|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-597 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 712.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 22 AKNTKGTVMRVWNYMGYQKAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQ 101
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 102 TFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDW 181
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 182 ILAIVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKAD 261
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 262 TFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEV 341
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 342 PEIKNKKDAFVVQNLQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDG 421
Cdd:COG1132 322 PEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 422 KNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQ 501
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 502 KQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESL 581
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
570
....*....|....*.
gi 447166279 582 MEDRGFYFDLYTSQFK 597
Cdd:COG1132 562 LARGGLYARLYRLQFG 577
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-595 |
2.43e-172 |
|
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: 506.29 E-value: 2.43e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 21 KAKNTKGTVMRVWNYMGYQKAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWL 100
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 101 QTFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALD 180
Cdd:COG2274 216 RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYS 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 181 WILAIVTLITVPIM----FFVTKKLVAYSgknfAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVS 256
Cdd:COG2274 295 PPLALVVLLLIPLYvllgLLFQPRLRRLS----REESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 257 ATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFE 336
Cdd:COG2274 371 RFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDD 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 337 IMDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQG 415
Cdd:COG2274 451 ILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 416 QIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGS 495
Cdd:COG2274 531 RILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGS 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 496 NLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEK 575
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
570 580
....*....|....*....|
gi 447166279 576 GNHESLMEDRGFYFDLYTSQ 595
Cdd:COG2274 691 GTHEELLARKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
28-597 |
2.82e-141 |
|
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: 421.82 E-value: 2.82e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 28 TVMRVWNYMGYQK-----AALTFIIFLVFVTTLLGLLGPylmgvIIDQYIVPKDLSGTARMCLLLIAIY---GVTVFLTw 99
Cdd:TIGR02203 1 TFRRLWSYVRPYKaglvlAGVAMILVAATESTLAALLKP-----LLDDGFGGRDRSVLWWVPLVVIGLAvlrGICSFVS- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 100 lqTFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFAL 179
Cdd:TIGR02203 75 --TYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 180 DWILAIVTLITVPI----MFFVTKKLVAYSgknfAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRV 255
Cdd:TIGR02203 153 SWQLTLIVVVMLPVlsilMRRVSKRLRRIS----KEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 256 SATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVF 335
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 336 EIMDEVPEIKNKKDAfvVQNLQGHVALENVSFGY-EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ 414
Cdd:TIGR02203 309 TLLDSPPEKDTGTRA--IERARGDVEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 415 GQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRL-DASDEEVINAAKAASAHSFIKHLPNQYETKIASE 493
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGEN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 494 GSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSIL 573
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546
|
570 580
....*....|....*....|....
gi 447166279 574 EKGNHESLMEDRGFYFDLYTSQFK 597
Cdd:TIGR02203 547 ERGTHNELLARNGLYAQLHNMQFR 570
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
33-595 |
1.72e-131 |
|
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: 397.65 E-value: 1.72e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 33 WNYMGYQKAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTArmcLLLIAIYGV----TVFLTWLQTFVMVNV 108
Cdd:COG5265 29 PPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVP---VGLLLAYGLlrllSVLFGELRDALFARV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 109 ALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDL---MSRVTNDIDNLnqaLTQSVVQIISSALTFIGVAIAMFAL-DWILA 184
Cdd:COG5265 106 TQRAVRRLALEVFRHLHALSLRFHLERQTGGLsrdIERGTKGIEFL---LRFLLFNILPTLLEIALVAGILLVKyDWWFA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 185 IVTLITVpimffvtkklVAYSGKNFA---KRQKDLGELNGFIEEAITGAdVTTL--------YGKEKKTVQNFNKINEQL 253
Cdd:COG5265 183 LITLVTV----------VLYIAFTVVvteWRTKFRREMNEADSEANTRA-VDSLlnyetvkyFGNEAREARRYDEALARY 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 254 RVSATKADTfsafifpSMNFINnLGMGLVIGTGSVMVLnGMTTVGVIA--------AFIN-YSRQFSRPLSQFATLMNTI 324
Cdd:COG5265 252 ERAAVKSQT-------SLALLN-FGQALIIALGLTAMM-LMAAQGVVAgtmtvgdfVLVNaYLIQLYIPLNFLGFVYREI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 325 QAAVAGGERVFEIMDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIIN 404
Cdd:COG5265 323 RQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLAR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 405 LLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPN 484
Cdd:COG5265 403 LLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPD 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 485 QYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQI 564
Cdd:COG5265 483 GYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEI 562
|
570 580 590
....*....|....*....|....*....|.
gi 447166279 565 LVIKDGSILEKGNHESLMEDRGFYFDLYTSQ 595
Cdd:COG5265 563 LVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
43-334 |
6.34e-127 |
|
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: 374.82 E-value: 6.34e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPK------DLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKI 116
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLgggggvDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 117 RQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFF 196
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 197 VTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINN 276
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 277 LGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
31-586 |
2.58e-126 |
|
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: 382.95 E-value: 2.58e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 31 RVWNYMGYQKAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPK-DLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVA 109
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGaPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 110 LKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLI 189
Cdd:COG4988 87 ARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 190 TVPI----MFFVTKKLVAYSGKNFAKrqkdLGELNGFIEEAITGadVTTL--YGKEKKTVQNFNKINEQLRVSatkadTF 263
Cdd:COG4988 167 TAPLiplfMILVGKGAAKASRRQWRA----LARLSGHFLDRLRG--LTTLklFGRAKAEAERIAEASEDFRKR-----TM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 264 S----AFIfpS---MNFINNLGMGLVIGTGSVMVLNG-MTTVGVIAAFInYSRQFSRPLSQFATLMNTIQAAVAGGERVF 335
Cdd:COG4988 236 KvlrvAFL--SsavLEFFASLSIALVAVYIGFRLLGGsLTLFAALFVLL-LAPEFFLPLRDLGSFYHARANGIAAAEKIF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 336 EIMDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQG 415
Cdd:COG4988 313 ALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 416 QIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGS 495
Cdd:COG4988 393 SILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 496 NLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEK 575
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
570
....*....|.
gi 447166279 576 GNHESLMEDRG 586
Cdd:COG4988 553 GTHEELLAKNG 563
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
32-596 |
5.98e-126 |
|
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: 382.51 E-value: 5.98e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 32 VWNYMG-YQKAALTFIIFLVFvTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVAL 110
Cdd:TIGR02204 9 LWPFVRpYRGRVLAALVALLI-TAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 111 KTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLIT 190
Cdd:TIGR02204 88 RVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 191 VPI----MFFVTKKLVAYSGKNfakrQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAF 266
Cdd:TIGR02204 168 VPLvllpILLFGRRVRKLSRES----QDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 267 IFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVPEIKN 346
Cdd:TIGR02204 244 LTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 347 KKDAFVV-QNLQGHVALENVSFGYEE--NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKN 423
Cdd:TIGR02204 324 PAHPKTLpVPLRGEIEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 424 IKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQ 503
Cdd:TIGR02204 404 LRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 504 LLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLME 583
Cdd:TIGR02204 484 RIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA 563
|
570
....*....|...
gi 447166279 584 DRGFYFDLYTSQF 596
Cdd:TIGR02204 564 KGGLYARLARLQF 576
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
28-596 |
3.87e-120 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 367.81 E-value: 3.87e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 28 TVMRVWNY-----MGYQKAALTFIIFLVFVTTLLGLLGPYLmgviiDQYIVPKDLSGTARMCLLLIA---IYGVTVFLTw 99
Cdd:PRK11176 12 TFRRLWPTiapfkAGLIVAGVALILNAASDTFMLSLLKPLL-----DDGFGKADRSVLKWMPLVVIGlmiLRGITSFIS- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 100 lqTFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFAL 179
Cdd:PRK11176 86 --SYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 180 DWILAIVTLITVPIMFFVTKkLVAYSGKNFAKR-QKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSAT 258
Cdd:PRK11176 164 SWQLSLILIVIAPIVSIAIR-VVSKRFRNISKNmQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 259 KADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAafINYSRQFS--RPLSQFATLMNTIQAAVAGGERVFE 336
Cdd:PRK11176 243 KMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAACQTLFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 337 IMDEVPEIKNKKdaFVVQNLQGHVALENVSFGYEENKTI-LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQG 415
Cdd:PRK11176 321 ILDLEQEKDEGK--RVIERAKGDIEFRNVTFTYPGKEVPaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 416 QIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDA-SDEEVINAAKAASAHSFIKHLPNQYETKIASEG 494
Cdd:PRK11176 399 EILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 495 SNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILE 574
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
570 580
....*....|....*....|..
gi 447166279 575 KGNHESLMEDRGFYFDLYTSQF 596
Cdd:PRK11176 559 RGTHAELLAQNGVYAQLHKMQF 580
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
107-592 |
4.94e-120 |
|
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: 367.17 E-value: 4.94e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 107 NVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIV 186
Cdd:COG4987 81 DATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 187 TLITVPIMFFVTKKLVAYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSA 265
Cdd:COG4987 161 LALGLLLAGLLLPLLAARLGRRAGRRLAAArAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 266 FIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFInysrqFSrPLSQFATLMNTIQAAVAGG------ERVFEIMD 339
Cdd:COG4987 241 LAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLV-----LA-ALALFEALAPLPAAAQHLGrvraaaRRLNELLD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 340 EVPEIKNKKDAfVVQNLQGHVALENVSFGY-EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIH 418
Cdd:COG4987 315 APPAVTEPAEP-APAPGGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 419 IDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLS 498
Cdd:COG4987 394 LGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLS 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 499 QGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNH 578
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTH 553
|
490
....*....|....
gi 447166279 579 ESLMEDRGFYFDLY 592
Cdd:COG4987 554 EELLAQNGRYRQLY 567
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
358-586 |
7.24e-120 |
|
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: 354.22 E-value: 7.24e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 358 GHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIG 437
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 438 VVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADI 517
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 518 LILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMEDRG 586
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
360-592 |
2.23e-119 |
|
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: 353.07 E-value: 2.23e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGV 438
Cdd:cd03251 1 VEFKNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADIL 518
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 519 ILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMEDRGFYFDLY 592
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-591 |
6.27e-117 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 363.66 E-value: 6.27e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 23 KNTKGTVMRVWNYMGYQKAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTAR----MCLLLIAIYGVTVFLT 98
Cdd:TIGR00958 143 SETADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASaiffMCLLSIASSVSAGLRG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 99 WLQTFVMVNVALKtiqkIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFA 178
Cdd:TIGR00958 223 GSFNYTMARINLR----IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLW 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 179 LDWILAIVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFN-KINEQLRVSA 257
Cdd:TIGR00958 299 LSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKeALEETLQLNK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 258 TKADTFSAFIFpSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEI 337
Cdd:TIGR00958 379 RKALAYAGYLW-TTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 338 MDEVPEIKNKkDAFVVQNLQGHVALENVSFGY--EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQG 415
Cdd:TIGR00958 458 LDRKPNIPLT-GTLAPLNLEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGG 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 416 QIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGS 495
Cdd:TIGR00958 537 QVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGS 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 496 NLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNnlMRDRTSFVIAHRLKTIEKADQILVIKDGSILEK 575
Cdd:TIGR00958 617 QLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEM 694
|
570
....*....|....*.
gi 447166279 576 GNHESLMEDRGFYFDL 591
Cdd:TIGR00958 695 GTHKQLMEDQGCYKHL 710
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
360-595 |
1.69e-110 |
|
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: 330.35 E-value: 1.69e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVV 439
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILI 519
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 520 LDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMEDRGFYFDLYTSQ 595
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
31-596 |
9.01e-106 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 330.77 E-value: 9.01e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 31 RVWNYMGYQKAALTFIIFLVFVTTLLGLLGPYLMGVIIDQyivpkdLSGTARMCLLLIAIYGVTVFltwlQTFVMVNVAL 110
Cdd:PRK13657 9 RVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDA------ISGKGDIFPLLAAWAGFGLF----NIIAGVLVAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 111 -------KTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNL--------NQALTQSVvqiisSALTFIGVAIA 175
Cdd:PRK13657 79 hadrlahRRRLAVLTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALfglwlefmREHLATLV-----ALVVLLPLALF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 176 MfalDWILAIVtLITVPIMFFVTKKLVAysgknfaKRQKDL--------GELNGFIEEAITGADVttlygkekktVQNFN 247
Cdd:PRK13657 154 M---NWRLSLV-LVVLGIVYTLITTLVM-------RKTKDGqaaveehyHDLFAHVSDAIGNVSV----------VQSYN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 248 KINEQLRVSATKADTFSAFIFPSMNF------IN----NLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQF 317
Cdd:PRK13657 213 RIEAETQALRDIADNLLAAQMPVLSWwalasvLNraasTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 318 ATLMNTIQAAVAGGERVFEIMDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGS 397
Cdd:PRK13657 293 VAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 398 GKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHS 477
Cdd:PRK13657 373 GKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 478 FIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKT 557
Cdd:PRK13657 453 FIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLST 532
|
570 580 590
....*....|....*....|....*....|....*....
gi 447166279 558 IEKADQILVIKDGSILEKGNHESLMEDRGFYFDLYTSQF 596
Cdd:PRK13657 533 VRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQG 571
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
360-595 |
3.01e-105 |
|
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: 317.17 E-value: 3.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEE--NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIG 437
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 438 VVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADI 517
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 518 LILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMEDRGFYFDLYTSQ 595
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
28-595 |
1.34e-97 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 309.73 E-value: 1.34e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 28 TVMRVWNYMGYQKAALTFIIFLVFVTTLLGLLGPYLMGVIIDQyIVPKD---LSGTARMCLLLIAIYGVTVFLTWLQTFV 104
Cdd:PRK10790 10 TLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDN-MVAKGnlpLGLVAGLAAAYVGLQLLAAGLHYAQSLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 105 MVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQaLTQSVVQIISSALTFIGVA-IAMFALDWIL 183
Cdd:PRK10790 89 FNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRD-LYVTVVATVLRSAALIGAMlVAMFSLDWRM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 184 AIVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEK---KTVQNFNKINEQLRVSATKA 260
Cdd:PRK10790 168 ALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQArfgERMGEASRSHYMARMQTLRL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 261 DTFsaFIFPSMNFINNL---GMGLVIGTGSVmvlnGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEI 337
Cdd:PRK10790 248 DGF--LLRPLLSLFSALilcGLLMLFGFSAS----GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 338 MDEvPEIKNKKDAFVVQnlQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQI 417
Cdd:PRK10790 322 MDG-PRQQYGNDDRPLQ--SGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 418 HIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRlDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNL 497
Cdd:PRK10790 399 RLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 498 SQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLnNLMRDRTSF-VIAHRLKTIEKADQILVIKDGSILEKG 576
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLvVIAHRLSTIVEADTILVLHRGQAVEQG 556
|
570
....*....|....*....
