd:cd03227 110 RGLDPRDGQALAEAILEHLVKGaQVIVITHLPELAELADKLI 151
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
19-237 |
1.37e-09 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 59.34 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 19 MILGFSMSFLNAIF-IALPIFLAA---KIFNNVLSHKPIYMKDILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMSAKE 94
Cdd:cd18547 1 LILVIILAIISTLLsVLGPYLLGKaidLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 95 RLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSLLACIGVLLSFF 174
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 175 AIQLLERKSRqnaPAYHNVQNQL------VEkvlEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTK 237
Cdd:cd18547 161 VTKFIAKRSQ---KYFRKQQKALgelngyIE---EMISGQKVVKAFNREEEAIEEFDEINEELYKASFK 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
328-559 |
2.22e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 328 LTIKNENIAFQNVNfsyDDKQVIKNVNFEIPTQTSTAIIGPSGSGKS----TLCHLL-----------LRFYDIDDgiir 392
Cdd:PRK15134 6 LAIENLSVAFRQQQ---TVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypsgdIRFHGESL---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 393 idgVDIKDMTLSTLM-SKISAVFQK--VYLfN--DTIENN---ILFGNPGATKE----EI--------IRAAKQacchdf 452
Cdd:PRK15134 79 ---LHASEQTLRGVRgNKIAMIFQEpmVSL-NplHTLEKQlyeVLSLHRGMRREaargEIlncldrvgIRQAAK------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 453 imslpegyqtMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLE 530
Cdd:PRK15134 149 ----------RLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLS 218
|
250 260 270
....*....|....*....|....*....|
gi 613101153 531 TIKN-ADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK15134 219 IVRKlADRVAVMQNGRCVEQNRAATLFSAP 248
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
348-559 |
2.56e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 58.26 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 348 QVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLlrfydIDDGIIRIDGVDIKDMTL-----STLMSKISAVFQ------- 415
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKML-----AGMIEPTSGELLIDDHPLhfgdySYRSQRIRMIFQdpstsln 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 416 ---KVYLFNDT--IENNILfgNPGATKEEIIRAAKQacchdfIMSLPEG---YQTMLnekgsnlSGGEKQRISIARAILK 487
Cdd:PRK15112 102 prqRISQILDFplRLNTDL--EPEQREKQIIETLRQ------VGLLPDHasyYPHML-------APGQKQRLGLARALIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 488 DAPIIILDEATSSIDPE-NEQLIQTAInEL--SKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK15112 167 RPKVIIADEALASLDMSmRSQLINLML-ELqeKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
463-529 |
2.68e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 2.68e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 463 MLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKL 529
Cdd:PRK13409 205 ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
364-550 |
2.92e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.89 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 364 AIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKdmTLSTLMSKISAVFQKVYLF-NDTIENNILFGN----PGA-TK 437
Cdd:PLN03211 98 AVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRK--PTKQILKRTGFVTQDDILYpHLTVRETLVFCSllrlPKSlTK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 438 EEIIRAAKQACCHdfiMSLPEGYQTML-NEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENE-QLIQTAINE 515
Cdd:PLN03211 176 QEKILVAESVISE---LGLTKCENTIIgNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLGSL 252
|
170 180 190
....*....|....*....|....*....|....*..
gi 613101153 516 LSKGKTVITIAHKLET--IKNADQIIVLNEGEIIQKG 550
Cdd:PLN03211 253 AQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFG 289
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
469-547 |
4.35e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.88 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 469 SNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKL-ETIKNADQIIVLNEGEI 546
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaAEGKAVIVISSELpELLGLSDRILVMREGRI 472
|
.
gi 613101153 547 I 547
Cdd:COG1129 473 V 473
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
344-530 |
6.10e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 57.02 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 344 YDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTlstlmSKISAVFQKVYLFN-D 422
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQNEGLLPwR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 423 TIENNILFG--NPGATKEEIIRAAKQacchdfimslpegyqtMLNEKGS---------NLSGGEKQRISIARAILKDAPI 491
Cdd:PRK11248 86 NVQDNVAFGlqLAGVEKMQRLEIAHQ----------------MLKKVGLegaekryiwQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 613101153 492 IILDEATSSIDPENEQLIQTAINEL--SKGKTVITIAHKLE 530
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITHDIE 190
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
332-547 |
6.50e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.02 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 332 NENIAFQNVNFSYDDKQVIknvnfeiptqtstAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKIS 411
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFV-------------TVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKVYL---FNDTIENNIL--------FG-NPGATKEEIIRAAKQacchdfIMSLPEGYQTMLNEKGSNLSGGEKQRI 479
Cdd:COG1101 84 RVFQDPMMgtaPSMTIEENLAlayrrgkrRGlRRGLTKKRRELFREL------LATLGLGLENRLDTKVGLLSGGQRQAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 480 SIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGK--TVITIAHKLE-TIKNADQIIVLNEGEII 547
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
330-556 |
9.42e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.43 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 330 IKNENIAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSK 409
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 410 -ISAVFQKVYLFND-TIENNILFGNPGATKEEIIRAAKQAccHDFimsLPEGYQTMLNEKGSnLSGGEKQRISIARAILK 487
Cdd:PRK11614 81 aVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWV--YEL---FPRLHERRIQRAGT-MSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 488 DAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKL-ETIKNADQIIVLNEGEIIQKGSHDELI 556
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLrEQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
464-559 |
1.04e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 58.10 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 464 LNEKGSNLSGGEKQRISIARAI---LKDApIIILDEATSSIDP-ENEQLIQTAINELSKGKTVITIAHKLETIKNADQII 539
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIgsgLTGV-LYVLDEPSIGLHQrDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
|
90 100
....*....|....*....|....*.
gi 613101153 540 VLNE------GEIIQKGSHDELIRKP 559
Cdd:TIGR00630 561 DIGPgagehgGEVVASGTPEEILANP 586
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
19-292 |
1.32e-08 |
|
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: 56.11 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 19 MILGFSMSFLN-AIFIALPIFLAaKIFNNVLSHKPIYMKDILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMSAKERLD 97
Cdd:pfam00664 1 LILAILLAILSgAISPAFPLVLG-RILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 98 IGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSLLACIGVLLSFFAIQ 177
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 178 LLERKSRQNAPAYHNVQNQLVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRIN-TKIEMQYIPFNLLHLLSLkVV 256
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGiKKAVANGLSFGITQFIGY-LS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 613101153 257 SIMIVLVACLLYMNHSIDLPTLIMISIFSFVIFDSV 292
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
472-559 |
1.33e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.64 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 472 SGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEIIQ 548
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVE 242
|
90
....*....|.
gi 613101153 549 KGSHDELIRKP 559
Cdd:PRK15079 243 LGTYDEVYHNP 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
323-557 |
1.57e-08 |
|
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: 57.12 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 323 ENGKNLTIKNENIAFQNVNFSY--DDKQVIK---NVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVD 397
Cdd:TIGR03269 268 EKECEVEVGEPIIKVRNVSKRYisVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGD 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 398 -IKDMTLSTLMSK------ISAVFQKVYLF--NDTIEN-----NILFGNPGATKEEIIrAAKQACCHDfimslpEGYQTM 463
Cdd:TIGR03269 348 eWVDMTKPGPDGRgrakryIGILHQEYDLYphRTVLDNlteaiGLELPDELARMKAVI-TLKMVGFDE------EKAEEI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 464 LNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKN-ADQIIV 540
Cdd:TIGR03269 421 LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAAL 500
|
250
....*....|....*..