gi 447166279 577 NHESLMEDRGFYFDLYTSQ 595
Cdd:PRK10790 557 THQQLLAAQGRYWQMYQLQ 575
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
47-595 |
7.32e-90 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 288.92 E-value: 7.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 47 IFLVFVTTLLGLLGPYLMGVIIDQyIVPKDLSgtARMCLLLIAIYGVTVFLTWLQTFV----MVNVALKTIQKIRQDIFE 122
Cdd:PRK10789 1 VALLIIIAMLQLIPPKVVGIIVDG-VTEQHMT--TGQILMWIGTMVLIAVVVYLLRYVwrvlLFGASYQLAVELREDFYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAM-FALDWILAIVTLITVPIMFFVTKKL 201
Cdd:PRK10789 78 QLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPVMAIMIKRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 202 VAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQ-----LRVSATKAdTFSAFIFPSMNFINN 276
Cdd:PRK10789 158 GDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDtgkknMRVARIDA-RFDPTIYIAIGMANL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 277 LGmglvIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVPEIKNKKDAFVVQnl 356
Cdd:PRK10789 237 LA----IGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEG-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 357 QGHVALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSK 435
Cdd:PRK10789 311 RGELDVNIRQFTYPQTdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 IGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:PRK10789 391 LAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNA 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 516 DILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMEDRGFYFDLYTSQ 595
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
43-334 |
2.40e-88 |
|
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: 275.42 E-value: 2.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVP--KDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDI 120
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPgqGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 121 FEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKK 200
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 201 LVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMG 280
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447166279 281 LVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
39-567 |
1.93e-86 |
|
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: 278.40 E-value: 1.93e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 39 QKAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPK-DLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIR 117
Cdd:TIGR02857 1 ARRALALLALLGVLGALLIIAQAWLLARVVDGLISAGePLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 118 QDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVP-IMFF 196
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPlIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 197 VTkkLVAYSGKNFAKRQ-KDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRvSAT----KADTFSAFIfpsM 271
Cdd:TIGR02857 161 MI--LIGWAAQAAARKQwAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYR-ERTmrvlRIAFLSSAV---L 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 272 NFINNLGMGLVIGTGSVMVLNG-MTTVGVIAAFInYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVPEIK-NKKD 349
Cdd:TIGR02857 235 ELFATLSVALVAVYIGFRLLAGdLDLATGLFVLL-LAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLaGKAP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 350 AFVVQNLQghVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDM 429
Cdd:TIGR02857 314 VTAAPASS--LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 430 NSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIAR 509
Cdd:TIGR02857 392 DSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALAR 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVI 567
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
28-591 |
1.18e-85 |
|
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: 278.31 E-value: 1.18e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 28 TVMRVWNYMGYQKAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTarmcLLLIAIYGVTVFLTwlqtFVMV- 106
Cdd:TIGR01192 6 VYVRALSYLNVHKNRVLLIVIANITLAAITIAEPILFGRIIDAISSKSDVLPT----LALWAGFGVFNTIA----YVLVa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 107 ----NVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWI 182
Cdd:TIGR01192 78 readRLAHGRRATLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 183 LAIVtLITVPIMFFVTKKLVAYSGKNF-AKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKAD 261
Cdd:TIGR01192 158 LSIV-LMVLGILYILIAKLVMQRTKNGqAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYPVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 262 TFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEV 341
Cdd:TIGR01192 237 DWWALASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 342 PEIKNKKDAFVVQNLQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDG 421
Cdd:TIGR01192 317 FQREEPADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 422 KNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQ 501
Cdd:TIGR01192 397 IDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 502 KQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESL 581
Cdd:TIGR01192 477 RQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQEL 556
|
570
....*....|
gi 447166279 582 MEDRGFYFDL 591
Cdd:TIGR01192 557 IQKDGRFYKL 566
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
42-334 |
9.55e-85 |
|
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: 266.26 E-value: 9.55e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 42 ALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIF 121
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 122 EKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKL 201
Cdd:cd18545 81 SHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 202 VAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGL 281
Cdd:cd18545 161 RRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTAL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447166279 282 VIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18545 241 VYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
360-570 |
5.58e-79 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 246.91 E-value: 5.58e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGV 438
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQDTYLFAGTIMDNIrygrldasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILADADIL 518
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447166279 519 ILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDG 570
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
43-334 |
1.75e-78 |
|
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: 250.16 E-value: 1.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFE 122
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLV 202
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166279 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
354-572 |
2.30e-77 |
|
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: 244.69 E-value: 2.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 354 QNLQGHVALENVSFGY--EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNS 431
Cdd:cd03248 6 DHLKGIVKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 432 LRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAI 511
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 512 LADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
39-593 |
5.91e-77 |
|
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: 258.13 E-value: 5.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 39 QKAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIvPKDLSGTARMCLL-LIAIYGVTVFLTWLQTFVMV----NVALKTI 113
Cdd:TIGR01193 154 QKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYI-PHKMMGTLGIISIgLIIAYIIQQILSYIQIFLLNvlgqRLSIDII 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 114 QKIRQDIFEkiqtLSLRFFDVRSQGDLMSRVTnDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPI 193
Cdd:TIGR01193 233 LSYIKHLFE----LPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPV 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 194 MffvtkKLVAYSGKN-FAKRQKDLGE----LNGFIEEAITGADVTTLYGKEKKTvqnFNKINEQL------RVSATKADT 262
Cdd:TIGR01193 308 Y-----AVIIILFKRtFNKLNHDAMQanavLNSSIIEDLNGIETIKSLTSEAER---YSKIDSEFgdylnkSFKYQKADQ 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 263 FSAFIFPSMNFINNLgmgLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVP 342
Cdd:TIGR01193 380 GQQAIKAVTKLILNV---VILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDS 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 343 EIKNKKDAFVVQNLQGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGK 422
Cdd:TIGR01193 457 EFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 423 NIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYG-RLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQ 501
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQ 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 502 KQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNlMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESL 581
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDEL 695
|
570
....*....|..
gi 447166279 582 MEDRGFYFDLYT 593
Cdd:TIGR01193 696 LDRNGFYASLIH 707
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
358-577 |
2.12e-74 |
|
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: 236.62 E-value: 2.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 358 GHVALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKI 436
Cdd:cd03244 1 GDIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAGTIMDNirygrLD----ASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAIL 512
Cdd:cd03244 81 SIIPQDPVLFSGTIRSN-----LDpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 513 ADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGN 577
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
360-595 |
6.01e-73 |
|
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: 233.53 E-value: 6.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYE-ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGV 438
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADIL 518
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 519 ILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMEDRGFYFDLYTSQ 595
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
86-555 |
1.08e-71 |
|
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: 239.96 E-value: 1.08e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 86 LLIAIYGVTVF------LTWLQTFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSV 159
Cdd:TIGR02868 52 LSVAAVAVRAFgigravFRYLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 160 VQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLVAYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGK 238
Cdd:TIGR02868 132 VPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASGA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 239 EKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFA 318
Cdd:TIGR02868 212 LPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALP 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 319 TLMNTIQAAVAGGERVFEIMDEVPEIKNKKDAFVVQNLQGHVALE--NVSFGYEENKTILKEVSLKARPGETIALVGPTG 396
Cdd:TIGR02868 292 AAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLElrDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSG 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 397 SGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAH 476
Cdd:TIGR02868 372 SGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLA 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 477 SFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRL 555
Cdd:TIGR02868 452 DWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
111-592 |
1.37e-70 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 237.80 E-value: 1.37e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 111 KTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAI----- 185
Cdd:PRK11160 90 RVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDLTLALtlggi 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 186 --VTLITVPIMFFvtkklvaYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKadt 262
Cdd:PRK11160 170 llLLLLLLPLLFY-------RLGKKPGQDLTHLrAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRR--- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 263 fsafifpsMNFINNLGMGLVIgtgsvmVLNGMTTVGV--IAAFINYSRQFSRP---LSQFATL-----MNTIQAA----- 327
Cdd:PRK11160 240 --------QANLTGLSQALMI------LANGLTVVLMlwLAAGGVGGNAQPGAliaLFVFAALaafeaLMPVAGAfqhlg 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 328 --VAGGERVFEIMDEVPEIKNKKDAfVVQNLQGHVALENVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTIIN 404
Cdd:PRK11160 306 qvIASARRINEITEQKPEVTFPTTS-TAAADQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 405 LLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHsfiKHLPN 484
Cdd:PRK11160 385 LLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLE---KLLED 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 485 Q--YETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKAD 562
Cdd:PRK11160 462 DkgLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFD 541
|
490 500 510
....*....|....*....|....*....|
gi 447166279 563 QILVIKDGSILEKGNHESLMEDRGFYFDLY 592
Cdd:PRK11160 542 RICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
43-334 |
1.38e-69 |
|
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: 226.65 E-value: 1.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQ-YIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIF 121
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLvTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 122 EKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKL 201
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 202 VAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGL 281
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447166279 282 VIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18778 241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
43-334 |
2.09e-68 |
|
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: 223.93 E-value: 2.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARM----CLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQ 118
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLllllVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 119 DIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVT 198
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 199 KKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLG 278
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 279 MGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
358-576 |
7.59e-68 |
|
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: 219.77 E-value: 7.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 358 GHVALENVSFGY--EENKTiLKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSK 435
Cdd:cd03245 1 GRIEFRNVSFSYpnQEIPA-LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 IGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 516 DILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKG 576
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
40-572 |
1.57e-66 |
|
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: 226.94 E-value: 1.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 40 KAALTFIIFLVFVTTLLGLLGP-YLMGViidqYivpkDLSGTAR-------MCLLLIAIYGVTVFLTWLQTFVMVNVALK 111
Cdd:COG4618 19 RRAFLSVGLFSFFINLLMLTPPlYMLQV----Y----DRVLTSRsvdtllmLTLLALGLYAVMGLLDAVRSRILVRVGAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 112 TIQKIRQDIFEKIQTLSLRFFDVRSQGDLmsrvtNDIDNLNQALTqsvvqiiSSALT----------FIGVaiaMFALDW 181
Cdd:COG4618 91 LDRRLGPRVFDAAFRAALRGGGGAAAQAL-----RDLDTLRQFLT-------GPGLFalfdlpwapiFLAV---LFLFHP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 182 ILAIVTLITVPIMF-------FVTKKLVAYSGKNFAKRqkdlgelNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLR 254
Cdd:COG4618 156 LLGLLALVGALVLValallneRLTRKPLKEANEAAIRA-------NAFAEAALRNAEVIEAMGMLPALRRRWQRANARAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 255 VSATKADTFSAFIfpsMNFINNLGMGL---VIGTGSVMVLNGMTTVGV-IAAFINYSRQFSrPLSQFATLMNTIQAAVAG 330
Cdd:COG4618 229 ALQARASDRAGGF---SALSKFLRLLLqsaVLGLGAYLVIQGEITPGAmIAASILMGRALA-PIEQAIGGWKQFVSARQA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 331 GERVFEIMDEVPEiknKKDAFVVQNLQGHVALENVSFGY-EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRF 409
Cdd:COG4618 305 YRRLNELLAAVPA---EPERMPLPRPKGRLSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 410 YDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNI-RYGrlDASDEEVINAAKAASAHSFIKHLPNQYET 488
Cdd:COG4618 382 WPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 489 KIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLmRDR--TSFVIAHRLKTIEKADQILV 566
Cdd:COG4618 460 RIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARgaTVVVITHRPSLLAAVDKLLV 538
|
....*.
gi 447166279 567 IKDGSI 572
Cdd:COG4618 539 LRDGRV 544
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
43-334 |
1.32e-61 |
|
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: 205.74 E-value: 1.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLV 202
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166279 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
43-334 |
4.52e-61 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 204.26 E-value: 4.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLV 202
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18546 161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166279 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18546 241 LLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
43-334 |
1.07e-57 |
|
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: 195.33 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLV 202
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166279 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
319-593 |
2.06e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 197.37 E-value: 2.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 319 TLMNTIQAAVAGGERVFEImDEVPEIKNKkdAFVVQNLQGHVALENVSFgyeenktilkevSLKArpGETIALVGPTGSG 398
Cdd:PRK11174 326 TFLETPLAHPQQGEKELAS-NDPVTIEAE--DLEILSPDGKTLAGPLNF------------TLPA--GQRIALVGPSGAG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 399 KTTIINLLTRF--YdiqQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAH 476
Cdd:PRK11174 389 KTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVS 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 477 SFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLK 556
Cdd:PRK11174 466 EFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLE 545
|
250 260 270
....*....|....*....|....*....|....*..
gi 447166279 557 TIEKADQILVIKDGSILEKGNHESLMEDRGFYFDLYT 593
Cdd:PRK11174 546 DLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
43-334 |
2.75e-55 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 189.65 E-value: 2.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLS---------GTARM------CLLLIAIYGVTVFLTWLQTFVMVN 107
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPgllglapllGPDPLallllaAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 108 VALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVT 187
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 188 LITVPIMFFVTKKlvaYSG--KNFAKRQ-KDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFS 264
Cdd:cd18564 161 LAVAPLLLLAARR---FSRriKEASREQrRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQ 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 265 AFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18564 238 ALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-591 |
1.44e-54 |
|
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: 200.56 E-value: 1.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 33 WNYMGYQKAALTFIIFLVFVTTLLGLLGP-YLMGVIIDQYIVpkdlSGTARMCLLLIAIYGVtvfLTWLQTFVM----VN 107
Cdd:TIGR00957 956 WDYMKAIGLFITFLSIFLFVCNHVSALASnYWLSLWTDDPMV----NGTQNNTSLRLSVYGA---LGILQGFAVfgysMA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 108 VALKTIQKIR---QDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILA 184
Cdd:TIGR00957 1029 VSIGGIQASRvlhQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAA 1108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 185 IVTLITVPIMFFVTKKLVAYSGKnfAKRQKDLGE--LNGFIEEAITGADVttlygkekktVQNFNKINEQLRVSATKADT 262
Cdd:TIGR00957 1109 VIIPPLGLLYFFVQRFYVASSRQ--LKRLESVSRspVYSHFNETLLGVSV----------IRAFEEQERFIHQSDLKVDE 1176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 263 FSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTV--------GVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:TIGR00957 1177 NQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVisrhslsaGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERL 1256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 335 FEIMdevpeiKNKKDA-FVVQNLQ--------GHVALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIIN 404
Cdd:TIGR00957 1257 KEYS------ETEKEApWQIQETAppsgwpprGRVEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTL 1330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 405 LLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIR-YGRLdaSDEEVINAAKAASAHSFIKHLP 483
Cdd:TIGR00957 1331 GLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWALELAHLKTFVSALP 1408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 484 NQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQ 563
Cdd:TIGR00957 1409 DKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTR 1488
|
570 580
....*....|....*....|....*...
gi 447166279 564 ILVIKDGSILEKGNHESLMEDRGFYFDL 591
Cdd:TIGR00957 1489 VIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
47-334 |
4.03e-54 |
|
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: 185.69 E-value: 4.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPK-DLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFEKIQ 125
Cdd:cd18541 5 ILFLILVDLLQLLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 126 TLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLVAYS 205
Cdd:cd18541 85 TLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 206 GKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGT 285
Cdd:cd18541 165 HKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWY 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 447166279 286 GSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18541 245 GGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
40-334 |
5.61e-54 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 185.38 E-value: 5.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 40 KAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARmcllLIAIYGVTVFLTWLQTFVMVNVA----LKTIQK 115
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTG----FILLYLGLILIQALSVFLFIRLAgkieMGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 116 IRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMF 195
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 196 FVTkklvAYSGKNFAKRQKDLGELN----GFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSM 271
Cdd:cd18540 157 VVS----IYFQKKILKAYRKVRKINsritGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 272 NFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18540 233 LFLGSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
358-576 |
2.17e-52 |
|
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: 178.37 E-value: 2.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 358 GHVALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKI 436
Cdd:cd03369 5 GEIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAGTIMDNI-RYGRLdaSDEEVINAakaasahsfikhlpnqyeTKIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 516 DILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKG 576
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
43-334 |
1.18e-51 |
|
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: 179.17 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTArmcLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLL---ALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLV 202
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 203 AYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166279 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18551 238 LGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
45-334 |
2.48e-50 |
|
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: 175.66 E-value: 2.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 45 FIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFEKI 124
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 125 QTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLVAY 204
Cdd:cd18548 83 QSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 205 SGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIG 284
Cdd:cd18548 163 AIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILW 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 447166279 285 TGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18548 243 FGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
43-314 |
3.47e-50 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 174.75 E-value: 3.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLS--GTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDI 120
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 121 FEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKK 200
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 201 LVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMG 280
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 447166279 281 LVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPL 314
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
43-334 |
2.89e-49 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 173.05 E-value: 2.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLV 202
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 203 AYSGKNFAKRQKDLGELNGFIEE--AITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMG 280
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447166279 281 LVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
51-334 |
4.85e-49 |
|
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: 172.75 E-value: 4.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 51 FVTTLLGLLGPYLMGVIID---------QYIVPKDLSGTARM------CLLLIAIYGVTVFLTWLQTFVMVNVALKTIQK 115
Cdd:cd18565 9 ILNRLFDLAPPLLIGVAIDavfngeasfLPLVPASLGPADPRgqlwllGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 116 IRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMF 195
Cdd:cd18565 89 LRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLII 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 196 FVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFIN 275
Cdd:cd18565 169 AGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVA 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 276 NLGMGLVIGTGSVMVLNGMT------TVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18565 249 GAGFVATFVVGGYWVLDGPPlftgtlTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
360-576 |
7.35e-49 |
|
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: 167.88 E-value: 7.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDmNSLRSKIGV 438
Cdd:cd03247 1 LSINNVSFSYPEQeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQDTYLFAGTIMDNIrygrldasdeevinaakaasahsfikhlpnqyetkiaseGSNLSQGQKQLLAIARAILADADIL 518
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 519 ILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKG 576
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
43-333 |
5.63e-48 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 169.55 E-value: 5.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVT---- 198
Cdd:cd18549 84 HLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTiyfn 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 199 KKLVAYSGKNFAKrqkdLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLG 278
Cdd:cd18549 164 KKMKKAFRRVREK----IGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 279 MGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGER 333
Cdd:cd18549 240 NLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
46-577 |
6.85e-48 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 180.61 E-value: 6.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 46 IIFLVFV-TTLLGLLGPYLM---GVIIDQYIVPKDLSGTArMCLLLIAIygVTVFLTWLQTFVMVNVALKTIQKIRQDIF 121
Cdd:PTZ00265 61 LLGVSFVcATISGGTLPFFVsvfGVIMKNMNLGENVNDII-FSLVLIGI--FQFILSFISSFCMDVVTTKILKTLKLEFL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 122 EKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVtkKL 201
Cdd:PTZ00265 138 KSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYIC--GV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 202 VAYSGKNFAKRQKDLGELN--GFIEEAITGADVTTLYGKEKKTVQNFNkINEQLrvsatkadtFSAFIFPSmNFINNLGM 279
Cdd:PTZ00265 216 ICNKKVKINKKTSLLYNNNtmSIIEEALVGIRTVVSYCGEKTILKKFN-LSEKL---------YSKYILKA-NFMESLHI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 280 GLVIG-----------TGSVMVLN------------GMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAvaggERVFE 336
Cdd:PTZ00265 285 GMINGfilasyafgfwYGTRIIISdlsnqqpnndfhGGSVISILLGVLISMFMLTIILPNITEYMKSLEAT----NSLYE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 337 IMDEVPEIKNKKDAFVVQNLQgHVALENVSFGYEENK--TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ 414
Cdd:PTZ00265 361 IINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 415 GQIHI-DGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYG-----RLDA--------------------------- 461
Cdd:PTZ00265 440 GDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkDLEAlsnyynedgndsqenknkrnscrakca 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 462 -------------------------SDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADAD 516
Cdd:PTZ00265 520 gdlndmsnttdsneliemrknyqtiKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPK 599
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 517 ILILDEATSNIDTRTELQIQEGLNNLM--RDRTSFVIAHRLKTIEKADQILVIkdgSILEKGN 577
Cdd:PTZ00265 600 ILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL---SNRERGS 659
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
360-585 |
1.20e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 166.35 E-value: 1.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVV 439
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQ--DTYLFAGTIMDNIRYG--RLDASDEEVINAAKAASAHSFIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILADA 515
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpeNLGLPREEIRERVEEALELVGLEHLADR-------PPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166279 516 DILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIA-HRLKTIEK-ADQILVIKDGSILEKGNHESLMEDR 585
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
47-334 |
5.53e-46 |
|
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: 163.81 E-value: 5.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFEKIQT 126
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 127 LSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKklvaYSG 206
Cdd:cd18576 82 LPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV----LFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 207 KNF----AKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18576 158 RRIrklsKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166279 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18576 238 LWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
47-334 |
2.34e-45 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 162.27 E-value: 2.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFEKIQT 126
Cdd:cd18543 5 LLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 127 LSLRFFD-VRSqGDLMSRVTNDIdNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTkklVAYS 205
Cdd:cd18543 85 LDGAFHDrWQS-GQLLSRATSDL-SLVQRFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVA---RRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 206 GKNFA---KRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLV 282
Cdd:cd18543 160 RRYFPasrRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166279 283 IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18543 240 LALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
85-582 |
1.73e-44 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 170.59 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 85 LLLIAIygvTVFLT-WLQTFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQ--GDLMSRVTNDIDNLNQALTQSVVQ 161
Cdd:PTZ00265 872 ILVIAI---AMFISeTLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHLLKTGLVNNIVI 948
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 162 IISSALTFIGVAIAMFALDWILAIVTLITVPIMFFV-------------TKKLVAYSGKNFAKRQKD--LGELNGFIEEA 226
Cdd:PTZ00265 949 FTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVfairarltankdvEKKEINQPGTVFAYNSDDeiFKDPSFLIQEA 1028
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 227 ITGADVTTLYGKE-------KKTVQNFNK-------INEQLRVSATKADTFS---AFIFPSM----------NFINNLGM 279
Cdd:PTZ00265 1029 FYNMNTVIIYGLEdyfcnliEKAIDYSNKgqkrktlVNSMLWGFSQSAQLFInsfAYWFGSFlirrgtilvdDFMKSLFT 1108
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 280 GLVIGT--GSVMVLNGMTTvgviAAFINYSRQFsrPLsqfATLMNTIQAAVAGGERvfeimdevpeIKNKKDafvvqnLQ 357
Cdd:PTZ00265 1109 FLFTGSyaGKLMSLKGDSE----NAKLSFEKYY--PL---IIRKSNIDVRDNGGIR----------IKNKND------IK 1163
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 358 GHVALENVSFGY--EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ--------------------- 414
Cdd:PTZ00265 1164 GKIEIMDVNFRYisRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyq 1243
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 415 ---------------------------------GQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRLDA 461
Cdd:PTZ00265 1244 gdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDA 1323
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 462 SDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNN 541
Cdd:PTZ00265 1324 TREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 447166279 542 L--MRDRTSFVIAHRLKTIEKADQILVI----KDGSILE-KGNHESLM 582
Cdd:PTZ00265 1404 IkdKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELL 1451
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
362-572 |
2.80e-43 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 152.76 E-value: 2.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVL 440
Cdd:cd03246 3 VENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 441 QDTYLFAGTIMDNIrygrldasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILADADILIL 520
Cdd:cd03246 83 QDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447166279 521 DEATSNIDTRTELQIQEGLNNL-MRDRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
356-582 |
3.55e-43 |
|
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: 155.45 E-value: 3.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 356 LQGHVALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRS 434
Cdd:cd03288 16 LGGEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 435 KIGVVLQDTYLFAGTIMDNIRYGRlDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILAD 514
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLM 582
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
362-570 |
7.12e-43 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 153.01 E-value: 7.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEE-NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVL 440
Cdd:cd03225 2 LKNLSFSYPDgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 441 Q--DTYLFAGTIMDNIRYG--RLDASDEEVINAAKAASAHSFIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILADAD 516
Cdd:cd03225 82 QnpDDQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEGLRDR-------SPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 517 ILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIA-HRLKTI-EKADQILVIKDG 570
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLlELADRVIVLEDG 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
360-576 |
2.05e-42 |
|
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: 152.33 E-value: 2.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ-----GQIHIDGKNIKEYDMN--SL 432
Cdd:cd03260 1 IELRDLNVYYGD-KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDvlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 433 RSKIGVVLQDTYLFAGTIMDNIRYG-RL------DASDEEVINAAKAAsahsfikHLPNqyETKIASEGSNLSQGQKQLL 505
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlRLhgiklkEELDERVEEALRKA-------ALWD--EVKDRLHALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166279 506 AIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEK-ADQILVIKDGSILEKG 576
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
47-334 |
5.02e-42 |
|
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: 153.10 E-value: 5.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFEKIQT 126
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 127 LSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLVAYSG 206
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 207 KNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGTG 286
Cdd:cd18557 162 KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 447166279 287 SVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18557 242 GYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
362-586 |
1.49e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 147.70 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDmNSLRSKIGVVLQ 441
Cdd:COG4555 4 VENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFAG-TIMDNIRY-GRLDASDEEVINAAKAASAHSFIkhLPNQYETKIasegSNLSQGQKQLLAIARAILADADILI 519
Cdd:COG4555 82 ERGLYDRlTVRENIRYfAELYGLFDEELKKRIEELIELLG--LEEFLDRRV----GELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 520 LDEATSNIDTRTELQIQEGLNNLMRDRTSFVIA-HRLKTIEK-ADQILVIKDGSILEKGNHESLMEDRG 586
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
376-525 |
2.59e-40 |
|
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: 143.56 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAG-TIMDNI 454
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 455 RYGRLdasDEEVINAAKAASAHSFIKHL--PNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-589 |
3.45e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 157.45 E-value: 3.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 33 WN-YMGYQKAA----LTFIIFLVFVTT-LLGLLGPYLMGVIIDQYiVPKDLSGTarmclLLIAIYGVTVF----LTWLQT 102
Cdd:PLN03232 898 WNvLMRYNKAVgglwVVMILLVCYLTTeVLRVSSSTWLSIWTDQS-TPKSYSPG-----FYIVVYALLGFgqvaVTFTNS 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 103 FVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQaltqSVVQIISSALTFIGVAIAMFALDWI 182
Cdd:PLN03232 972 FWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDR----NVANLMNMFMNQLWQLLSTFALIGT 1047
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 183 LAIVTLITV-PIMFFVTKKLVAYSGKNFAKRQKDlgelngfieeAITGADVTTLYGKEKK---TVQNFNKINEQLRVSAT 258
Cdd:PLN03232 1048 VSTISLWAImPLLILFYAAYLYYQSTSREVRRLD----------SVTRSPIYAQFGEALNglsSIRAYKAYDRMAKINGK 1117
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 259 KADTFSAFIFPSMNF-------INNLGMGLVIGTGSVMVL-NGMT--------TVGVIAAF-INYSRQFSRPLSQFATLM 321
Cdd:PLN03232 1118 SMDNNIRFTLANTSSnrwltirLETLGGVMIWLTATFAVLrNGNAenqagfasTMGLLLSYtLNITTLLSGVLRQASKAE 1197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 322 NTIQAAvaggERVFEIMD---EVPEIKNKKDAFVVQNLQGHVALENVSFGYE-ENKTILKEVSLKARPGETIALVGPTGS 397
Cdd:PLN03232 1198 NSLNSV----ERVGNYIDlpsEATAIIENNRPVSGWPSRGSIKFEDVHLRYRpGLPPVLHGLSFFVSPSEKVGVVGRTGA 1273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 398 GKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRYGRlDASDEEVINAAKAASAHS 477
Cdd:PLN03232 1274 GKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS-EHNDADLWEALERAHIKD 1352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 478 FIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKT 557
Cdd:PLN03232 1353 VIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNT 1432
|
570 580 590
....*....|....*....|....*....|..
gi 447166279 558 IEKADQILVIKDGSILEKGNHESLMEDRGFYF 589
Cdd:PLN03232 1433 IIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
40-334 |
3.54e-40 |
|
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: 147.98 E-value: 3.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 40 KAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQD 119
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTK 199
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 200 KLVaysgKNFAKRQKDL----GELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFIN 275
Cdd:cd18570 160 LFN----KPFKKKNREVmesnAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLIS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 276 NLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18570 236 LIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
119-585 |
4.75e-40 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 157.25 E-value: 4.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 119 DIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISsalTFIGVAIAMFALDWILAIVTLITVPIMFFVT 198
Cdd:PTZ00243 1036 DLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQ---CLFSICSSILVTSASQPFVLVALVPCGYLYY 1112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 199 KKLVAYSGKNFA-KRQKDLGE--LNGFIEEAITGADVTTLYGKEKKTVQnfnkinEQLRvsatKAD-TFSAFIFPSM--- 271
Cdd:PTZ00243 1113 RLMQFYNSANREiRRIKSVAKspVFTLLEEALQGSATITAYGKAHLVMQ------EALR----RLDvVYSCSYLENVanr 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 272 ------NFINNLGMGLV--IGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERVFEIMDEV-- 341
Cdd:PTZ00243 1183 wlgvrvEFLSNIVVTVIalIGVIGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVph 1262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 342 ---PEIKNKKDAF-------------VV-----------QNLQ-GHVALENVSFGYEEN-KTILKEVSLKARPGETIALV 392
Cdd:PTZ00243 1263 edmPELDEEVDALerrtgmaadvtgtVViepasptsaapHPVQaGSLVFEGVQMRYREGlPLVLRGVSFRIAPREKVGIV 1342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 393 GPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIRyGRLDASDEEVINAAKA 472
Cdd:PTZ00243 1343 GRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALEL 1421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 473 ASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILIL-DEATSNIDTRTELQIQEGLNNLMRDRTSFVI 551
Cdd:PTZ00243 1422 VGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITI 1501
|
490 500 510
....*....|....*....|....*....|....
gi 447166279 552 AHRLKTIEKADQILVIKDGSILEKGNHESLMEDR 585
Cdd:PTZ00243 1502 AHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
362-570 |
1.02e-36 |
|
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: 134.29 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQ 441
Cdd:cd00267 2 IENLSFRYGG-RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 dtylfagtimdnirygrldasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILADADILILD 521
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447166279 522 EATSNIDTRTELQIQEGLNNLMRD-RTSFVIAHRLKTIEKA-DQILVIKDG 570
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
360-582 |
1.36e-36 |
|
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: 137.10 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVV 439
Cdd:COG1120 2 LEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYL-FAGTIMDNIRYGR---------LDASDEEVINAAKAASAhsfIKHLPNQYETkiasegsNLSQGQKQLLAIAR 509
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAVEEALERTG---LEHLADRPVD-------ELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 510 AILADADILILDEATSNIDTRTELQIQEGLNNL--MRDRTSFVIAH------RLktiekADQILVIKDGSILEKGNHESL 581
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHdlnlaaRY-----ADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 447166279 582 M 582
Cdd:COG1120 226 L 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
360-574 |
1.71e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 135.94 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGY---EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSL---- 432
Cdd:COG1136 5 LELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 433 RSKIGVVLQDTYLFAG-TIMDNI----RYGRLDASDEEvinaAKAASA------HSFIKHLPNQyetkiasegsnLSQGQ 501
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENValplLLAGVSRKERR----ERARELlervglGDRLDHRPSQ-----------LSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 502 KQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR-TSFVIA-HRLKTIEKADQILVIKDGSILE 574
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
360-584 |
1.71e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 142.73 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENK----TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDMNSL 432
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 433 RSKIGVVLQDTY--LFAG-TIMDNIRYG---RLDASDEEVinAAKAASA-------HSFIKHLPNQyetkiasegsnLSQ 499
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAEPlrlHGLLSRAER--RERVAELlervglpPDLADRYPHE-----------LSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 500 GQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIEK-ADQILVIKDGSILEKG 576
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
....*...