gi 613101153 541 LNEGEIIQKGSHDELIR 557
Cdd:TIGR03269 501 MRDGKIVKIGDPEEIVE 517
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
338-547 |
1.72e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.14 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFY-------DIDDGIIRIDGVDIKDmtlsTLMSKI 410
Cdd:TIGR02633 5 KGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgEIYWSGSPLKASNIRD----TERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 411 SAVFQKVYLFND-TIENNILFGN----PGATKE--EIIRAAKQACCHDFIMSLPEGYQTMlnekgsNLSGGEKQRISIAR 483
Cdd:TIGR02633 81 VIIHQELTLVPElSVAENIFLGNeitlPGGRMAynAMYLRAKNLLRELQLDADNVTRPVG------DYGGGQQQLVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 484 AILKDAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETIKN-ADQIIVLNEGEII 547
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLkAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
330-533 |
1.80e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.45 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 330 IKNEN-IAFQNVNFSYDDKQV-IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRidgVDIKD------- 400
Cdd:TIGR00954 446 EYQDNgIKFENIPLVTPNGDVlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT---KPAKGklfyvpq 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 401 ---MTLSTLMSKIsavfqkvyLFNDTIENNILFGNPGATKEEIIRAAKQacchDFIMSLPEGYQTMLNEKgSNLSGGEKQ 477
Cdd:TIGR00954 523 rpyMTLGTLRDQI--------IYPDSSEDMKRRGLSDKDLEQILDNVQL----THILEREGGWSAVQDWM-DVLSGGEKQ 589
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 613101153 478 RISIARAILKDAPIIILDEATSSIDPENEQLIQTAINElsKGKTVITIAHKLETIK 533
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWK 643
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
365-545 |
3.02e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 54.72 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 365 IIGPSGSGKSTLCHLLlrfydIDDGIIRIDGVDIKDMTLSTLMSKISAVFQ-KVYLFNDTIENNilFGNPGATKEEIIRa 443
Cdd:cd03237 30 ILGPNGIGKTTFIKML-----AGVLKPDEGDIEIELDTVSYKPQYIKADYEgTVRDLLSSITKD--FYTHPYFKTEIAK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 444 akqacchdfimslPEGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINE--LSKGKT 521
Cdd:cd03237 102 -------------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRfaENNEKT 168
|
170 180
....*....|....*....|....*
gi 613101153 522 VITIAHKLETIKN-ADQIIVLnEGE 545
Cdd:cd03237 169 AFVVEHDIIMIDYlADRLIVF-EGE 192
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
343-570 |
4.14e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.32 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 343 SYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRfydiddgiiridgVD-------IKDMTLSTLMSkISAVFQ 415
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG-------------ILeptsgrvEVNGRVSALLE-LGAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 416 kvylfND-TIENNILFGnpGA----TKEEIIRAAKQ----ACCHDFImslpegyqtmlNEKGSNLSGGEKQRISIARAIL 486
Cdd:COG1134 101 -----PElTGRENIYLN--GRllglSRKEIDEKFDEivefAELGDFI-----------DQPVKTYSSGMRARLAFAVATA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 487 KDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKpgmYQD 564
Cdd:COG1134 163 VDPDILLVDEVLAVGDAAFQKKCLARIRELREsGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA---YEA 239
|
....*.
gi 613101153 565 FIRIKS 570
Cdd:COG1134 240 LLAGRE 245
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
471-562 |
4.42e-08 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 56.23 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 471 LSGGEKQRISIARAILKDA---PIIILDEATSSIDPEN-EQLIQTaINEL-SKGKTVITIAHKLETIKNADQIIVL---- 541
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDiRKLLEV-LHRLvDKGNTVVVIEHNLDVIKTADWIIDLgpeg 909
|
90 100
....*....|....*....|...
gi 613101153 542 --NEGEIIQKGSHDELIRKPGMY 562
Cdd:PRK00349 910 gdGGGEIVATGTPEEVAKVEASY 932
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
338-530 |
4.49e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 54.48 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYD----DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiddgiiriDGVDIKDMTLS-TLMSKISA 412
Cdd:COG4525 7 RHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGF----------LAPSSGEITLDgVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 ----VFQKVYLFN--DTIENnILF-----GNPGATKEEIIRAAKQacchdfIMSLPEGYQTMLNEkgsnLSGGEKQRISI 481
Cdd:COG4525 77 drgvVFQKDALLPwlNVLDN-VAFglrlrGVPKAERRARAEELLA------LVGLADFARRRIWQ----LSGGMRQRVGI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 613101153 482 ARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLE 530
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITHSVE 196
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
458-547 |
5.22e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 458 EGYQTMLNEKGS-------NLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKL 529
Cdd:NF040905 385 EEYRKKMNIKTPsvfqkvgNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAeGKGVIVISSEL 464
|
90
....*....|....*....
gi 613101153 530 -ETIKNADQIIVLNEGEII 547
Cdd:NF040905 465 pELLGMCDRIYVMNEGRIT 483
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-280 |
5.24e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 54.82 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 19 MILGFSMSFLNAIFIALPIFLAAKIFNNVLSHKPI--YMKDILNVVIIMVLLVIGR----FITAYFKSKSHESIAYEMsa 92
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPggNTSLLLLLVLGLAGAYVLSallgILRGRLLARLGERITADL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 93 keRLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENF-AMKMVDVVVNGyILIIVLILSLLVVSWQVSLLACIGVLL 171
Cdd:cd18563 79 --RRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFlSDGLPDFLTNI-LMIIGIGVVLFSLNWKLALLVLIPVPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 172 SFFAIQLLERKSRqnaPAYH-------NVQNQLVEkvleVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTKIEMQYIP 244
Cdd:cd18563 156 VVWGSYFFWKKIR---RLFHrqwrrwsRLNSVLND----TLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWAT 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 613101153 245 FN-LLHLLsLKVVSIMIVLVACLLYMNHSIDLPTLIM 280
Cdd:cd18563 229 FFpLLTFL-TSLGTLIVWYFGGRQVLSGTMTLGTLVA 264
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
350-544 |
5.24e-08 |
|
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: 54.01 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 350 IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiddGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLFN-DTIENNI 428
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL-----AQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 429 LFG----NPGATKEEiiraaKQACCHDFIMSLpeGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDE---ATSSI 501
Cdd:TIGR01184 76 ALAvdrvLPDLSKSE-----RRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEpfgALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 613101153 502 DPEN--EQLIQTAiNElsKGKTVITIAHKL-ETIKNADQIIVLNEG 544
Cdd:TIGR01184 149 TRGNlqEELMQIW-EE--HRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
463-529 |
6.33e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 6.33e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 463 MLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPenEQLIQTA--INELSK-GKTVITIAHKL 529
Cdd:COG1245 205 ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRLNVArlIRELAEeGKYVLVVEHDL 272
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
337-498 |
9.51e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 54.69 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 337 FQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRfydidDGIIRIDGVDI-KDMTLSTLMskisavfQ 415
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG-----ELEPDSGEVSIpKGLRIGYLP-------Q 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 416 KVYLFND-TIENNILFGNPG-----ATKEEIIRA--------AKQACCHDFIMSLpEGY----------------QTMLN 465
Cdd:COG0488 69 EPPLDDDlTVLDTVLDGDAElraleAELEELEAKlaepdedlERLAELQEEFEAL-GGWeaearaeeilsglgfpEEDLD 147
|
170 180 190
....*....|....*....|....*....|...