gi 447166279 577 NHESLMED 584
Cdd:COG1123 488 PTEEVFAN 495
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
358-589 |
1.77e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 146.42 E-value: 1.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 358 GHVALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKI 436
Cdd:PLN03130 1236 GSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAGTIMDNirygrLDA----SDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAIL 512
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFN-----LDPfnehNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 513 ADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMEDRGFYF 589
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAF 1467
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
360-572 |
1.15e-35 |
|
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: 131.75 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEyDMNSLRSKIGVV 439
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFAG-TIMDNIRYgrldasdeevinaakaasahsfikhlpnqyetkiasegsnlSQGQKQLLAIARAILADADIL 518
Cdd:cd03230 79 PEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 519 ILDEATSNIDTRTELQIQEGLNNLMRD-RTSFVIAHRLKTIEK-ADQILVIKDGSI 572
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
360-571 |
2.51e-35 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 131.82 E-value: 2.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKT----ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeydmnslrsk 435
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 IGVVLQDTYLFAGTIMDNIRYGR-LDASD-EEVInaaKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKpFDEERyEKVI---KACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 514 DADILILDEATSNIDTRTELQIQEG--LNNLMRDRTSFVIAHRLKTIEKADQILVIKDGS 571
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
360-584 |
6.48e-35 |
|
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: 138.50 E-value: 6.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEEN-KTILKEVSLKARPGETIALVGPTGSGKTTI---INLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSK 435
Cdd:COG1123 5 LEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLalaLMGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 IGVVLQD--TYLFAGTIMDNIRYG--RLDASDEEVINAAKAASAHSFIKHLPNQYEtkiasegSNLSQGQKQLLAIARAI 511
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 512 LADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTI-EKADQILVIKDGSILEKGNHESLMED 584
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
362-576 |
1.01e-34 |
|
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: 131.09 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENK---TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYD---MNSLRSK 435
Cdd:cd03257 4 VKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 IGVVLQDTY-----LFagTIMDNIrygrldasdEEVINAAKAASAHSFIK----------HLPNQYETKIASEgsnLSQG 500
Cdd:cd03257 84 IQMVFQDPMsslnpRM--TIGEQI---------AEPLRIHGKLSKKEARKeavllllvgvGLPEEVLNRYPHE---LSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 501 QKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR-TSFV-IAHRLKTIEK-ADQILVIKDGSILEKG 576
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELgLTLLfITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
360-574 |
2.31e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.79 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKN---IKEYDMNSLRSKI 436
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAG-TIMDNIRY-----GRLDASDEEVINAA--------KAasahsfiKHLPNQyetkiasegsnLSQGQK 502
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALplrvtGKSRKEIRRRVREVldlvglsdKA-------KALPHE-----------LSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 503 QLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIA-HRLKTIEKADQ-ILVIKDGSILE 574
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
360-574 |
2.80e-34 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 130.31 E-value: 2.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGY---EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKI 436
Cdd:COG1124 2 LEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYL-------FAGTIMDNIRYGRLDASDEEVINAAKAAS-AHSFIKHLPNQyetkiasegsnLSQGQKQLLAIA 508
Cdd:COG1124 82 QMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPHQ-----------LSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 509 RAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIEK-ADQILVIKDGSILE 574
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVE 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
360-572 |
2.43e-33 |
|
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: 126.84 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKT---ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSL---- 432
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 433 RSKIGVVLQDTYLFAG-TIMDNIRY-----GRLDASDEEVINAA--KAASAHSfIKHLPNQyetkiasegsnLSQGQKQL 504
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEELleRVGLGDR-LNHYPSE-----------LSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 505 LAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR-TSFVIA-HRLKTIEKADQILVIKDGSI 572
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
360-582 |
1.78e-32 |
|
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: 125.11 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVV 439
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFAG-TIMDNIR-YGRLDASDEEVInAAKAASAHSFIKHLPNQYETKIASEgsnLSQGQKQLLAIARAILADADI 517
Cdd:cd03295 81 IQQIGLFPHmTVEENIAlVPKLLKWPKEKI-RERADELLALVGLDPAEFADRYPHE---LSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 518 LILDEATSNIDTRTELQIQEGLNNLMRD--RTSFVIAHRL-KTIEKADQILVIKDGSILEKGNHESLM 582
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
362-570 |
1.83e-32 |
|
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: 123.07 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNS--LRSKIGVV 439
Cdd:cd03229 3 LKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFAG-TIMDNIRYGrldasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILADADIL 518
Cdd:cd03229 82 FQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 519 ILDEATSNIDTRTELQIQEGLNNL--MRDRTSFVIAHRLKTIEK-ADQILVIKDG 570
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
360-567 |
3.79e-32 |
|
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: 123.74 E-value: 3.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEEN---KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEydmnsLRSKI 436
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFA-GTIMDNIRYG----RLDASD--EEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIAR 509
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqGVPKAEarERAEELLELVGLSGFENAYPHQ-----------LSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHrlkTIEKA----DQILVI 567
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTH---DIDEAvflaDRVVVL 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
361-576 |
6.64e-32 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 121.39 E-value: 6.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 361 ALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVL 440
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 441 QdtylfagtIMDnirygRLDASDEevinaakaasAHSFIkhlpnqyetkiasegSNLSQGQKQLLAIARAILADADILIL 520
Cdd:cd03214 80 Q--------ALE-----LLGLAHL----------ADRPF---------------NELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 521 DEATSNIDTRTELQIQEGLNNLMRDRTSFVIA--HRLK-TIEKADQILVIKDGSILEKG 576
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMvlHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
41-334 |
9.01e-32 |
|
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: 124.89 E-value: 9.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 41 AALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIvpkdLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDI 120
Cdd:cd18577 11 AGAALPLMTIVFGDLFDAFTDFGSGESSPDEF----LDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 121 FEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFI-GVAIAmFALDWILAIVTLITVPIMFFVTK 199
Cdd:cd18577 87 LKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIaGFIIA-FIYSWKLTLVLLATLPLIAIVGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 200 KLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGM 279
Cdd:cd18577 166 IMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMY 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 280 GLVIGTGSVMVLNGMTTVG-VIAAFIN-----YSrqfsrpLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18577 246 ALAFWYGSRLVRDGEISPGdVLTVFFAvligaFS------LGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
358-588 |
1.01e-31 |
|
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: 124.20 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 358 GHVALENVSFGY-EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQqGQIHIDGKNIKEYDMNSLRSKI 436
Cdd:cd03289 1 GQMTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAGTIMDNIR-YGRLdaSDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 516 DILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMEDRGFY 588
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
362-576 |
1.27e-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: 121.86 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeyDMNSLRSKIGVVLQ 441
Cdd:cd03259 3 LKGLSKTYGS-VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFAG-TIMDNIRYG-RLDASDEEVINAAKAASA-----HSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILAD 514
Cdd:cd03259 80 DYALFPHlTVAENIAFGlKLRGVPKAEIRARVRELLelvglEGLLNRYPHE-----------LSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRL-KTIEKADQILVIKDGSILEKG 576
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
362-572 |
2.45e-31 |
|
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: 120.82 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDmnsLRSKIGVVLQ 441
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DT--YLFAGTIMDNIRYGRLDASD-----EEV---INAAKAASAHSFIkhlpnqyetkiasegsnLSQGQKQLLAIARAI 511
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAgneqaETVlkdLDLYALKERHPLS-----------------LSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 512 LADADILILDEATSNIDTRTELQIQEGLNNLM-RDRTSFVIAHRLKTIEK-ADQILVIKDGSI 572
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
360-583 |
2.80e-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: 121.63 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDMNSLRSKI 436
Cdd:COG1127 6 IEVRNLTKSFGD-RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAG-TIMDNI-----RYGRLDAS--DEEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIA 508
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVafplrEHTDLSEAeiRELVLEKLELVGLPGAADKMPSE-----------LSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 509 RAILADADILILDEATSNIDTRTELQIqeglNNLMRDR------TSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESL 581
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVI----DELIRELrdelglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 447166279 582 ME 583
Cdd:COG1127 230 LA 231
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
47-334 |
3.70e-31 |
|
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: 122.65 E-value: 3.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFEKIQT 126
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 127 LSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLVAYSG 206
Cdd:cd18572 82 QDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 207 KNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGTG 286
Cdd:cd18572 162 KLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 447166279 287 SVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18572 242 GHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
360-572 |
7.50e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.58 E-value: 7.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEydmnsLRSKIGVV 439
Cdd:COG1121 7 IELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYL---FAGTIMDNI---RYG------RLDASDEEVINAA-KAASAHSFIKHlpnqyetKIasegSNLSQGQKQLLA 506
Cdd:COG1121 81 PQRAEVdwdFPITVRDVVlmgRYGrrglfrRPSRADREAVDEAlERVGLEDLADR-------PI----GELSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 507 IARAILADADILILDEATSNIDTRTELQIQEGLNNL-MRDRTSFVIAHRLKTIEK-ADQILVIKDGSI 572
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
362-576 |
3.84e-30 |
|
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: 118.37 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDMNSLRSKIGV 438
Cdd:cd03261 3 LRGLTKSFGG-RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQDTYLFAG-TIMDNI-----RYGRLDAS--DEEVINAAKAASAHSFIKHLPnqyetkiasegSNLSQGQKQLLAIARA 510
Cdd:cd03261 82 LFQSGALFDSlTVFENVafplrEHTRLSEEeiREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 511 ILADADILILDEATSNIDTRTELQIQEGLNNLMR--DRTSFVIAHRLKTIEK-ADQILVIKDGSILEKG 576
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
112-588 |
4.43e-30 |
|
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: 126.56 E-value: 4.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 112 TIQKIRQDIFEKIQTLSLR----FFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGvAIAMFALDWILAIVT 187
Cdd:TIGR01271 952 TLLTVSKRLHEQMLHSVLQapmaVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLG-AIFVVSVLQPYIFIA 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 188 LITVPIMFFVtkkLVAYsgknFAKRQKDLGELNGFIEEAITGADVTTL--------YGKEKKTVQNFNK-IN-------- 250
Cdd:TIGR01271 1031 AIPVAVIFIM---LRAY----FLRTSQQLKQLESEARSPIFSHLITSLkglwtiraFGRQSYFETLFHKaLNlhtanwfl 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 251 --EQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSrplsqfaTLMNTIqaav 328
Cdd:TIGR01271 1104 ylSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVD-------GLMRSV---- 1172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 329 aggERVFEIMD---EVPEIKNK------KDAFVVQNL--------QGHVALENVSFGY-EENKTILKEVSLKARPGETIA 390
Cdd:TIGR01271 1173 ---SRVFKFIDlpqEEPRPSGGggkyqlSTVLVIENPhaqkcwpsGGQMDVQGLTAKYtEAGRAVLQDLSFSVEGGQRVG 1249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 391 LVGPTGSGKTTIINLLTRFYDiQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMDNIR-YGRLdaSDEEVINA 469
Cdd:TIGR01271 1250 LLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDpYEQW--SDEEIWKV 1326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 470 AKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSF 549
Cdd:TIGR01271 1327 AEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVI 1406
|
490 500 510
....*....|....*....|....*....|....*....
gi 447166279 550 VIAHRLKTIEKADQILVIKDGSILEKGNHESLMEDRGFY 588
Cdd:TIGR01271 1407 LSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
47-334 |
6.65e-30 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 119.45 E-value: 6.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIyGVTVFL--------TWLQTFVMVNVALKTIQKIRQ 118
Cdd:cd18554 5 IVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTLDEKVYKLFTII-GIMFFIflilrppvEYYRQYFAQWIANKILYDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 119 DIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFvt 198
Cdd:cd18554 84 DLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYIL-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 199 kkLVAYSGKNFAK----RQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFI 274
Cdd:cd18554 162 --AVKYFFGRLRKltkeRSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 275 NNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18554 240 TDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
362-568 |
8.32e-30 |
|
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: 116.86 E-value: 8.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEydmnsLRSKIGVVLQ 441
Cdd:cd03235 2 VEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYL---FAGTIMDNI---RYG------RLDASDEEVINAAKAASAhsfIKHLPNQyetKIasegSNLSQGQKQLLAIAR 509
Cdd:cd03235 76 RRSIdrdFPISVRDVVlmgLYGhkglfrRLSKADKAKVDEALERVG---LSELADR---QI----GELSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 510 AILADADILILDEATSNIDTRTELQIQEGLNNL-MRDRTSFVIAHRLKTIEK-ADQILVIK 568
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLN 206
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
362-587 |
9.23e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.55 E-value: 9.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVL 440
Cdd:PRK13632 10 VENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 441 Q--DTYLFAGTIMDNIRYG----RLDASDEEVI--NAAKAASAHSFIKHLPnqyetkiasegSNLSQGQKQLLAIARAIL 512
Cdd:PRK13632 90 QnpDNQFIGATVEDDIAFGlenkKVPPKKMKDIidDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 513 ADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIA--HRLKTIEKADQILVIKDGSILEKGNHESLMEDRGF 587
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
359-534 |
3.77e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 116.34 E-value: 3.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 359 HVALENVSFGYEENK---TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEydmnsLRSK 435
Cdd:COG1116 7 ALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 IGVVLQDTYLFA-GTIMDNIRYGrLDASDEEVINAAKAASAH-------SFIKHLPNQyetkiasegsnLSQGQKQLLAI 507
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALG-LELRGVPKAERRERARELlelvglaGFEDAYPHQ-----------LSGGMRQRVAI 149
|
170 180
....*....|....*....|....*....