gi 613101153 466 EKGSNLSGGEKQRISIARAILKDAPIIILDEAT 498
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
339-547 |
1.06e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 339 NVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDID--DGIIRIDGVDIKDmTLSTLMSKISAVFQK 416
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDsgSILFQGKEIDFKS-SKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 VYLFND-TIENNILFGNPgATKEEIIRAAKQAccHDFIMSLPE-GYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIIL 494
Cdd:PRK10982 82 LNLVLQrSVMDNMWLGRY-PTKGMFVDQDKMY--RDTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 495 DEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETI-KNADQIIVLNEGEII 547
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLkERGCGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
335-534 |
1.25e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAF--QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLrfydiddgiiridgvdikdmtlstlmSKISA 412
Cdd:PRK11147 318 IVFemENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLML--------------------------GQLQA 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 413 VFQKVYL--------FND---------TIENNILFGnpgatKEEIIRAAKQAccH------DFIMSlPEgyQTMLNEKGs 469
Cdd:PRK11147 372 DSGRIHCgtklevayFDQhraeldpekTVMDNLAEG-----KQEVMVNGRPR--HvlgylqDFLFH-PK--RAMTPVKA- 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 470 nLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELsKGkTVITIAHKLETIKN 534
Cdd:PRK11147 441 -LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSY-QG-TVLLVSHDRQFVDN 502
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
19-279 |
1.31e-07 |
|
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: 53.20 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 19 MILGFSMSFLNAIFIALPIFLAAKIFNNVLSHKPiyMKDILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMSAKERLDI 98
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGL--RELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 99 GDKLKNVRLGYFNSHHSNELTTIVTTDL----TFLENFAMKMVDVVVngyiLIIVLILSLLVVSWQVSLLACIGVLLSFF 174
Cdd:cd18542 79 YDHLQRLSFSFHDKARTGDLMSRCTSDVdtirRFLAFGLVELVRAVL----LFIGALIIMFSINWKLTLISLAIIPFIAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 175 AIQLLERKSRqnaPAYHNVQNQLVE---KVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRIN---TKIEMQYIPfnLL 248
Cdd:cd18542 155 FSYVFFKKVR---PAFEEIREQEGElntVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNiklAKLLAKYWP--LM 229
|
250 260 270
....*....|....*....|....*....|.
gi 613101153 249 HLLSLkVVSIMIVLVACLLYMNHSIDLPTLI 279
Cdd:cd18542 230 DFLSG-LQIVLVLWVGGYLVINGEITLGELV 259
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
362-532 |
1.34e-07 |
|
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: 51.22 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 362 STAIIGPSGSGKSTLCHLLLRFYDIDdgiiridgvdikdmtlstlmskisavfqkvylfndtiENNILFGNPGATKEEII 441
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPP-------------------------------------GGGVIYIDGEDILEEVL 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 442 RAAKQacchdfimslpegyqTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQ-------TAIN 514
Cdd:smart00382 47 DQLLL---------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlLLLL 111
|
170
....*....|....*...
gi 613101153 515 ELSKGKTVITIAHKLETI 532
Cdd:smart00382 112 KSEKNLTVILTTNDEKDL 129
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
470-545 |
1.76e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.42 E-value: 1.76e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 470 NLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKNADQIIVLNEGE 545
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
335-527 |
1.99e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.79 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLrfydiddgiiRIDGVDIKDMTL-STLmsKISAV 413
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMIT----------GQEQPDSGTIEIgETV--KLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 414 FQkvylFNDTIENN------ILFGNpgatkeEIIRAAKQAcchdfIMSlpEGYQTMLNEKGS-------NLSGGEKQRIS 480
Cdd:TIGR03719 391 DQ----SRDALDPNktvweeISGGL------DIIKLGKRE-----IPS--RAYVGRFNFKGSdqqkkvgQLSGGERNRVH 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 613101153 481 IARAILKDAPIIILDEATSSIDPENEQLIQTAINELSkGKTVItIAH 527
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA-GCAVV-ISH 498
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
467-559 |
2.86e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 51.95 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 467 KGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTV-ITIAHKLETIKNADQIIVLNEG 544
Cdd:COG1137 133 KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLkERGIGVlITDHNVRETLGICDRAYIISEG 212
|
90
....*....|....*
gi 613101153 545 EIIQKGSHDELIRKP 559
Cdd:COG1137 213 KVLAEGTPEEILNNP 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
353-559 |
2.91e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 52.66 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 353 VNFEIPTQTSTAIIGPSGSGKSTLCHLLL--------RFYDIDDGIIRIDGVDIKDmtlstLMSKISAVFQKVY--Lfnd 422
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTmietptggELYYQGQDLLKADPEAQKL-----LRQKIQIVFQNPYgsL--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 423 tiennilfgNP----GATKEE--II-----RAAKQACCHDfIMSL----PEGYQT---MLnekgsnlSGGEKQRISIARA 484
Cdd:PRK11308 106 ---------NPrkkvGQILEEplLIntslsAAERREKALA-MMAKvglrPEHYDRyphMF-------SGGQRQRIAIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 485 ILKDAPIIILDEATSSIDPEneqlIQTAINEL------SKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIR 557
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVS----VQAQVLNLmmdlqqELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFN 244
|
..
gi 613101153 558 KP 559
Cdd:PRK11308 245 NP 246
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
335-552 |
2.97e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLrfyDIDDGIIRIDGVDIKDMTLSTLMSKISAVF 414
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLA---GREDYEVTGGTVEFKGKDLLELSPEDRAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 415 QKVYLFNDTIEnnilfgNPGATKEEIIRAAKQAC-------------CHDFI------MSLPEGYQTMLNEKGsnLSGGE 475
Cdd:PRK09580 79 GIFMAFQYPVE------IPGVSNQFFLQTALNAVrsyrgqepldrfdFQDLMeekialLKMPEDLLTRSVNVG--FSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 476 KQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSKGK-TVITIAHK---LETIKnADQIIVLNEGEIIQKGS 551
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKrSFIIVTHYqriLDYIK-PDYVHVLYQGRIVKSGD 229
|
.
gi 613101153 552 H 552
Cdd:PRK09580 230 F 230
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
471-562 |
3.35e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 53.49 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 471 LSGGEKQRISIARAILKDAP---IIILDEATSSIDPEN-EQLIQtAINEL-SKGKTVITIAHKLETIKNADQIIVL---- 541
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDiRKLLE-VLHRLvDKGNTVVVIEHNLDVIKTADWIIDLgpeg 905
|
90 100
....*....|....*....|...
gi 613101153 542 --NEGEIIQKGSHDELIRKPGMY 562
Cdd:COG0178 906 gdGGGEIVAEGTPEEVAKVKASY 928
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
346-560 |
3.98e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.62 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 346 DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFY---------DIDDGIIRIDGVDIKDMTLSTLMSKISAVFQK 416
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvrqtagRVLLDGKPVAPCALRGRKIATIMQNPRSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 VYLFND-TIENNILFGNPGAtkeeiiRAAKQACCHDfiMSLPEGyQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILD 495
Cdd:PRK10418 95 LHTMHThARETCLALGKPAD------DATLTAALEA--VGLENA-ARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613101153 496 EATSSIDpeneQLIQTAINEL------SKGKTVITIAHKLETI-KNADQIIVLNEGEIIQKGSHDELIRKPG 560
Cdd:PRK10418 166 EPTTDLD----VVAQARILDLlesivqKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
459-559 |
4.80e-07 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 52.72 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 459 GYQTmLNEKGSNLSGGEKQRISIARAI---LKDApIIILDEatSSI-----DpeNEQLIQTaINEL-SKGKTVITIAHKL 529
Cdd:COG0178 475 DYLT-LDRSAGTLSGGEAQRIRLATQIgsgLVGV-LYVLDE--PSIglhqrD--NDRLIET-LKRLrDLGNTVIVVEHDE 547
|
90 100 110
....*....|....*....|....*....|....*.
gi 613101153 530 ETIKNADQIIVL------NEGEIIQKGSHDELIRKP 559
Cdd:COG0178 548 DTIRAADYIIDIgpgageHGGEVVAQGTPEEILKNP 583
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
339-536 |
5.65e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 339 NVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKdmtlstlmsKISAVFQKVY 418
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK---------KDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 419 LF---------NDTIENNILF------GNPGATkeEIIRAAKQACCHDFIMSLpegyqtmlnekgsnLSGGEKQRISIAR 483
Cdd:PRK13540 77 CFvghrsginpYLTLRENCLYdihfspGAVGIT--ELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 613101153 484 AILKDAPIIILDEATSSIDPENEQLIQTAINE-LSKGKTVITIAHKLETIKNAD 536
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALDELSLLTIITKIQEhRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
437-545 |
5.69e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 437 KEEIIRAakqacchdfiMSLPEGYQTMLNEkgsnLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL 516
Cdd:PRK13409 434 KSEIIKP----------LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499
|
90 100 110
....*....|....*....|....*....|..
gi 613101153 517 --SKGKTVITIAHKLETIKN-ADQIIVLnEGE 545
Cdd:PRK13409 500 aeEREATALVVDHDIYMIDYiSDRLMVF-EGE 530
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
328-559 |
6.50e-07 |
|
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: 51.99 E-value: 6.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 328 LTIKNENIAFQNvnfSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGII----RIDGVDIKDMTL 403
Cdd:COG4172 7 LSVEDLSVAFGQ---GGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPsgsiLFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 404 STLM----SKISAVFQK-------VYlfndTIENNIlfgnpgatkEEIIR--------AAKQAcchdfIMSL-------- 456
Cdd:COG4172 84 RELRrirgNRIAMIFQEpmtslnpLH----TIGKQI---------AEVLRlhrglsgaAARAR-----ALELlervgipd 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 457 PEgyqTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPeneqLIQTAINELSK------GKTVITIAHKLE 530
Cdd:COG4172 146 PE---RRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQAQILDLLKdlqrelGMALLLITHDLG 218
|
250 260 270
....*....|....*....|....*....|
gi 613101153 531 TIKN-ADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:COG4172 219 VVRRfADRVAVMRQGEIVEQGPTAELFAAP 248
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
313-537 |
8.84e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 313 EKIKNA--PELDENGKNLTI-KNEN-IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLL----RFY 384
Cdd:PRK10938 235 EQLEGVqlPEPDEPSARHALpANEPrIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGY 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 385 DiddgiiridgvdiKDMTL--------STL------MSKISAVFQKVYLFNDTIENNIL---FGNPGatkeeIIRAAKqa 447
Cdd:PRK10938 315 S-------------NDLTLfgrrrgsgETIwdikkhIGYVSSSLHLDYRVSTSVRNVILsgfFDSIG-----IYQAVS-- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 448 cchDFIMSLPEGYQTMLNEKGS-------NLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL-SKG 519
Cdd:PRK10938 375 ---DRQQKLAQQWLDILGIDKRtadapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiSEG 451
|
250 260 270
....*....|....*....|....*....|
gi 613101153 520 KTVI------------TIAHKLETIKNADQ 537
Cdd:PRK10938 452 ETQLlfvshhaedapaCITHRLEFVPDGDI 481
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
471-559 |
9.18e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.90 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 471 LSGGEKQRISIARAILKDAPIIILDEATSSIDPEneqlIQTAINEL------SKGKTVITIAHKLETI-KNADQIIVLNE 543
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVT----IQAQIIELllelqqKENMALVLITHDLALVaEAAHKIIVMYA 229
|
90
....*....|....*.
gi 613101153 544 GEIIQKGSHDELIRKP 559
Cdd:PRK11022 230 GQVVETGKAHDIFRAP 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
469-546 |
1.17e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 469 SNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKL-ETIKNADQIIVLNEGEI 546
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQqGVAIIVISSELpEVLGLSDRVLVMHEGKL 483
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
58-239 |
1.35e-06 |
|
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: 50.23 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 58 ILNVVIIMVLLVIGR----FITAYFKSKSHESIAYEMsakeRLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFA 133
Cdd:cd18778 39 LLGLALLLLGAYLLRallnFLRIYLNHVAEQKVVADL----RSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 134 MKMVDVVVNGYILIIVLILSLLVVSWQVSLLACIGVLLSFFAIQLLERKSRqnaPAYHNVQNQLVE---KVLEVIRGIQV 210
Cdd:cd18778 115 ADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVR---PRYRKVREALGElnaLLQDNLSGIRE 191
|
170 180
....*....|....*....|....*....
gi 613101153 211 IKSFAKENTslksfnqsvnESKRINTKIE 239
Cdd:cd18778 192 IQAFGREEE----------EAKRFEALSR 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
350-559 |
1.37e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 350 IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMTLSTLMS---KISAVFQKVYLFND---T 423
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrDIQFIFQDPYASLDprqT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 424 IENNILfgnpgatkeEIIR----------AAKQACCHDFIMSLPEGYQTMLNEkgsnLSGGEKQRISIARAILKDAPIII 493
Cdd:PRK10261 420 VGDSIM---------EPLRvhgllpgkaaAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 494 LDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKP 559
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
463-545 |
1.38e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 463 MLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL--SKGKTVITIAHKLETIKN-ADQII 539
Cdd:COG1245 448 LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaeNRGKTAMVVDHDIYLIDYiSDRLM 527
|
....*.
gi 613101153 540 VLnEGE 545
Cdd:COG1245 528 VF-EGE 532
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
344-550 |
1.72e-06 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 49.25 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 344 YDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLlrfydidDGIIRIDGVDIKDMTL------STLMSKISAVF-QK 416
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKIL-------SGLLQPTSGEVRVAGLvpwkrrKKFLRRIGVVFgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 VYLFNDTiennilfgnPGATKEEIIRAakqacchdfIMSLPEG-YQT-------------MLNEKGSNLSGGEKQRISIA 482
Cdd:cd03267 104 TQLWWDL---------PVIDSFYLLAA---------IYDLPPArFKKrldelselldleeLLDTPVRQLSLGQRMRAEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 483 RAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETI-KNADQIIVLNEGEIIQKG 550
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRerGTTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
471-559 |
1.83e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 50.84 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 471 LSGGEKQRISIARAI-------LkdapiIILDEAtsSI-----DpeNEQLIQTAINELSKGKTVITIAHKLETIKNADQI 538
Cdd:PRK00349 490 LSGGEAQRIRLATQIgsgltgvL-----YVLDEP--SIglhqrD--NDRLIETLKHLRDLGNTLIVVEHDEDTIRAADYI 560
|
90 100
....*....|....*....|....*..
gi 613101153 539 IVL------NEGEIIQKGSHDELIRKP 559
Cdd:PRK00349 561 VDIgpgagvHGGEVVASGTPEEIMKNP 587
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
470-554 |
2.00e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 470 NLSGGEKQRISIARAILKDAPIIILDEATSSID--PENEqlIQTAINELSK-GKTVITIAHKL-ETIKNADQIIVLNEGE 545
Cdd:PRK11288 396 NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDvgAKHE--IYNVIYELAAqGVAVLFVSSDLpEVLGVADRIVVMREGR 473
|
....*....
gi 613101153 546 IIQKGSHDE 554
Cdd:PRK11288 474 IAGELAREQ 482
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
471-559 |
3.10e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 471 LSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETI-KNADQIIVLNEGEII 547
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQTV 238
|
90
....*....|..
gi 613101153 548 QKGSHDELIRKP 559
Cdd:PRK15093 239 ETAPSKELVTTP 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
472-559 |
3.33e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.34 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 472 SGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK--GKTVITIAHKLETIKN-ADQIIVLNEGEIIQ 548
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTME 242
|
90
....*....|.