gi 447166279 508 ARAILADADILILDEATSNID--TRTELQ 534
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDalTRERLQ 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
360-581 |
1.37e-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: 113.83 E-value: 1.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENK---TILKEVSLKARPGETIALVGPTGSGKTT---IINLLTRfYDiqQGQIHIDGKNI---KEYDMN 430
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER-PT--SGSVLVDGTDLtllSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 431 SLRSKIGVVLQDTYLFAG-TIMDNIRYG-RLDASDEEVINAAkaasahsfIKHLPNQ--YETKIASEGSNLSQGQKQLLA 506
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALPlEIAGVPKAEIEER--------VLELLELvgLEDKADAYPAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 507 IARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESL 581
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
360-576 |
1.41e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.11 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTI-LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGV 438
Cdd:PRK13635 6 IRVEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQ--DTYLFAGTIMDNIRYG-------RlDASDEEVINAAKAASAHSFIKHLPnqyetkiasegSNLSQGQKQLLAIAR 509
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFGlenigvpR-EEMVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFV--IAHRLKTIEKADQILVIKDGSILEKG 576
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVlsITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
362-572 |
2.47e-28 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 113.43 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDMNSLRSKIGV 438
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQDTYLFAG-TIMDNIRYGRLdasdeevinaakaaSAHSFIKHLPNQY---ETKIASE--------------GSNLSQG 500
Cdd:cd03256 83 IFQQFNLIERlSVLENVLSGRL--------------GRRSTWRSLFGLFpkeEKQRALAalervglldkayqrADQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 501 QKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIA--HRLKTIEK-ADQILVIKDGSI 572
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVslHQVDLAREyADRIVGLKDGRI 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
360-584 |
4.43e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 113.68 E-value: 4.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVV 439
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQ--DTYLFAGTIMDNIRYG----RLDASD-EEVINAAKAASAHSFIKHLPNQYetkiasegsnLSQGQKQLLAIARAIL 512
Cdd:PRK13647 85 FQdpDDQVFSSTVWDDVAFGpvnmGLDKDEvERRVEEALKAVRMWDFRDKPPYH----------LSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 513 ADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIA-HRLK-TIEKADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
47-307 |
4.81e-28 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 114.15 E-value: 4.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTA-----RMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIF 121
Cdd:cd18573 2 LALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFglslkTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 122 EKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVP---IMFFVT 198
Cdd:cd18573 82 KSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPpiaVGAVFY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 199 KKLVaysgKNFAKR-QKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNL 277
Cdd:cd18573 162 GRYV----RKLSKQvQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNL 237
|
250 260 270
....*....|....*....|....*....|
gi 447166279 278 GMGLVIGTGSVMVLNGMTTVGVIAAFINYS 307
Cdd:cd18573 238 SLLSVLYYGGSLVASGELTVGDLTSFLMYA 267
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
40-522 |
6.33e-28 |
|
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: 117.98 E-value: 6.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 40 KAALTFIIFLVFVTTLLGLLGPYLMGVIIDQyivpkdLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKI--- 116
Cdd:COG4615 9 RESRWLLLLALLLGLLSGLANAGLIALINQA------LNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAvar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 117 -RQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALtQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMF 195
Cdd:COG4615 83 lRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAF-VRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 196 FVTKKLVAYSGKNFAK-RQKDlGELNGFIEEAITGAdvttlygKEKKtvqnFNK------INEQLRVSA-------TKAD 261
Cdd:COG4615 162 AGYRLLVRRARRHLRRaREAE-DRLFKHFRALLEGF-------KELK----LNRrrrrafFDEDLQPTAeryrdlrIRAD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 262 TFSAFIFPSMNFINNLGMGLVIGtgsVMVLNGMTTVGVIAAF---INYSRQfsrPLSQFATLMNTI-QAAVAGG--ERVF 335
Cdd:COG4615 230 TIFALANNWGNLLFFALIGLILF---LLPALGWADPAVLSGFvlvLLFLRG---PLSQLVGALPTLsRANVALRkiEELE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 336 EIMDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKT----ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYD 411
Cdd:COG4615 304 LALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 412 IQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFagtimDNIrYGRLDASDEEVINAakaasahsFIKHLpnQYETKIA 491
Cdd:COG4615 384 PESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DRL-LGLDGEADPARARE--------LLERL--ELDHKVS 447
|
490 500 510
....*....|....*....|....*....|....*.
gi 447166279 492 SEG-----SNLSQGQKQLLAIARAILADADILILDE 522
Cdd:COG4615 448 VEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
364-572 |
1.09e-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: 110.70 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 364 NVSFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTI---INLLTRfydIQQGQIHIDGKNI--KEYDMNSLRSKIGV 438
Cdd:cd03262 7 HKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTIIIDGLKLtdDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQDTYLFAG-TIMDNIRYG---RLDASDEEVINAAKAASAHSFIKHLPNQYEtkiasegSNLSQGQKQLLAIARAILAD 514
Cdd:cd03262 81 VFQQFNLFPHlTVLENITLApikVKGMSKAEAEERALELLEKVGLADKADAYP-------AQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 515 ADILILDEATSNIDtrTELqIQEGLnNLMRD-----RTSFVIAHRLKTIEK-ADQILVIKDGSI 572
Cdd:cd03262 154 PKVMLFDEPTSALD--PEL-VGEVL-DVMKDlaeegMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
362-583 |
1.24e-27 |
|
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: 111.27 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENKtiLKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeyDMNSLRSKIGVVLQ 441
Cdd:cd03299 3 VENLSKDWKEFK--LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFAG-TIMDNIRYG----RLDAS--DEEVINAAKAASahsfIKHLPNQYETKiasegsnLSQGQKQLLAIARAILAD 514
Cdd:cd03299 79 NYALFPHmTVYKNIAYGlkkrKVDKKeiERKVLEIAEMLG----IDHLLNRKPET-------LSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLmRDRTSFVIAHRLKTIEKA----DQILVIKDGSILEKGNHESLME 583
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKI-RKEFGVTVLHVTHDFEEAwalaDKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
40-325 |
1.46e-27 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 112.60 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 40 KAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQD 119
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFV-- 197
Cdd:cd18555 81 FFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLll 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 198 --TKKLVAYSGKNFAKRQKdlgeLNGFIEEAITG-ADVTTLyGKEKKTVQNF-NKINEQLRVSaTKADTFSAFIFPSMNF 273
Cdd:cd18555 160 ltRKKIKKLNQEEIVAQTK----VQSYLTETLYGiETIKSL-GSEKNIYKKWeNLFKKQLKAF-KKKERLSNILNSISSS 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447166279 274 INNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQ 325
Cdd:cd18555 234 IQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFI 285
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
360-576 |
5.61e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.47 E-value: 5.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeyDMNSLRSK---I 436
Cdd:COG3839 4 LELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR-----DVTDLPPKdrnI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDtylFA----GTIMDNIRYG----RLDAS--DEEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLA 506
Cdd:COG3839 78 AMVFQS---YAlyphMTVYENIAFPlklrKVPKAeiDRRVREAAELLGLEDLLDRKPKQ-----------LSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 507 IARAILADADILILDEATSNID------TRTEL-QIQEGLNnlmrdrTSFVIA-H------RLktiekADQILVIKDGSI 572
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrveMRAEIkRLHRRLG------TTTIYVtHdqveamTL-----ADRIAVMNDGRI 212
|
....
gi 447166279 573 LEKG 576
Cdd:COG3839 213 QQVG 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
360-576 |
7.16e-27 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 108.50 E-value: 7.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeyDMNSLRSK---I 436
Cdd:cd03301 1 VELENVTKRFG-NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR-----DVTDLPPKdrdI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAG-TIMDNIRYG-RLDASDEEVINAAKAASAHSF-IKHLPNQYETKiasegsnLSQGQKQLLAIARAILA 513
Cdd:cd03301 75 AMVFQNYALYPHmTVYDNIAFGlKLRKVPKDEIDERVREVAELLqIEHLLDRKPKQ-------LSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 514 DADILILDEATSNIDTRTELQIQEGLNNLMRD---RTSFVIAHRLKTIEKADQILVIKDGSILEKG 576
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgtTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
360-547 |
1.01e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 109.36 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-----QGQIHIDGKNI--KEYDMNSL 432
Cdd:COG1117 12 IEVRNLNVYYGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIydPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 433 RSKIGVVLQDTYLFAGTIMDNIRYG-RL------DASDEEVINAAKAAsahsfikHLPNQYETKIASEGSNLSQGQKQLL 505
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVAYGlRLhgikskSELDEIVEESLRKA-------ALWDEVKDRLKKSALGLSGGQQQRL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447166279 506 AIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRT 547
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYT 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
360-576 |
1.40e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 111.34 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeyDMNSL---RSKI 436
Cdd:COG3842 6 LELENVSKRYGDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR-----DVTGLppeKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDtY-LFAG-TIMDNIRYG-RLDASDEEVInAAKAASA------HSFIKHLPNQyetkiasegsnLSQGQKQLLAI 507
Cdd:COG3842 80 GMVFQD-YaLFPHlTVAENVAFGlRMRGVPKAEI-RARVAELlelvglEGLADRYPHQ-----------LSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 508 ARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR-TSFVIA-H------RLktiekADQILVIKDGSILEKG 576
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgITFIYVtHdqeealAL-----ADRIAVMNDGRIEQVG 218
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
36-344 |
2.88e-26 |
|
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: 109.46 E-value: 2.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 36 MGYQKAALTFIIFLVFVTTLLGLLGP---YLMGVIIDQYIVPKD---LSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVA 109
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPvfaILFSKLISVFSLPDDdelRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 110 LKTIQKIRQDIFEKIqtlsLR----FFD--VRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFI-GVAIAmFALDWI 182
Cdd:cd18578 81 ERLTRRLRKLAFRAI----LRqdiaWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVaGLIIA-FVYGWK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 183 LAIVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADT 262
Cdd:cd18578 156 LALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 263 FSAFIFPSMNFINNLGMGLVIGTGSVMVLNG-MTTVGVIAAF--INYSRQFsrpLSQFATLMNTIQAAVAGGERVFEIMD 339
Cdd:cd18578 236 ISGLGFGLSQSLTFFAYALAFWYGGRLVANGeYTFEQFFIVFmaLIFGAQS---AGQAFSFAPDIAKAKAAAARIFRLLD 312
|
....*
gi 447166279 340 EVPEI 344
Cdd:cd18578 313 RKPEI 317
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
40-334 |
3.29e-26 |
|
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: 108.83 E-value: 3.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 40 KAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQD 119
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTK 199
Cdd:cd18782 81 IIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 200 kLVAYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKKTVQNF-----NKINEQLRVSATKAdTFSAFIFpsmnF 273
Cdd:cd18782 160 -LFGPILRRQIRRRAEAsAKTQSYLVESLTGIQTVKAQNAELKARWRWqnryaRSLGEGFKLTVLGT-TSGSLSQ----F 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 274 INNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18782 234 LNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
360-584 |
5.82e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.96 E-value: 5.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTI---INLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSK 435
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTIsklINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 IGVVLQ--DTYLFAGTIMDNIRYG---RLDASDEEVINAAKAASAHSFIKHlpnqyetkIASEGSNLSQGQKQLLAIARA 510
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGlenRAVPRPEMIKIVRDVLADVGMLDY--------IDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 511 ILADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
46-307 |
8.39e-26 |
|
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: 107.57 E-value: 8.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 46 IIFLVFVTTLLGLLgPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFEKIQ 125
Cdd:cd18575 2 LIALLIAAAATLAL-GQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 126 TLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPI----MFFVTKKL 201
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLvvlpIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 202 VAYSgknfAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGL 281
Cdd:cd18575 161 RRLS----RASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVF 236
|
250 260
....*....|....*....|....*.
gi 447166279 282 VIGTGSVMVLNGMTTVGVIAAFINYS 307
Cdd:cd18575 237 VLWLGAHDVLAGRMSAGELSQFVFYA 262
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
373-573 |
2.10e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 104.51 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeYDMNSLRSKIGVVLQDTYLFAG-TIM 451
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYCPQFDALFDElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 452 DNIR-YGRLDASDEEVINaakaASAHSFIKHL-PNQYETKIAsegSNLSQGQKQLLAIARAILADADILILDEATSNIDT 529
Cdd:cd03263 94 EHLRfYARLKGLPKSEIK----EEVELLLRVLgLTDKANKRA---RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447166279 530 RTELQIQEGLNNLMRDRTSFVIAHRLKTIEK-ADQILVIKDGSIL 573
Cdd:cd03263 167 ASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
360-583 |
2.65e-25 |
|
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: 104.63 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNslRSKIGVV 439
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFAG-TIMDNIRYG-RLDASDEEVINaAKAASAHSFIKHLpnQYETKIASEgsnLSQGQKQLLAIARAILADADI 517
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlRLKKLPKAEIK-ERVAEALDLVQLE--GYANRKPSQ---LSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 518 LILDEATSNIDTRTELQIQEGLNNLMRD-RTSFV-IAH-RLKTIEKADQILVIKDGSILEKGNHESLME 583
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVfVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
360-582 |
3.92e-25 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 104.40 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRfyDIQQG---QIHIDGKNIKEYDMNSLRSKI 436
Cdd:COG1119 4 LELRNVTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG--DLPPTygnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVV---LQDTYL------------FAGTImdniryGRLDASDEEVINAAKAASAHSFIKHLPNQ-YETkiasegsnLSQG 500
Cdd:COG1119 81 GLVspaLQLRFPrdetvldvvlsgFFDSI------GLYREPTDEQRERARELLELLGLAHLADRpFGT--------LSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 501 QKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR-TSFV-IAHRLKTI-EKADQILVIKDGSILEKGN 577
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVlVTHHVEEIpPGITHVLLLKDGRVVAAGP 226
|
....*
gi 447166279 578 HESLM 582
Cdd:COG1119 227 KEEVL 231
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
362-582 |
4.03e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.07 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEEnktILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeyDMNSLRSKIGVVLQ 441
Cdd:COG3840 4 LDDLTYRYGD---FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT--ALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFAG-TIMDNIRYG-----RLDASD-EEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILAD 514
Cdd:COG3840 79 ENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 515 ADILILDEATSNIDT--RTE-LQIqegLNNLMRDR--TSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESLM 582
Cdd:COG3840 148 RPILLLDEPFSALDPalRQEmLDL---VDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
376-570 |
7.70e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.18 E-value: 7.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGK-----NIKEydmnSLRSKIGVVLQDTYLFAG-T 449
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrSPRD----AQAAGIAIIHQELNLVPNlS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 450 IMDNI-------RYGRLDasDEEVINAAKAAsahsfIKHL-----PNqyeTKIasegSNLSQGQKQLLAIARAILADADI 517
Cdd:COG1129 96 VAENIflgreprRGGLID--WRAMRRRAREL-----LARLgldidPD---TPV----GDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 518 LILDEATSNIdTRTELQIqegLNNLMRD----RTSFV-IAHRLKTIEK-ADQILVIKDG 570
Cdd:COG1129 162 LILDEPTASL-TEREVER---LFRIIRRlkaqGVAIIyISHRLDEVFEiADRVTVLRDG 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
376-583 |
1.24e-24 |
|
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: 103.49 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSL----RSKIGVVLQDTYLFAG-TI 450
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 451 MDNIRYGRLDASDEEVINAAKAASA------HSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEAlelvglEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166279 525 SNIDTRTELQIQEGLNNLMRD--RTSFVIAHRL-KTIEKADQILVIKDGSILEKGNHESLME 583
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
362-584 |
1.33e-24 |
|
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: 102.13 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDMNslRSKIGV 438
Cdd:cd03224 3 VENLNAGYGKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglPPHERA--RAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQDTYLFAG-TIMDNIR---YGRLDASDEEVINAAKAAsahsfikhLPNQYEtKIASEGSNLSQGQKQLLAIARAILAD 514
Cdd:cd03224 80 VPEGRRIFPElTVEENLLlgaYARRRAKRKARLERVYEL--------FPRLKE-RRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVI----AHRLKTIekADQILVIKDGSILEKGNHESLMED 584
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLAD 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
364-584 |
2.37e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.85 E-value: 2.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 364 NVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeYDMNSL---RSKIGVVL 440
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 441 Q--DTYLFAGTIMDNIRYGRL------DASDEEVINAAKAASAHSFIKHLPNqyetkiasegsNLSQGQKQLLAIARAIL 512
Cdd:PRK13639 85 QnpDDQLFAPTVEEDVAFGPLnlglskEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 513 ADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIA-HRLKTIEK-ADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
373-576 |
2.78e-24 |
|
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: 100.32 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLT--RFYDIQQGQIHIDGKNIkeyDMNSLRSKIGVVLQDTYLFAG-T 449
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTlT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 450 IMDNIRYgrldasdeevinaakaasahsfikhlpnqyetkiASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDT 529
Cdd:cd03213 99 VRETLMF----------------------------------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447166279 530 RTELQIQEGLNNLMRD-RTSFVIAHRLKT--IEKADQILVIKDGSILEKG 576
Cdd:cd03213 145 SSALQVMSLLRRLADTgRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
362-569 |
5.47e-24 |
|
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: 99.86 E-value: 5.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEyDMNSLRSKIGVVLQ 441
Cdd:COG4133 5 AENLSCRRGE-RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFAG-TIMDNIRY----GRLDASDEEVINAAKAASAHSFIkHLPnqyetkiaseGSNLSQGQKQLLAIARAILADAD 516
Cdd:COG4133 83 ADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGLA-DLP----------VRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447166279 517 ILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIA-HRLKTIEkADQILVIKD 569
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELA-AARVLDLGD 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
362-577 |
6.89e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.05 E-value: 6.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEEN----KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI--KEYDMNSLRSK 435
Cdd:PRK13637 5 IENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 IGVVLQ--DTYLFAGTIMDNIRYG--RLDASDEEVINAAKAAsahsfIKHLPNQYETKIASEGSNLSQGQKQLLAIARAI 511
Cdd:PRK13637 85 VGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 512 LADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIEK-ADQILVIKDGSILEKGN 577
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
372-576 |
2.14e-23 |
|
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: 98.44 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeyDMNSLRSKIGVVLQDTYLFAG-TI 450
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 451 MDNIR-----YGRLDASDEEVINaakaasahsfIKHLPNQYETKIASegsnLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:cd03268 90 RENLRllarlLGIRKKRIDEVLD----------VVGLKDSAKKKVKG----FSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447166279 526 NIDTRTELQIQEGLNNLMRDRTSFVIA-HRLKTIEK-ADQILVIKDGSILEKG 576
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
376-584 |
2.45e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 104.00 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTT----IINLLTrfydiQQGQIHIDGKNI---KEYDMNSLRSKIGVVLQDTYlfaG 448
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIP-----SEGEIRFDGQDLdglSRRALRPLRRRMQVVFQDPF---G 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 449 ------TIMDNIRYG------RLDASD-EEVINAA------KAASAHSFikhlPNQyetkiasegsnLSQGQKQLLAIAR 509
Cdd:COG4172 374 slsprmTVGQIIAEGlrvhgpGLSAAErRARVAEAleevglDPAARHRY----PHE-----------FSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMRDR-TSFV-IAHRLKTIEK-ADQILVIKDGSILEKGNHESLMED 584
Cdd:COG4172 439 ALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHgLAYLfISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
360-572 |
2.54e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.19 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKT--ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIG 437
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 438 VVLQ--DTYLFAGTIMDNIRYG------RLDASDEEVINAAKAASAHSFIKHLPnqyetkiasegSNLSQGQKQLLAIAR 509
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
40-311 |
2.66e-23 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 100.23 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 40 KAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQD 119
Cdd:cd18567 1 KRALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVtk 199
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALL-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 200 KLVAYSgknfakRQKDLGEL--------NGFIEEAITGADVTTLYGKE---KKTVQNF--NKINEQLRVSatKADTFSAF 266
Cdd:cd18567 158 RLALYP------PLRRATEEqivasakeQSHFLETIRGIQTIKLFGREaerEARWLNLlvDAINADIRLQ--RLQILFSA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 447166279 267 IfpsMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFS 311
Cdd:cd18567 230 A---NGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFS 271
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
46-334 |
4.37e-23 |
|
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: 99.63 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 46 IIFLVfVTTLLGLLGPYLMGVIIDqyIVPKDLSGT--------ARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIR 117
Cdd:cd18780 2 TIALL-VSSGTNLALPYFFGQVID--AVTNHSGSGgeealralNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 118 QDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFV 197
Cdd:cd18780 79 KRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 198 TkklVAYSG--KNFAKRQKD-LGELNGFIEEAITGADVTTLYGKEKKTVQNFN-KINEQLRVSATKADTFSAFiFPSMNF 273
Cdd:cd18780 159 A---VIYGKyvRKLSKKFQDaLAAASTVAEESISNIRTVRSFAKETKEVSRYSeKINESYLLGKKLARASGGF-NGFMGA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 274 INNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18780 235 AAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
369-577 |
4.96e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.69 E-value: 4.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 369 YEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-----QGQIHIDGKNI--KEYDMNSLRSKIGVVLQ 441
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFAGTIMDNIRYG-RLDA-SDEEVINAA-----KAASahsfikhLPNQYETKIASEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK14239 94 QPNPFPMSIYENVVYGlRLKGiKDKQVLDEAvekslKGAS-------IWDEVKDRLHDSALGLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEK-ADQILVIKDGSILEKGN 577
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
376-576 |
6.14e-23 |
|
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: 97.89 E-value: 6.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNsLRSKIGVV--LQDTYLFAG-TIMD 452
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGrtFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 453 NIRYGRLDASDEEVINAAKAAS-------AHSFIK--HLPNQYETKIAsegsNLSQGQKQLLAIARAILADADILILDEA 523
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREerearerAEELLErvGLADLADRPAG----ELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 524 TS--NIDTRTEL-QIQEGLNNlmRDRTSFVIAHRLKTIEK-ADQILVIKDGSILEKG 576
Cdd:cd03219 171 AAglNPEETEELaELIRELRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEG 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
363-556 |
9.97e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.93 E-value: 9.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 363 ENVSFgYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDI-----QQGQIHIDGKNI--KEYDMNSLRSK 435
Cdd:PRK14243 14 ENLNV-YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVEVRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 IGVVLQDTYLFAGTIMDNIRYG-RLDAS----DEEVINAAKAASahsfikhLPNQYETKIASEGSNLSQGQKQLLAIARA 510
Cdd:PRK14243 93 IGMVFQKPNPFPKSIYDNIAYGaRINGYkgdmDELVERSLRQAA-------LWDEVKDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447166279 511 ILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLK 556
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
360-584 |
1.31e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.09 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVS--FGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIK--EYDMNSLRSK 435
Cdd:PRK09493 2 IEFKNVSkhFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 IGVVLQDTYLFAG-TIMDNIRYGRLD---ASDEEVINAAK--------AASAHsfikHLPnqyetkiasegSNLSQGQKQ 503
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFGPLRvrgASKEEAEKQARellakvglAERAH----HYP-----------SELSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 504 LLAIARAILADADILILDEATSNIDtrTELQiQEGLnNLMRD-----RTSFVIAHRLKTIEK-ADQILVIKDGSILEKGN 577
Cdd:PRK09493 144 RVAIARALAVKPKLMLFDEPTSALD--PELR-HEVL-KVMQDlaeegMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGD 219
|
....*..
gi 447166279 578 HESLMED 584
Cdd:PRK09493 220 PQVLIKN 226
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
360-570 |
3.59e-22 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 93.26 E-value: 3.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENV--SFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikEYDMNS----LR 433
Cdd:cd03216 1 LELRGItkRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK---EVSFASprdaRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 434 SKIGVVLQdtylfagtimdnirygrldasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILA 513
Cdd:cd03216 75 AGIAMVYQ-------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 514 DADILILDEATSNIDTRtelQIQEgLNNLMRDRT----SFV-IAHRLKTI-EKADQILVIKDG 570
Cdd:cd03216 100 NARLLILDEPTAALTPA---EVER-LFKVIRRLRaqgvAVIfISHRLDEVfEIADRVTVLRDG 158
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
379-584 |
3.95e-22 |
|
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: 97.43 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 379 VSLKARPGETIALVGPTGSGKTTIINLLTRFYD---IQQGQIHIDGKNI---KEYDMNSLRSK-IGVVLQDTYlfagT-- 449
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLlklSEKELRKIRGReIQMIFQDPM----Tsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 450 ---------IMDNIRYGRlDASDEEVINAAKAA-------SAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILA 513
Cdd:COG0444 100 npvmtvgdqIAEPLRIHG-GLSKAEARERAIELlervglpDPERRLDRYPHE-----------LSGGMRQRVMIARALAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 514 DADILILDEATSNIDTRTELQIQEGLNNLMRDR-TSFV-IAHRLKTIEK-ADQILVIKDGSILEKGNHESLMED 584
Cdd:COG0444 168 EPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLAILfITHDLGVVAEiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
360-577 |
4.63e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.87 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-----QGQIHIDGKNIKE--YDMNSL 432
Cdd:PRK14258 8 IKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYErrVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 433 RSKIGVVLQDTYLFAGTIMDNIRYG--------RLDAsDEEVINAAKAASAHSFIKHlpnqyetKIASEGSNLSQGQKQL 504
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrpKLEI-DDIVESALKDADLWDEIKH-------KIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 505 LAIARAILADADILILDEATSNIDTRTELQIQEGLNNL-MRDRTSFVI-AHRLKtiekadQILVIKDGSILEKGN 577
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIvSHNLH------QVSRLSDFTAFFKGN 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
136-581 |
5.85e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 101.21 E-value: 5.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 136 SQGDLMSRVTNDIDNLNQ------ALTQSVVQIISSALTF---IGVAiAMFAldwilAIVTLITVPIMFFVTKKLVAYSG 206
Cdd:PLN03232 396 ASGKVTNMITTDANALQQiaeqlhGLWSAPFRIIVSMVLLyqqLGVA-SLFG-----SLILFLLIPLQTLIVRKMRKLTK 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 207 KNFAKRQKDLGELNgfieEAITGADVTTLYGKEKKTVQNFNKI-NEQLRV--SATKADTFSAFIFPSMNFINNLgmglvI 283
Cdd:PLN03232 470 EGLQWTDKRVGIIN----EILASMDTVKCYAWEKSFESRIQGIrNEELSWfrKAQLLSAFNSFILNSIPVVVTL-----V 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 284 GTGSVMVLNGMTTVGviAAFINYS--RQFSRPLSQFATLMNTIQAAVAGGERVFE-------IMDEVPEIKNKKDAFVVQ 354
Cdd:PLN03232 541 SFGVFVLLGGDLTPA--RAFTSLSlfAVLRSPLNMLPNLLSQVVNANVSLQRIEElllseerILAQNPPLQPGAPAISIK 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 355 NlqghvalENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTrfydiqqGQI-HIDGKNIkeydmnSLR 433
Cdd:PLN03232 619 N-------GYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML-------GELsHAETSSV------VIR 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 434 SKIGVVLQDTYLFAGTIMDNIRYGRlDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:PLN03232 679 GSVAYVPQVSWIFNATVRENILFGS-DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYS 757
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 514 DADILILDEATSNIDTRTELQIQEG-LNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESL 581
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
362-576 |
6.23e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 97.52 E-value: 6.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeYDMNSLRSKIGVVLQ 441
Cdd:COG1118 5 VRNISKRFG-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFAG-TIMDNIRYG--RLDASDEEVinAAKAAS------AHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAIL 512
Cdd:COG1118 83 HYALFPHmTVAENIAFGlrVRPPSKAEI--RARVEEllelvqLEGLADRYPSQ-----------LSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 513 ADADILILDEATSNIDT--RTELQIQegLNNLMRD--RTS-FVI-----AHRLktiekADQILVIKDGSILEKG 576
Cdd:COG1118 150 VEPEVLLLDEPFGALDAkvRKELRRW--LRRLHDElgGTTvFVThdqeeALEL-----ADRVVVMNQGRIEQVG 216
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
360-572 |
1.37e-21 |
|
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: 93.24 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNS---LRSKI 436
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAG-TIMDNIRYGR--LDASDEEVINAAKAASAHSFIKHlpnqyetKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFALevTGVPPREIRKRVPAALELVGLSH-------KHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 514 DADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQ--ILVIKDGSI 572
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
362-582 |
2.09e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.93 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQ 441
Cdd:PRK11231 5 TENLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFAG-TIMDNIRYGR---------LDASDEEVINAAKAASAhsfIKHLPNQYETkiasegsNLSQGQKQLLAIARAI 511
Cdd:PRK11231 84 HHLTPEGiTVRELVAYGRspwlslwgrLSAEDNARVNQAMEQTR---INHLADRRLT-------DLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 512 LADADILILDEATSNIDtrteLQIQEGLNNLMRD-----RTSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESLM 582
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLD----INHQVELMRLMRElntqgKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
385-576 |
3.06e-21 |
|
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: 92.36 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 385 PGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDG-------KNIkeyDMNSLRSKIGVVLQDTYLFAG-TIMDNIRY 456
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKI---NLPPQQRKIGLVFQQYALFPHlNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 457 GRLDASDEEVINAAKAASAHSFIKHLPNQYETKiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQ 536
Cdd:cd03297 99 GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQ-------LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447166279 537 EGLNNLMRD--RTSFVIAHRLKTIEK-ADQILVIKDGSILEKG 576
Cdd:cd03297 172 PELKQIKKNlnIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
375-585 |
3.23e-21 |
|
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: 94.15 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 375 ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeydmnslrskIGVVLQDTYLFAGTIMDNI 454
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 455 RYGrLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQ 534
Cdd:cd03291 119 IFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447166279 535 IQEG-LNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMEDR 585
Cdd:cd03291 198 IFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
362-524 |
3.73e-21 |
|
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: 92.74 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSL-RSKIGVVL 440
Cdd:COG0410 6 VENLHAGYGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 441 QDTYLFAG-TIMDNIRYGRLDASDEEVINAAKAASAHSFikhlPNQYEtKIASEGSNLSQGQKQLLAIARAILADADILI 519
Cdd:COG0410 85 EGRRIFPSlTVEENLLLGAYARRDRAEVRADLERVYELF----PRLKE-RRRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
....*
gi 447166279 520 LDEAT 524
Cdd:COG0410 160 LDEPS 164
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
43-571 |
3.77e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 97.19 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQyIVPKDLSG----TARMCLLLIAIYGVTVFLTWLQtfvmvnvalktiqkirq 118
Cdd:COG4178 27 LALLLLLTLASVGLNVLLNFWNRDFYDA-LQARDAAAfwqqLGVFALLAAISILLAVYQTYLR----------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 119 difekiQTLSLR------------------FFDVRSQGDLMS----RVTNDIDNL-NQALT------QSVVQIIS----- 164
Cdd:COG4178 89 ------QRLQIRwrewlterlldrwlsnraYYRLQLSGGEIDnpdqRIAEDIRLFtETTLSlslgllSSVVTLISfigil 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 165 ------SALTFIGVAIA----MFaldWILAIVTLITVPIMFFVTKKLVaysGKNFAKRQK--DL-GEL-----NGfieEA 226
Cdd:COG4178 163 wslsgsLTFTLGGYSITipgyMV---WAALIYAIIGTLLTHLIGRPLI---RLNFEQQRReaDFrFALvrvreNA---ES 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 227 ITgadvttLYG---KEKKT--------VQNFNK-INEQLRVSA-TKADTFSAFIFPSmnfinnlgmgLVIgtgSVMVLNG 293
Cdd:COG4178 234 IA------LYRgeaAERRRlrrrfdavIANWRRlIRRQRNLTFfTTGYGQLAVIFPI----------LVA---APRYFAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 294 MTTVGVI----AAFinysRQFSRPLSQFATLMNTIQAAVAGGERV--FEIMDEVPEIKNKKDAFVVQNLQGHVALENVSF 367
Cdd:COG4178 295 EITLGGLmqaaSAF----GQVQGALSWFVDNYQSLAEWRATVDRLagFEEALEAADALPEAASRIETSEDGALALEDLTL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 368 GYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHI-DGKNIkeydmnslrskigVVL-QDTYL 445
Cdd:COG4178 371 RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------------LFLpQRPYL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 446 FAGTIMDNIRY--GRLDASDEEVINAAKAASahsfIKHLPNQYETKiASEGSNLSQGQKQLLAIARAILADADILILDEA 523
Cdd:COG4178 438 PLGTLREALLYpaTAEAFSDAELREALEAVG----LGHLAERLDEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 447166279 524 TSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGS 571
Cdd:COG4178 513 TSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
364-572 |
4.26e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.15 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 364 NVSFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEydMNSLRSKIGVVLQDT 443
Cdd:PRK10851 9 KKSFG---RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARDRKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 444 YLFAG-TIMDNIRYG-----RLDASDEEVINaAKAASAHSFIK--HLPNQYEtkiasegSNLSQGQKQLLAIARAILADA 515
Cdd:PRK10851 84 ALFRHmTVFDNIAFGltvlpRRERPNAAAIK-AKVTQLLEMVQlaHLADRYP-------AQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 516 DILILDEATSNIDT--RTEL-----QIQEGLNnlmrdRTS-FVIAHRLKTIEKADQILVIKDGSI 572
Cdd:PRK10851 156 QILLLDEPFGALDAqvRKELrrwlrQLHEELK-----FTSvFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
360-581 |
4.51e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 93.62 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDI-----QQGQIHIDGKNIKEY-DMNSLR 433
Cdd:PRK14271 22 MAAVNLTLGFA-GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 434 SKIGVVLQDTYLFAGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:PRK14271 101 RRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 514 DADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESL 581
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
359-577 |
4.62e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 94.76 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 359 HVALENVSFGYEENK---TILKEVSLKARPGETIALVGPTGSGKTT---IINLLTRFydiQQGQIHIDGKNIKEYDMNSL 432
Cdd:COG1135 1 MIELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLERP---TSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 433 ---RSKIGVVLQDTYLFAG-TIMDNIRYG-RLDASDEEVInAAKAAS----------AHSFikhlPNQyetkiasegsnL 497
Cdd:COG1135 78 raaRRKIGMIFQHFNLLSSrTVAENVALPlEIAGVPKAEI-RKRVAEllelvglsdkADAY----PSQ-----------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 498 SQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLmRDR---TSFVIAHRLKTIEK-ADQILVIKDGSIL 573
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI-NRElglTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
....