gi 613101153 549 KGSHDELIRKP 559
Cdd:PRK09473 243 YGNARDVFYQP 253
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
9-237 |
3.37e-06 |
|
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: 49.37 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 9 LNWMRPYKARMILGFSMSFLNAIfiALPIF--LAAKIFNNVLSHKPIYMKDILNVVIIMVLLV-IGRFITAYFKSkshes 85
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGA--VFPVFaiLFSKLISVFSLPDDDELRSEANFWALMFLVLaIVAGIAYFLQG----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 86 IAYEMSAkERLdigdkLKNVRLGYFNS-------------HHSNELTTIVTTDLTFLEN----FAMKMVDVVVN------ 142
Cdd:cd18578 74 YLFGIAG-ERL-----TRRLRKLAFRAilrqdiawfddpeNSTGALTSRLSTDASDVRGlvgdRLGLILQAIVTlvagli 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 143 -----GyiliivlilsllvvsWQVSL--LACIGVLL--SFFAIQLLERKSRQNAPAYHNVQNQLVEkvleVIRGIQVIKS 213
Cdd:cd18578 148 iafvyG---------------WKLALvgLATVPLLLlaGYLRMRLLSGFEEKNKKAYEESSKIASE----AVSNIRTVAS 208
|
250 260
....*....|....*....|....
gi 613101153 214 FAKENTSLKSFNQSVNESKRINTK 237
Cdd:cd18578 209 LTLEDYFLEKYEEALEEPLKKGLR 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
469-547 |
3.75e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.62 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 469 SNLSGGEKQRISIARAILKDAPIIILDEATSSI-DPENEQLIQtAINEL-SKGKTVITIAHKLETI-KNADQIIVLNEGE 545
Cdd:PRK10762 140 GELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFR-VIRELkSQGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
..
gi 613101153 546 II 547
Cdd:PRK10762 219 FI 220
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
19-280 |
4.20e-06 |
|
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: 48.92 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 19 MILGFSMSFLNAIFIALPIFLAAKIFNNVLSHKPIYMKDILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMSAKERLDI 98
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 99 GDKLKNVRLGYFNSHHSNELTTIVTTD------------LTFLENFAMkMVDVVVngyiliivlilSLLVVSWQVSLLAC 166
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDtealnelftsglVTLIGDLLL-LIGILI-----------AMFLLNWRLALISL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 167 IGVLLSFFAIQLLERKSRqnaPAYHNVQNQLVE---KVLEVIRGIQVIKSFAKENTSLKSFNQsVNESKRINTKIEMQY- 242
Cdd:cd18544 149 LVLPLLLLATYLFRKKSR---KAYREVREKLSRlnaFLQESISGMSVIQLFNREKREFEEFDE-INQEYRKANLKSIKLf 224
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 613101153 243 -IPFNLLHLLSlkVVSIMIVL-VACLLYMNHSIDLPTLIM 280
Cdd:cd18544 225 aLFRPLVELLS--SLALALVLwYGGGQVLSGAVTLGVLYA 262
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
335-546 |
4.65e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVI-KNVNFEIPTQTSTAIIGPSGSGKSTLCHLLlrfydiddgiiridGVDIKDMTLSTLMS-KIS- 411
Cdd:PLN03073 509 ISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLI--------------SGELQPSSGTVFRSaKVRm 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 412 AVFQKVYLFN-DTIENNILFGN---PGATKEEIiraakQACCHDFIMSLPEGYQTMLnekgsNLSGGEKQRISIARAILK 487
Cdd:PLN03073 575 AVFSQHHVDGlDLSSNPLLYMMrcfPGVPEQKL-----RAHLGSFGVTGNLALQPMY-----TLSGGQKSRVAFAKITFK 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 488 DAPIIILDEATSSIDPEN-EQLIQTAIneLSKGKtVITIAHKLETIKNA-DQIIVLNEGEI 546
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAvEALIQGLV--LFQGG-VLMVSHDEHLISGSvDELWVVSEGKV 702
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
338-561 |
4.94e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLrfydiddGIIRIDGVDIK------------------ 399
Cdd:PRK15064 323 ENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-------GELEPDSGTVKwsenanigyyaqdhaydf 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 400 --DMTLSTLMSK----------ISAVFQKvylfndtiennILFGNpgatkEEIIRAAKqacchdfimslpegyqtmlnek 467
Cdd:PRK15064 396 enDLTLFDWMSQwrqegddeqaVRGTLGR-----------LLFSQ-----DDIKKSVK---------------------- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 468 gsNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAInELSKGkTVITIAHKLETIKN-ADQIIVLNEGEI 546
Cdd:PRK15064 438 --VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMAL-EKYEG-TLIFVSHDREFVSSlATRIIEITPDGV 513
|
250
....*....|....*.
gi 613101153 547 IQ-KGSHDELIRKPGM 561
Cdd:PRK15064 514 VDfSGTYEEYLRSQGI 529
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
463-529 |
6.17e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.13 E-value: 6.17e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 463 MLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKL 529
Cdd:cd03236 132 VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDL 199
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
335-544 |
7.95e-06 |
|
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: 46.85 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYD----DKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLlrfydiddgIIRIDGVDIK-DMTLSTLMSK 409
Cdd:cd03232 4 LTWKNLNYTVPvkggKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL---------AGRKTAGVITgEILINGRPLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 410 ISavFQKVYLFndtIENNILFgNPGATKEEIIRAAkqACCHDfimslpegyqtmlnekgsnLSGGEKQRISIARAILKDA 489
Cdd:cd03232 75 KN--FQRSTGY---VEQQDVH-SPNLTVREALRFS--ALLRG-------------------LSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 490 PIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHK--LETIKNADQIIVLNEG 544
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
469-558 |
7.97e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 469 SNLSGGEKQRISIARAIL---KDAPIIILDEATSSIDPEN-EQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNE- 543
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPe 887
|
90 100
....*....|....*....|
gi 613101153 544 -----GEIIQKGSHDELIRK 558
Cdd:PRK00635 888 ggnlgGYLLASCSPEELIHL 907
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
470-546 |
7.98e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.46 E-value: 7.98e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 470 NLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKL-ETIKNADQIIVLNEGEI 546
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMpEVLGMSDRILVMHEGRI 473
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
469-539 |
9.35e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.81 E-value: 9.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 469 SNLSGGEKQRISIA--RAIL--KDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQII 539
Cdd:pfam02463 1076 DLLSGGEKTLVALAliFAIQkyKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
471-546 |
1.00e-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: 48.28 E-value: 1.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 471 LSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELS-KGKTVITIAHKL-ETIKNADQIIVLNEGEI 546
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
18-279 |
1.15e-05 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 47.46 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 18 RMILGFSMSFLN-AIFIALPIFLAAKIFNNVLSHKpiyMKDILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMSAKERL 96
Cdd:cd18545 1 KLLLALLLMLLStAASLAGPYLIKIAIDEYIPNGD---LSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 97 DIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSLLACIGVLLSFFAI 176
Cdd:cd18545 78 DLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 177 QLLERKSRQNAPAYHNVQNQLVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTK-IEMQYIPFNLLHLLSLkV 255
Cdd:cd18545 158 FLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRaVRLNALFWPLVELISA-L 236
|
250 260
....*....|....*....|....
gi 613101153 256 VSIMIVLVACLLYMNHSIDLPTLI 279
Cdd:cd18545 237 GTALVYWYGGKLVLGGAITVGVLV 260
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
19-289 |
1.67e-05 |
|
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: 47.01 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 19 MILGFSMSFLNAIF-IALPiFLAAKIFNNVLSHKPiyMKDILNVVIIMVLL----VIGRFITAYFKSKSHESIAYEMsak 93
Cdd:cd18548 1 AILAPLFKLLEVLLeLLLP-TLMADIIDEGIANGD--LSYILRTGLLMLLLallgLIAGILAGYFAAKASQGFGRDL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 94 eRLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSLLACIGVLLSF 173
Cdd:cd18548 75 -RKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 174 FAIQLLERKSRqnaPAYHNVQNQ---LVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTKIEMQYIPFNLLHL 250
Cdd:cd18548 154 LVVFLIMKKAI---PLFKKVQKKldrLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMM 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 613101153 251 LSLKVVSIMIVLVACLLYMNHSIDLPTLI------MISIFSFVIF 289
Cdd:cd18548 231 LIMNLAIVAILWFGGHLINAGSLQVGDLVafinylMQILMSLMML 275
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
464-548 |
1.69e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.47 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 464 LNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELS-KGKTVITIAHKL-ETIKNADQIIVL 541
Cdd:PRK09700 403 VNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELpEIITVCDRIAVF 482
|
....*..