gi 447166279 574 EKGN 577
Cdd:COG1135 221 EQGP 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
362-574 |
5.11e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 96.96 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQ 441
Cdd:PRK10522 325 LRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFagtimdniryGRLDASDEEvinAAKAASAHSFIKHLpnQYETKIASEGS-----NLSQGQKQLLAIARAILADAD 516
Cdd:PRK10522 405 DFHLF----------DQLLGPEGK---PANPALVEKWLERL--KMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 517 ILILDEATSNIDTRTELQIQEGLNNLMRD--RTSFVIAHRLKTIEKADQILVIKDGSILE 574
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
360-576 |
6.56e-21 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 91.10 E-value: 6.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEeNKTILKEVSLKARPGeTIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEyDMNSLRSKIGVV 439
Cdd:cd03264 1 LQLENLTKRYG-KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFAG-TIMDNIRY---------GRLDASDEEVINAAkaasahsfikHLPNQYETKIASegsnLSQGQKQLLAIAR 509
Cdd:cd03264 78 PQEFGVYPNfTVREFLDYiawlkgipsKEVKARVDEVLELV----------NLGDRAKKKIGS----LSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEK-ADQILVIKDGSILEKG 576
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
360-576 |
7.10e-21 |
|
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: 91.40 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTILkevSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEydMNSLRSKIGVV 439
Cdd:cd03298 1 VRLDKIRFSYGEQPMHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFAG-TIMDNIRYG-----RLDASDEEVINAAKAASA-HSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAIL 512
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGlspglKLTAEDRQAIEVALARVGlAGLEKRLPGE-----------LSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 513 ADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIEK-ADQILVIKDGSILEKG 576
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-584 |
7.88e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.21 E-value: 7.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 361 ALENVSFG-YEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ-----GQIHIDGKNIKEYDMNSL-- 432
Cdd:PRK14267 4 AIETVNLRvYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIev 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 433 RSKIGVVLQDTYLFAG-TIMDNI----RYGRLDAS----DEEVINAAKAASAHSFIKHLPNQYEtkiasegSNLSQGQKQ 503
Cdd:PRK14267 84 RREVGMVFQYPNPFPHlTIYDNVaigvKLNGLVKSkkelDERVEWALKKAALWDEVKDRLNDYP-------SNLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 504 LLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHR-LKTIEKADQILVIKDGSILEKGNHESLM 582
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
..
gi 447166279 583 ED 584
Cdd:PRK14267 237 EN 238
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
40-327 |
8.89e-21 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 92.95 E-value: 8.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 40 KAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNvalkTIQKIrqD 119
Cdd:cd18588 1 KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSH----TTNRI--D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 120 I------FEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTqsvvqiiSSALT------FIGVAIA-MFALDWILAIV 186
Cdd:cd18588 75 AelgarlFRHLLRLPLSYFESRQVGDTVARV-RELESIRQFLT-------GSALTlvldlvFSVVFLAvMFYYSPTLTLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 187 TLITVPIMF----FVTKKLvaysgKNFAKRQKDLGELN-GFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKAD 261
Cdd:cd18588 147 VLASLPLYAllslLVTPIL-----RRRLEEKFQRGAENqSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 262 TFSAFIFPSMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAA 327
Cdd:cd18588 222 NLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQA 287
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
374-573 |
9.44e-21 |
|
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: 92.02 E-value: 9.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 374 TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDmnslRSKIGVV--LQDTYLFAG 448
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHR----IARLGIArtFQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 449 -TIMDNIRYGRLDASDEEVINAA----------KAASAHSF-------IKHLPNQYetkiaseGSNLSQGQKQLLAIARA 510
Cdd:COG0411 94 lTVLENVLVAAHARLGRGLLAALlrlprarreeREARERAEellervgLADRADEP-------AGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 511 ILADADILILDEATS--NIDTRTEL-----QIQEGlnnlmRDRTSFVIAHRLKTIEK-ADQILVIKDGSIL 573
Cdd:COG0411 167 LATEPKLLLLDEPAAglNPEETEELaelirRLRDE-----RGITILLIEHDMDLVMGlADRIVVLDFGRVI 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
364-576 |
1.27e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.76 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 364 NVSFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDT 443
Cdd:PRK13548 9 SVRLG---GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 444 YL-FAGTIMDNIRYGRLD-----ASDEEVINAAKAASAhsfIKHLPN-QYETkiasegsnLSQGQKQLLAIARAI--LAD 514
Cdd:PRK13548 86 SLsFPFTVEEVVAMGRAPhglsrAEDDALVAAALAQVD---LAHLAGrDYPQ--------LSGGEQQRVQLARVLaqLWE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 515 AD----ILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIA--HRLK-TIEKADQILVIKDGSILEKG 576
Cdd:PRK13548 155 PDgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVvlHDLNlAARYADRIVLLHQGRLVADG 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
372-584 |
1.89e-20 |
|
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: 90.68 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSlRSKIGVVL--QDTYLFAG- 448
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGYlpQEASIFRKl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 449 TIMDNIR--YGRLDASDEEVINAAKAASAHSFIKHLPNQYetkiaseGSNLSQGQKQLLAIARAILADADILILDEATSN 526
Cdd:cd03218 91 TVEENILavLEIRGLSKKEREEKLEELLEEFHITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 527 IDTRTELQIQEGLNNLMRDRTSFVIA-HRLK-TIEKADQILVIKDGSILEKGNHESLMED 584
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
369-581 |
2.74e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.88 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 369 YEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHID------GKNIKEYDMNSLRSKIGVVLQD 442
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 443 TYLFAG-TIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILD 521
Cdd:PRK14246 99 PNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 522 EATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESL 581
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
375-571 |
3.20e-20 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 95.36 E-value: 3.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 375 ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeydmnslrskIGVVLQDTYLFAGTIMDNI 454
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 455 RYGrLDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQ 534
Cdd:TIGR01271 508 IFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190
....*....|....*....|....*....|....*...
gi 447166279 535 IQEG-LNNLMRDRTSFVIAHRLKTIEKADQILVIKDGS 571
Cdd:TIGR01271 587 IFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
360-576 |
3.41e-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: 90.09 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVS--FGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeyDMNSLRSKIG 437
Cdd:cd03296 3 IEVRNVSkrFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 438 VVLQDTYLFAG-TIMDNIRYG-RLDASDEEVINAAKAASAHSFIK-----HLPNQYEtkiasegSNLSQGQKQLLAIARA 510
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLKlvqldWLADRYP-------AQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 511 ILADADILILDEATSNIDTrtelQIQEGLNNLMR---DRTS----FVIAHRLKTIEKADQILVIKDGSILEKG 576
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDA----KVRKELRRWLRrlhDELHvttvFVTHDQEEALEVADRVVVMNKGRIEQVG 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
376-576 |
5.13e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 88.96 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGknikeYDMNS----LRSKIGVVLQDTYLFAG-TI 450
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-----FDVVKepaeARRRLGFVSDSTGLYDRlTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 451 MDNIRY-GRLdasdeeviNAAKAASAHSFIKHLPNQYETK--IASEGSNLSQGQKQLLAIARAILADADILILDEATSNI 527
Cdd:cd03266 96 RENLEYfAGL--------YGLKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447166279 528 DTRTELQIQEGLNNLMRDRTSFVIA-HRLKTIEK-ADQILVIKDGSILEKG 576
Cdd:cd03266 168 DVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-576 |
5.84e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.59 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 365 VSFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-----QGQIHIDGKNIKEYDMNSLRSKIGVV 439
Cdd:PRK14247 11 VSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFAG-TIMDNIRYG----RLDASDEEVINAAKAASAHSfikHLPNQYETKIASEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK14247 88 FQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWALEKA---QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEK-ADQILVIKDGSILEKG 576
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
46-334 |
1.76e-19 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 89.16 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 46 IIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSgtarmcLLLIAIYGVTVFLTWLQTFVMV--NVALKTIQKIRQDIFEK 123
Cdd:cd18568 7 ILLASLLLQLLGLALPLFTQIILDRVLVHKNIS------LLNLILIGLLIVGIFQILLSAVrqYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 124 I--QTLSL--RFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVP----IMF 195
Cdd:cd18568 81 FykHLLSLplSFFASRKVGDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPlyvlLTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 196 FVTKKLVAYSGKNFAKRQkdlgELNGFIEEAITGAD-VTTLYGKEKKTVQNFNKINEQL--RVSATKADTFSAFIFpsmN 272
Cdd:cd18568 160 LSSPKLKRNSREIFQANA----EQQSFLVEALTGIAtIKALAAERPIRWRWENKFAKALntRFRGQKLSIVLQLIS---S 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166279 273 FINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18568 233 LINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
360-572 |
2.19e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.39 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeyDMNSLRSKIGVV 439
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFAG-TIMDNIRYG-RL-----DASDEEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAIL 512
Cdd:PRK09452 92 FQSYALFPHmTVFENVAFGlRMqktpaAEITPRVMEALRMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 513 ADADILILDEATSNIDTRTELQIQEGLNNLMRD---RTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKlgiTFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
360-571 |
2.34e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 87.00 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIinLLTRFYDIQ--QGQIHIDGKNIKEYDMNSLRSK-- 435
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVHWSNKNESEPSFEATRSRnr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 --IGVVLQDTYLFAGTIMDNIRYGRlDASDEEVINAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:cd03290 79 ysVAYAAQKPWLLNATVEENITFGS-PFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 514 DADILILDEATSNIDTR-TELQIQEGLNNLMRD--RTSFVIAHRLKTIEKADQILVIKDGS 571
Cdd:cd03290 158 NTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
363-581 |
2.40e-19 |
|
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: 87.04 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 363 ENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEyDMNSLRSKIGVVLQD 442
Cdd:cd03265 4 ENLVKKYGDF-EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 443 tylfagTIMDNIrygrLDASDEEVINAAkaasahsfIKHLPNQYETKIASEG--------------SNLSQGQKQLLAIA 508
Cdd:cd03265 82 ------LSVDDE----LTGWENLYIHAR--------LYGVPGAERRERIDELldfvglleaadrlvKTYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 509 RAILADADILILDEATSNIDTRTELQIQEGLNNLMR--DRTSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESL 581
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
362-576 |
2.77e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 88.23 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENKTI--LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVV 439
Cdd:PRK13642 7 VENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQ--DTYLFAGTIMDNIRYGRLDAS---DEEVINAAKAASAHSFIkhlpnQYETKiasEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK13642 87 FQnpDNQFVGATVEDDVAFGMENQGiprEEMIKRVDEALLAVNML-----DFKTR---EPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLmRDR---TSFVIAHRLKTIEKADQILVIKDGSILEKG 576
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEI-KEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
355-577 |
3.12e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.53 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 355 NLQGHVALENVSFGYEENKTI----LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQ-------IHIDGKN 423
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 424 IKEydMNSLRSKIGVVLQ--DTYLFAGTIMDNIRYG--RLDASDEEVInaaKAASAHSFIKHLPNQYETKIASEgsnLSQ 499
Cdd:PRK13645 82 IKE--VKRLRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAY---KKVPELLKLVQLPEDYVKRSPFE---LSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 500 GQKQLLAIARAILADADILILDEATSNIDTRTE---LQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKG 576
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
.