gi 613101153 542 NEGEIIQ 548
Cdd:PRK09700 483 CEGRLTQ 489
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
335-376 |
2.14e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 2.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTL 376
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTL 366
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
441-544 |
2.24e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 441 IRAAKQACCHDFIMSLPEGyQTMlnekgSNLSGGEKQRISIARAIL---KDAPIIILDEATSSIDPENEQLIQTAINEL- 516
Cdd:PRK00635 1676 IQKPLQALIDNGLGYLPLG-QNL-----SSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLv 1749
|
90 100
....*....|....*....|....*...
gi 613101153 517 SKGKTVITIAHKLETIKNADQIIVLNEG 544
Cdd:PRK00635 1750 SLGHSVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
474-548 |
2.48e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 2.48e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613101153 474 GEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKL-ETIKNADQIIVLNEGEIIQ 548
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELkAQGITSIIISHKLnEIRRVADSITVLRDGRTIE 219
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
324-376 |
2.62e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.37 E-value: 2.62e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 324 NGKNLTIKN--ENiafqnvNfsyddkqvIKNVNFEIPTQTSTAIIGPSGSGKSTL 376
Cdd:PRK00349 611 NGKFLKLKGarEN------N--------LKNVDVEIPLGKFTCVTGVSGSGKSTL 651
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
468-560 |
2.72e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.65 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 468 GSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETIKN-ADQIIVLNEGE 545
Cdd:NF000106 142 AAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQlAHELTVIDRGR 221
|
90
....*....|....*
gi 613101153 546 IIQKGSHDELIRKPG 560
Cdd:NF000106 222 VIADGKVDELKTKVG 236
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
347-547 |
2.81e-05 |
|
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: 45.33 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 347 KQVIKNVNFEIPTQTSTAIIGPSGSGKSTLchllLRFYDIDDGIIRIDGVDIKDMTLStlMSKISAVFQKVYLFNDtiEN 426
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTL----LKALANRTEGNVSVEGDIHYNGIP--YKEFAEKYPGEIIYVS--EE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 427 NILFgnPGATKEEIIRAAKQACCHDFImslpegyqtmlnekgSNLSGGEKQRISIARAILKDAPIIILDEAT----SSID 502
Cdd:cd03233 92 DVHF--PTLTVRETLDFALRCKGNEFV---------------RGISGGERKRVSIAEALVSRASVLCWDNSTrgldSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 613101153 503 PENEQLIQTAINELsKGKTVITIAHKLETIKNA-DQIIVLNEGEII 547
Cdd:cd03233 155 LEILKCIRTMADVL-KTTTFVSLYQASDEIYDLfDKVLVLYEGRQI 199
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
434-530 |
5.14e-05 |
|
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: 46.55 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 434 GATKEEIIRAAKQAcchdfIMSLpeGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLI-QTA 512
Cdd:TIGR01257 2041 GVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTI 2113
|
90
....*....|....*...
gi 613101153 513 INELSKGKTVITIAHKLE 530
Cdd:TIGR01257 2114 VSIIREGRAVVLTSHSME 2131
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
358-546 |
5.97e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.77 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 358 PTQTsTAIIGPSGSGKSTLCHLLLRFYDIDDGIIRIDGVDIKDMT---LSTLMSK-ISAVFQKVYLFN--DTIENNILfg 431
Cdd:PRK10584 35 RGET-IALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeeaRAKLRAKhVGFVFQSFMLIPtlNALENVEL-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 432 nPGATKEEIIRAAKQACChDFIMSLpeGYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQT 511
Cdd:PRK10584 112 -PALLRGESSRQSRNGAK-ALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 613101153 512 AINELSK--GKTVITIAHKLETIKNADQIIVLNEGEI 546
Cdd:PRK10584 188 LLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
107-308 |
6.44e-05 |
|
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: 45.02 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 107 LGYFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSLLACIGVLLSFFAIQLLERKSRQN 186
Cdd:cd18590 84 IGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 187 APAYHNVQNQLVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTKIEMQYIpfnlLHLLSLKVVSIMiVLVACL 266
Cdd:cd18590 164 SQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRA----VYLLVRRVLQLG-VQVLML 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 613101153 267 LYMNHSIDLPTLIMISIFSFVIF--DSVENINSAAHVLEmiDMT 308
Cdd:cd18590 239 YCGRQLIQSGHLTTGSLVSFILYqkNLGSYVRTLVYIYG--DML 280
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
19-237 |
8.10e-05 |
|
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: 44.77 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 19 MILGFSMSFLNAIFIALPIFLAAKIFNNVLSH------KPIYMKDILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMSA 92
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFgsgessPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 93 KERLDIgdkLKNV---RLGYFNSHHSNELTTIVTTDLTFLEN-FAMKMVDVV----------VNGYILIivlilsllvvs 158
Cdd:cd18577 81 RIRKRY---LKALlrqDIAWFDKNGAGELTSRLTSDTNLIQDgIGEKLGLLIqslstfiagfIIAFIYS----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 159 WQVSLLACIGVLLSFFAIQLLERKSRQnapaYHNVQNQLVEK----VLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRI 234
Cdd:cd18577 147 WKLTLVLLATLPLIAIVGGIMGKLLSK----YTKKEQEAYAKagsiAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKA 222
|
...
gi 613101153 235 NTK 237
Cdd:cd18577 223 GIK 225
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
324-378 |
8.29e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.79 E-value: 8.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 324 NGKNLTIKNeniAFQNvNfsyddkqvIKNVNFEIPTQTSTAIIGPSGSGKSTLCH 378
Cdd:COG0178 607 NGKFLTIKG---AREN-N--------LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-217 |
8.43e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 44.86 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 19 MILGFSMSFLNAIFIALPIFLAAKIFNNVLSHKPIYMKDILN-------------VVIIMVLLVIGRFITAYFKSKSHES 85
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFLPLVPAslgpadprgqlwlLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 86 IAYEMSAKERLDIGDKLKNVRLGYFNSHHSNELTTIVTTDL----TFLENFAMKMVDVVVNgyilIIVLILSLLVVSWQV 161
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVnqleRFLDDGANSIIRVVVT----VLGIGAILFYLNWQL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613101153 162 SLLAcigvLLSFFAIQLLERK-SRQNAPAYHNVQnqlvEKV------LE-VIRGIQVIKSFAKE 217
Cdd:cd18565 157 ALVA----LLPVPLIIAGTYWfQRRIEPRYRAVR----EAVgdlnarLEnNLSGIAVIKAFTAE 212
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
472-554 |
1.16e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 472 SGGEKQRISIARAILKDAPIIILDEATSSIDP----ENEQLIQTAINELSKGKTVITIAHKLETIKNADQIIVLNEGEII 547
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSatalEFIRALKTSANILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQI 290
|
....*..
gi 613101153 548 QKGSHDE 554
Cdd:TIGR00956 291 YFGPADK 297
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
328-545 |
1.27e-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: 43.41 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 328 LTIKNENiafqnvnfSYDDKQVIknvNFEIPTQTSTAII-GPSGSGKSTLCH-LLLRFYDIDDGIIRIDGVDikdMTLST 405
Cdd:cd03279 6 LELKNFG--------PFREEQVI---DFTGLDNNGLFLIcGPTGAGKSTILDaITYALYGKTPRYGRQENLR---SVFAP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 406 LMSKISAVFQkvylFNDTIENNILFGNPGATKEEIIRaakqacchdfIMSLPEG-YQTMLNEKGSNLSGGEKQRISIARA 484
Cdd:cd03279 72 GEDTAEVSFT----FQLGGKKYRVERSRGLDYDQFTR----------IVLLPQGeFDRFLARPVSTLSGGETFLASLSLA 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613101153 485 I-LKD-------API--IILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHkLETIKNA-DQIIVLNEGE 545
Cdd:cd03279 138 LaLSEvlqnrggARLeaLFIDEGFGTLDPEALEAVATALELIrTENRMVGVISH-VEELKERiPQRLEVIKTP 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
469-547 |
1.76e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.25 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 469 SNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINEL-SKGKTVITIAHKLETIKN-ADQIIVLNEGEI 546
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrDAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
.
gi 613101153 547 I 547
Cdd:COG3845 481 V 481
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
471-539 |
2.05e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 42.84 E-value: 2.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613101153 471 LSGGEKQRISIAR--AIL--KDAPIIILDEATSSIDPENEQLIQTAINELSKGKTVITIAHKLETIKNADQII 539
Cdd:cd03278 114 LSGGEKALTALALlfAIFrvRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLY 186
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
471-527 |
2.13e-04 |
|
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: 42.87 E-value: 2.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 613101153 471 LSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAI-NELSKGKTVITIAH 527
Cdd:cd03231 126 LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
458-546 |
2.40e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.89 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 458 EGYQTMLNEKGSN-------LSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKL 529
Cdd:PRK15439 384 ERYRRALNIKFNHaeqaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAqNVAVLFISSDL 463
|
90
....*....|....*...
gi 613101153 530 ETI-KNADQIIVLNEGEI 546
Cdd:PRK15439 464 EEIeQMADRVLVMHQGEI 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
459-546 |
2.90e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 459 GYQTMLnekgSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELS-KGKTVITIAHKL-ETIKNAD 536
Cdd:PRK10982 384 GHRTQI----GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMpELLGITD 459
|
90
....*....|
gi 613101153 537 QIIVLNEGEI 546
Cdd:PRK10982 460 RILVMSNGLV 469
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-266 |
3.10e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 42.88 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 19 MILGFSMSFLNAIFIALPIFLAAKIFNNVLSHKPIYMKDILN-------------VVIIMVLLVIGRFITAYFKSKSHES 85
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLGLApllgpdplallllAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 86 IAYEMSAKERLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLENFAMKMV-DVVVN-----GYiliivlILSLLVVSW 159
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVlPLLTNlltlvGM------LGVMFWLDW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 160 QVSLLACIGVLLSFFAIQLLERKSRQNAPAYHNVQNQLVEKVLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRIN---T 236
Cdd:cd18564 155 QLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGlraA 234
|
250 260 270
....*....|....*....|....*....|
gi 613101153 237 KIEMQYIPfnllhllslkVVSIMIVLVACL 266
Cdd:cd18564 235 RLQALLSP----------VVDVLVAVGTAL 254
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
335-524 |
3.33e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.14 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 335 IAFQNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLLRFydiddGIIRIDGVDIKDMTLST--------L 406
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGL-----LHVESGQIQIDGKTATRgdrsrfmaY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 407 MSKISAVFQKVylfnDTIEN-NILFGNPGatkeeiiRAAKQACCHDF-IMSLPEGYQTMLNEkgsnLSGGEKQRISIARA 484
Cdd:PRK13543 87 LGHLPGLKADL----STLENlHFLCGLHG-------RRAKQMPGSALaIVGLAGYEDTLVRQ----LSAGQKKRLALARL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 613101153 485 ILKDAPIIILDEATSSIDPENEQLIQTAINE--LSKGKTVIT 524
Cdd:PRK13543 152 WLSPAPLWLLDEPYANLDLEGITLVNRMISAhlRGGGAALVT 193
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
350-567 |
5.44e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 350 IKNVNFEIPTQTSTAIIGPSGSGKSTLCHLLlrfydIDDGIIRIDGVDIKDMtlSTLMSKISAVFQKVylfnDTIENNIL 429
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLI-----AGVTMPNKGTVDIKGS--AALIAISSGLNGQL----TGIENIEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 430 FG-NPGATKEEIIRAAKQacchdfIMSLPEgYQTMLNEKGSNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQL 508
Cdd:PRK13545 109 KGlMMGLTKEKIKEIIPE------IIEFAD-IGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 509 IQTAINEL-SKGKTVITIAHKLETIKN-ADQIIVLNEGEIIQKGSHDELIRKpgmYQDFIR 567
Cdd:PRK13545 182 CLDKMNEFkEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDH---YDEFLK 239
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
33-246 |
6.97e-04 |
|
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: 41.85 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 33 IALPIFlAAKIFNNVLSHKPIY----MKDILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMSAKERLDIGDKLKNVRLG 108
Cdd:cd18780 13 LALPYF-FGQVIDAVTNHSGSGgeeaLRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 109 YFNSHHSNELTTIVTTDLTFLENFAMKMVDVVVNGYILIIVLILSLLVVSWQVSLLACIGV-LLSFFAIQL------LER 181
Cdd:cd18780 92 FFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVpPLSIGAVIYgkyvrkLSK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613101153 182 KSRQNAPAYHNVQNqlvekvlEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTKIEMQYIPFN 246
Cdd:cd18780 172 KFQDALAAASTVAE-------ESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFN 229
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
159-279 |
7.46e-04 |
|
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: 41.76 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 159 WQVSLLACIGVLLSFFAIQLLERKSRQNAPAYHNVQ---NQLVEkvlEVIRGIQVIKSFAKENTSLKSFNQSVNESKRIN 235
Cdd:cd18572 136 WRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALaeaNQVAE---EALSNIRTVRSFATEEREARRYERALDKALKLS 212
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 613101153 236 TKIEMQYIPFNLLHLLSLKVVSIMIVLVACLLYMNHSIDLPTLI 279
Cdd:cd18572 213 VRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLV 256
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
343-539 |
7.66e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 343 SYDDKQVIKnvnFEIPTqtsTAIIGPSGSGKSTL--ChLLLRFYDIDDGIIRIDGVDIKDMTLSTLMSKISAVFQKVYLF 420
Cdd:cd03240 11 SFHERSEIE---FFSPL---TLIVGQNGAGKTTIieA-LKYALTGELPPNSKGGAHDPKLIREGEVRAQVKLAFENANGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 421 NDTIENNIlfgnpgatkeEIIRAAkqacchdfIMSLPEGYQTMLNEKGSNLSGGEKQ------RISIARAILKDAPIIIL 494
Cdd:cd03240 84 KYTITRSL----------AILENV--------IFCHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 613101153 495 DEATSSIDPEN-EQLIQTAINELSKGKT--VITIAHKLETIKNADQII 539
Cdd:cd03240 146 DEPTTNLDEENiEESLAEIIEERKSQKNfqLIVITHDEELVDAADHIY 193
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
337-376 |
1.21e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.19 E-value: 1.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 613101153 337 FQNVNFSYDDKQVIknvnfEIPTQTSTAIIGPSGSGKSTL 376
Cdd:pfam13555 4 LQLINWGTFDGHTI-----PIDPRGNTLLTGPSGSGKSTL 38
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
469-527 |
1.64e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 41.07 E-value: 1.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 613101153 469 SNLSGGEKQRISIARAILKDAPIIILDEATSSIDPENEQLIQTAINELsKGkTVITIAH 527
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
438-558 |
2.27e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 438 EEIIRAAKQACChdFIMSLPEGYQTmLNEKGSNLSGGEKQRISIARAILKDAPII--ILDEATSSIDPEN-EQLIQTAIN 514
Cdd:PRK00635 447 EEVLQGLKSRLS--ILIDLGLPYLT-PERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDtHKLINVIKK 523
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 613101153 515 ELSKGKTVITIAHKLETIKNADQIIVLNE------GEIIQKGSHDELIRK 558
Cdd:PRK00635 524 LRDQGNTVLLVEHDEQMISLADRIIDIGPgagifgGEVLFNGSPREFLAK 573
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
351-376 |
4.07e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 4.07e-03
10 20
....*....|....*....|....*.
gi 613101153 351 KNVNFEIPTQTSTAIIGPSGSGKSTL 376
Cdd:COG0178 17 KNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
338-539 |
4.24e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.44 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 338 QNVNF-SYDDKQVIKnvnfeiPTQTSTAIIGPSGSGKSTLchlllrfydiddgiiridgvdikdmtlstlMSKISAVFQk 416
Cdd:cd03239 5 TLKNFkSYRDETVVG------GSNSFNAIVGPNGSGKSNI------------------------------VDAICFVLG- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 417 vYLFNDTIENNILFGNPGATKEEIIRAAKQAcchdfimSLPEGYQTMLNEK-GSNLSGGEKQRISIARAI----LKDAPI 491
Cdd:cd03239 48 -GKAAKLRRGSLLFLAGGGVKAGINSASVEI-------TFDKSYFLVLQGKvEQILSGGEKSLSALALIFalqeIKPSPF 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 613101153 492 IILDEATSSIDPENEQLIQTAINELSK-GKTVITIAHKLETIKNADQII 539
Cdd:cd03239 120 YVLDEIDAALDPTNRRRVSDMIKEMAKhTSQFIVITLKKEMFENADKLI 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
471-539 |
4.34e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.04 E-value: 4.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613101153 471 LSGGEKQRISIAR--AIL--KDAPIIILDEATSSIDPEN-EQLIQTaINELSKGKTVITIAHKLETIKNADQII 539
Cdd:TIGR02168 1090 LSGGEKALTALALlfAIFkvKPAPFCILDEVDAPLDDANvERFANL-LKEFSKNTQFIVITHNKGTMEVADQLY 1162
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
338-376 |
5.01e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.72 E-value: 5.01e-03
10 20 30
....*....|....*....|....*....|....*....
gi 613101153 338 QNVNFSYDDKQVIKNVNFEIPTQTSTAIIGPSGSGKSTL 376
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSL 43
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
20-285 |
5.38e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 39.10 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 20 ILGFSMsFLNAIFIALPIFLAAkIFNNVLSHKPIYMKDIL--NVVIIMVLLVIGRFITAYFKSKS-------------HE 84
Cdd:cd18566 7 VLLASL-FINILALATPLFILQ-VYDRVIPNESIPTLQVLviGVVIAILLESLLRLLRSYILAWIgarfdhrlsnaafEH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 85 SIAYEMSAKERLDIGDKLKNVrlgyfnshhsNELTTI--------VTT--DLTFLENFAMKMVdvVVNGYILIIVlilsl 154
Cdd:cd18566 85 LLSLPLSFFEREPSGAHLERL----------NSLEQIrefltgqaLLAllDLPFVLIFLGLIW--YLGGKLVLVP----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 155 lvvswqVSLLACIgVLLSFFAIQLLERKSRQNAPAYHNVQNQLVEkvleVIRGIQVIKSFAKENTSLKSF-NQSVNESKR 233
Cdd:cd18566 148 ------LVLLGLF-VLVAILLGPILRRALKERSRADERRQNFLIE----TLTGIHTIKAMAMEPQMLRRYeRLQANAAYA 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 613101153 234 INTKIEMQYIPFNLLHLLSlKVVSIMIVLVACLLYMNHSIDLPTLIMISIFS 285
Cdd:cd18566 217 GFKVAKINAVAQTLGQLFS-QVSMVAVVAFGALLVINGDLTVGALIACTMLS 267
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
30-288 |
7.13e-03 |
|
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: 38.62 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 30 AIFIALPiFLAAKIFNNVLSHKpiYMKDILNVVIIMVLLVIGRFITAYFKSKSHESIAYEMSAKERLDIGDKLKNVRLGY 109
Cdd:cd18576 10 AIGLVFP-LLAGQLIDAALGGG--DTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 110 FNSHHSNELTTIVTTDLT------------FLENFAMKMVDVVVngyiliivlilsLLVVSWQVSLLACIGVLLSFFAIQ 177
Cdd:cd18576 87 FHERRVGELTSRLSNDVTqiqdtltttlaeFLRQILTLIGGVVL------------LFFISWKLTLLMLATVPVVVLVAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 178 LLERKSRqnaPAYHNVQNQLVEK---VLEVIRGIQVIKSFAKENTSLKSFNQSVNESKRINTK---IEMQYIPFNllhLL 251
Cdd:cd18576 155 LFGRRIR---KLSKKVQDELAEAntiVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKrarIRALFSSFI---IF 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 613101153 252 SLKVVSIMIVLVACLLYMNHSIDLPTLIMISIFSFVI 288
Cdd:cd18576 229 LLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFI 265
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
359-384 |
7.29e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.94 E-value: 7.29e-03
10 20
....*....|....*....|....*.
gi 613101153 359 TQTSTAIIGPSGSGKSTLCHLLLRFY 384
Cdd:pfam13401 4 GAGILVLTGESGTGKTTLLRRLLEQL 29
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
159-295 |
8.42e-03 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 38.58 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 159 WQVSLLACIGVLLSFFAIQL----LERKSRQNAPAYHNVQNQLVEkvleVIRGIQVIKSFAKENTSLKSFNQSVNESKRI 234
Cdd:cd18570 141 WKLFLITLLIIPLYILIILLfnkpFKKKNREVMESNAELNSYLIE----SLKGIETIKSLNAEEQFLKKIEKKFSKLLKK 216
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613101153 235 NTKIEMQYIPFNLLHLLSLKVVSIMIVLVACLLYMNHSIDLPTLIMISIFSFVIFDSVENI 295
Cdd:cd18570 217 SFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENL 277
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
169-285 |
8.84e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 38.34 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 169 VLLSFFAIQLLERKSRQNAPAYHNVQNQLVEkvleVIRGIQVIKSFAKENTSLKS----FNQSVNESKRintKIEMQYIP 244
Cdd:cd18782 155 LLLTFLFGPILRRQIRRRAEASAKTQSYLVE----SLTGIQTVKAQNAELKARWRwqnrYARSLGEGFK---LTVLGTTS 227
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 613101153 245 FNLLHLLSlKVVSIMIVLVACLLYMNHSIDLPTLIMISIFS 285
Cdd:cd18782 228 GSLSQFLN-KLSSLLVLWVGAYLVLRGELTLGQLIAFRILS 267
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
58-231 |
9.47e-03 |
|
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: 38.23 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 58 ILNVVIIMVLLVIGRFITAYFKSksheSIAYEMSAKERLDIGDKLKNVRLGYFNSHHSNELTTIVTTDLTFLEN------ 131
Cdd:cd18575 39 FLLLLAVALVLALASALRFYLVS----WLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTvvgssl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613101153 132 -FAMKMVDVVVNGyiliivlILSLLVVSWQVSLLACIGVLLSFFAIQLLERKSRQNAPAYHNVQNQLVEKVLEVIRGIQV 210
Cdd:cd18575 115 sIALRNLLLLIGG-------LVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKT 187
|
170 180
....*....|....*....|.
gi 613101153 211 IKSFAKENTSLKSFNQSVNES 231
Cdd:cd18575 188 VQAFTREDAERQRFATAVEAA 208
|
|
| |