gi 447166279 577 N 577
Cdd:PRK13645 234 S 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
372-581 |
3.42e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDiQQGQIHIDGKNIKEYD---MNSLRSKIGVVLQDTY---- 444
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPNssln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 445 --LFAGTIMDN---IRYGRLDAS--DEEVINAAK-----AASAHSFikhlPNQYetkiasegsnlSQGQKQLLAIARAIL 512
Cdd:PRK15134 377 prLNVLQIIEEglrVHQPTLSAAqrEQQVIAVMEevgldPETRHRY----PAEF-----------SGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166279 513 ADADILILDEATSNIDTRTELQIQEGLNNLM-RDRTSFV-IAHRLKTIEK-ADQILVIKDGSILEKGNHESL 581
Cdd:PRK15134 442 LKPSLIILDEPTSSLDKTVQAQILALLKSLQqKHQLAYLfISHDLHVVRAlCHQVIVLRQGEVVEQGDCERV 513
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
362-585 |
3.56e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 88.15 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEEN----KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI----KEYDMNSLR 433
Cdd:PRK13634 5 FQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 434 SKIGVVLQ--DTYLFAGTIMDNIRYGRLD--ASDEEVINAAKAASAhsfIKHLPNQYETKIASEgsnLSQGQKQLLAIAR 509
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLPEELLARSPFE---LSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESLMEDR 585
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
360-574 |
4.01e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIdGKNIkeydmnslrsKIGVV 439
Cdd:COG0488 316 LELEGLSKSYGD-KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFAG--TIMDNIRYGRLDASDEEVINAAKAasahsFikhL--PNQYETKIASegsnLSQGQKQLLAIARAILADA 515
Cdd:COG0488 384 DQHQEELDPdkTVLDELRDGAPGGTEQEVRGYLGR-----F---LfsGDDAFKPVGV----LSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 516 DILILDEATSN--IDTRTELqiQEGLNNLmrDRTSFVIAH-R--LKTIekADQILVIKDGSILE 574
Cdd:COG0488 452 NVLLLDEPTNHldIETLEAL--EEALDDF--PGTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
376-588 |
4.27e-19 |
|
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: 91.93 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeydmnslrskIGVVLQDTYLFAGTIMDNIR 455
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 456 YGRldASDEEVINAAKAASAH-SFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQ 534
Cdd:TIGR00957 721 FGK--ALNEKYYQQVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 535 IQE---GLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMEDRGFY 588
Cdd:TIGR00957 799 IFEhviGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
360-584 |
4.76e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYD-MNSLRSKIGV 438
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQ--DTYLFAGTIMDNIRYG--RLDASDEEVINAAKAASAHSFIKhlpnQYETKiasEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRALAEIGLE----KYRHR---SPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLMRD-RTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
367-574 |
6.76e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.05 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 367 FGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYD---MNSLRSKIGVVLQDT 443
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 444 yLFA----GTIMDNIR-----YGRLDASD-----EEVINAAKAASAHsfIKHLPNQyetkiasegsnLSQGQKQLLAIAR 509
Cdd:PRK10419 99 -ISAvnprKTVREIIReplrhLLSLDKAErlaraSEMLRAVDLDDSV--LDKRPPQ-----------LSGGQLQRVCLAR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMRDR-TSFV-IAHRLKTIEK-ADQILVIKDGSILE 574
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFgTACLfITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
360-584 |
7.11e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 91.34 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEE--NKTILKEVSLKARPGETIALVGPTGSGKTTIIN-LLTRFYDIQQGQIHIdgknikeydmnslRSKI 436
Cdd:PLN03130 615 ISIKNGYFSWDSkaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI-------------RGTV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAGTIMDNIRYGR-LDASDEEviNAAKAASAHSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSpFDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 516 DILILDEATSNIDTRTELQIQEG-LNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMED 584
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
360-570 |
7.56e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 85.41 E-value: 7.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDmnslRSKIGVV 439
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFAG-TIMDNIRY-GRL-DASDEEVinaakAASAHSFIK--HLPNQYETKIasegSNLSQGQKQLLAIARAILAD 514
Cdd:cd03269 76 PEERGLYPKmKVIDQLVYlAQLkGLKKEEA-----RRRIDEWLErlELSEYANKRV----EELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVI-AHRLKTIEK-ADQILVIKDG 570
Cdd:cd03269 147 PELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVEElCDRVLLLNKG 204
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
47-256 |
9.41e-19 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 87.08 E-value: 9.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPK-DLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFEKIQ 125
Cdd:cd18584 2 VLLGLLAALLIIAQAWLLARIIAGVFLEGaGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 126 TLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPI--MFFVtkkLVA 203
Cdd:cd18584 82 ALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPLipLFMI---LIG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447166279 204 YSGKNFAKRQ-KDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVS 256
Cdd:cd18584 159 KAAQAASRRQwAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRR 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
373-584 |
9.41e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 85.96 E-value: 9.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 373 KTILKEVSLKARPGETIALVGPTGSGKTTI---INLLTRFYD--IQQGQIHIDGK---NIKEYDMNSLRSKIGVVLQDTY 444
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLEQPEAgtIRVGDITIDTArslSQQKGLIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 445 LFAG-TIMDNIRYGRL---DASDEEVINAAKAASAHSFIKHLPNQYETKiasegsnLSQGQKQLLAIARAILADADILIL 520
Cdd:PRK11264 96 LFPHrTVLENIIEGPVivkGEPKEEATARARELLAKVGLAGKETSYPRR-------LSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 521 DEATSNIDtrTELqIQEGLNNLM----RDRTSFVIAHRLK-TIEKADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK11264 169 DEPTSALD--PEL-VGEVLNTIRqlaqEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
370-574 |
1.00e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 85.60 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 370 EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMN---SLRSK-IGVVLQdTYL 445
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAKhVGFVFQ-SFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 446 FAGTI--MDNIRYGRL--DASDEEVINAAKAASAH----SFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILADADI 517
Cdd:PRK10584 99 LIPTLnaLENVELPALlrGESSRQSRNGAKALLEQlglgKRLDHLPAQ-----------LSGGEQQRVALARAFNGRPDV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 518 LILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIEKADQILVIKDGSILE 574
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
362-561 |
1.73e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.52 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKeyDMNSLRskiGVVLQ 441
Cdd:PRK11248 4 ISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAER---GVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFA-GTIMDNIRYGRLDASdeeVINAAKAASAHSFIKhlpnqyetKIASEGS------NLSQGQKQLLAIARAILAD 514
Cdd:PRK11248 78 NEGLLPwRNVQDNVAFGLQLAG---VEKMQRLEIAHQMLK--------KVGLEGAekryiwQLSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLMRD--RTSFVIAHrlkTIEKA 561
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITH---DIEEA 192
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
371-583 |
1.93e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 89.84 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDgknikeydmnslRSkIGVVLQDTYLFAGTI 450
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 451 MDNIRYgrldaSDEEviNAAKAASA------HSFIKHLPNQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:PTZ00243 738 RGNILF-----FDEE--DAARLADAvrvsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 525 SNIDTRT-ELQIQEGLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLME 583
Cdd:PTZ00243 811 SALDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
47-317 |
2.42e-18 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 85.63 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTarMCLLLIAIYGVT----VFLTWLQTFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18582 2 LLLLVLAKLLNVAVPFLLKYAVDALSAPASALLA--VPLLLLLAYGLArilsSLFNELRDALFARVSQRAVRRLALRVFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 123 KIQTLSLRFFDVRSQGDL---MSRVTNDIDNLnqaLTQSVVQIISSALTFIGVAIAMFAL-DWILAIVTLITVPIMFFVT 198
Cdd:cd18582 80 HLHSLSLRFHLSRKTGALsraIERGTRGIEFL---LRFLLFNILPTILELLLVCGILWYLyGWSYALITLVTVALYVAFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 199 KKLVAYSGKnFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNL 277
Cdd:cd18582 157 IKVTEWRTK-FRREMNEAdNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 447166279 278 GMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQF 317
Cdd:cd18582 236 GLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFL 275
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
360-584 |
2.44e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 85.19 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTI-LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGV 438
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQD-TYLFAGTIMD-NIRYGRLDasdeeviNAAKAASAHSFIKHLPNQYE--TKIASEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK13648 88 VFQNpDNQFVGSIVKyDVAFGLEN-------HAVPYDEMHRRVSEALKQVDmlERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIEKADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
363-576 |
2.90e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 363 ENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQD 442
Cdd:PRK10253 11 EQLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 443 TYLFAGTIMDNI----RY------GRLDASDEEVINAAKAASAhsfIKHLPNQyetkiasEGSNLSQGQKQLLAIARAIL 512
Cdd:PRK10253 90 ATTPGDITVQELvargRYphqplfTRWRKEDEEAVTKAMQATG---ITHLADQ-------SVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 513 ADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRL-KTIEKADQILVIKDGSILEKG 576
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLnQACRYASHLIALREGKIVAQG 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
360-585 |
3.25e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.27 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTI----LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMN----S 431
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 432 LRSKIGVVLQ--DTYLFAGTIMDNIRYGRLD--ASDEEVINAAKaasahSFIKH--LPNQYETKIASEgsnLSQGQKQLL 505
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAL-----KWLKKvgLSEDLISKSPFE---LSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 506 AIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRD-RTSFVIAHRLKTI-EKADQILVIKDGSILEKGNHESLME 583
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFS 234
|
..
gi 447166279 584 DR 585
Cdd:PRK13641 235 DK 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
362-585 |
4.16e-18 |
|
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: 83.73 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDMnsLRSKIGV 438
Cdd:TIGR03410 3 VSNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklPPHER--ARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQDTYLFAG-TIMDNIRYGrldasdeevinAAKAASAHSFIKhlPNQYE------TKIASEGSNLSQGQKQLLAIARAI 511
Cdd:TIGR03410 80 VPQGREIFPRlTVEENLLTG-----------LAALPRRSRKIP--DEIYElfpvlkEMLGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 512 LADADILILDEATSNIDTRTELQIQEGLNNL--MRDRTSFVIAHRLK-TIEKADQILVIKDGSILEKGNHESLMEDR 585
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDELDEDK 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
362-528 |
5.56e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.04 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDgKNIkeydmnslrsKIGVVLQ 441
Cdd:COG0488 1 LENLSKSFGG-RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGL----------RIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFAG-TIMDNI------------RYGRLDAS-DEEVINAAKAASAHSFIKHLpN--QYETKIAS--EG--------- 494
Cdd:COG0488 69 EPPLDDDlTVLDTVldgdaelraleaELEELEAKlAEPDEDLERLAELQEEFEAL-GgwEAEARAEEilSGlgfpeedld 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 447166279 495 ---SNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:COG0488 148 rpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
362-597 |
6.45e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.53 E-value: 6.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDG------KNIKEYDMNSLRSK 435
Cdd:PRK11124 5 LNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 IGVVLQDTYLFAG-TIMDN-----IRYgrLDASDEEVINAAK--------AASAHSFIKHlpnqyetkiasegsnLSQGQ 501
Cdd:PRK11124 84 VGMVFQQYNLWPHlTVQQNlieapCRV--LGLSKDQALARAEkllerlrlKPYADRFPLH---------------LSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 502 KQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR-TSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHE 579
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
250
....*....|....*...
gi 447166279 580 SLMEDRgfyfdlyTSQFK 597
Cdd:PRK11124 227 CFTQPQ-------TEAFK 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
365-582 |
7.34e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 7.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 365 VSFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTY 444
Cdd:PRK09536 11 VEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 445 L-FAGTIMDNIRYGRL----------DASDEEVINAAKAASAHSFikhlpnqyetkIASEGSNLSQGQKQLLAIARAILA 513
Cdd:PRK09536 88 LsFEFDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQF-----------ADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 514 DADILILDEATSNIDTRTELQIQEGLNNLMRD-RTSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESLM 582
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
360-569 |
7.99e-18 |
|
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: 81.05 E-value: 7.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGknikeyDMNSLrskigVV 439
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE------GEDLL-----FL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFAGTIMDNIRYgrldASDEEvinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILADADILI 519
Cdd:cd03223 70 PQRPYLPLGTLREQLIY----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447166279 520 LDEATSNIDTRTELQIQEGLNNLMrdrTSFV-IAHRlKTIEK-ADQILVIKD 569
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELG---ITVIsVGHR-PSLWKfHDRVLDLDG 162
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
360-581 |
9.95e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.77 E-value: 9.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENV--SFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEydmNSLRSK-I 436
Cdd:PRK11432 7 VVLKNItkRFG---SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAG-TIMDNIRYG--RLDASDEEVINAAKAASAHSFIKHLPNQYETKIasegsnlSQGQKQLLAIARAILA 513
Cdd:PRK11432 81 CMVFQSYALFPHmSLGENVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRYVDQI-------SGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 514 DADILILDEATSNIDTRTELQIQEGLNNLMR--DRTSFVIAH-RLKTIEKADQILVIKDGSILEKGNHESL 581
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
378-584 |
1.10e-17 |
|
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: 84.77 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 378 EVSLKARPGETIALVGPTGSGKTTIINL---LTRFydiQQGQIHIDGK---------NIKEYdmnslRSKIGVVLQDTYL 445
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLERP---DSGRIRLGGEvlqdsargiFLPPH-----RRRIGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 446 FAG-TIMDNIRYGRLdasdeeviNAAKAASAHSF--------IKHLPNQYETkiasegsNLSQGQKQLLAIARAILADAD 516
Cdd:COG4148 89 FPHlSVRGNLLYGRK--------RAPRAERRISFdevvellgIGHLLDRRPA-------TLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 517 ILILDEATSNIDTRTELQIQEGLNNLmRDRTS----FV------IAhRLktiekADQILVIKDGSILEKGNHESLMED 584
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERL-RDELDipilYVshsldeVA-RL-----ADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
368-576 |
1.70e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 81.81 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 368 GYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeydmnsLRSKIGVvlqdTYLFA 447
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---------VSSLLGL----GGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 448 G--TIMDNIR-----YGRLDASDEEVINAAKAASAhsfikhLPNQYETKIasegSNLSQGQKQLLAIARAILADADILIL 520
Cdd:cd03220 97 PelTGRENIYlngrlLGLSRKEIDEKIDEIIEFSE------LGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 521 DEATSNIDTRTELQIQEGLNNLMRDRTSFVIA-HRLKTIEK-ADQILVIKDGSILEKG 576
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
360-582 |
2.25e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.55 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTilkEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNikEYDMNSLRSKIGVV 439
Cdd:PRK10771 2 LKLTDITWLYHHLPM---RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFAG-TIMDNIRYG-----RLDASDEEVINA-AKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAIL 512
Cdd:PRK10771 77 FQENNLFSHlTVAQNIGLGlnpglKLNAAQREKLHAiARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 513 ADADILILDEATSNIDT--RTE-LQIqegLNNLMRDR--TSFVIAHRLktiEKADQI----LVIKDGSILEKGNHESLM 582
Cdd:PRK10771 146 REQPILLLDEPFSALDPalRQEmLTL---VSQVCQERqlTLLMVSHSL---EDAARIaprsLVVADGRIAWDGPTDELL 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
362-577 |
2.85e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.85 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENV--SFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEydmnSLRSKIGvv 439
Cdd:COG4152 4 LKGLtkRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIG-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 lqdtYLFA--G-----TIMDNIRY-GRL---DASDeevinaAKAASAHSFIKH-LPNQYETKIasegSNLSQGQKQLLAI 507
Cdd:COG4152 75 ----YLPEerGlypkmKVGEQLVYlARLkglSKAE------AKRRADEWLERLgLGDRANKKV----EELSKGNQQKVQL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 508 ARAILADADILILDEATS-----NIDTrtelqIQEGLNNLMRDRTSfVI--AHRLKTIEK-ADQILVIKDGSILEKGN 577
Cdd:COG4152 141 IAALLHDPELLILDEPFSgldpvNVEL-----LKDVIRELAAKGTT-VIfsSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
379-584 |
4.06e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 82.70 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 379 VSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYD---MNSLRSKIGVVLQDTYlfaGTImdNIR 455
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNPY---GSL--NPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 456 YgRLDASDEE--VIN-----AAKAASAHSFIKHL---PNQYEtkiaSEGSNLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:PRK11308 109 K-KVGQILEEplLINtslsaAERREKALAMMAKVglrPEHYD----RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 526 NIDtrteLQIQEGLNNLMRD-----RTSFV-IAHRLKTIEK-ADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK11308 184 ALD----VSVQAQVLNLMMDlqqelGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
376-584 |
4.17e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.54 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRS----KIGVVLQDTYLFAG-TI 450
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 451 MDNIRYGRLDAS------DEEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:PRK10070 124 LDNTAFGMELAGinaeerREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 525 SNIDTRTELQIQEGLNNLM--RDRTSFVIAHRL-KTIEKADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
371-576 |
4.39e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 79.88 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRF--YDIQQGQIHIDGKNIKEYDMNSlRSKIGVVL--QDTYLF 446
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLGIFLafQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 447 AG-TIMDNIRYgrldasdeevINaakaasahsfikhlpnqyetkiasEGsnLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:cd03217 90 PGvKNADFLRY----------VN------------------------EG--FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447166279 526 NIDTRTELQIQEGLNNLMRDRTSF-VIAHRLKTIE--KADQILVIKDGSILEKG 576
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSVlIITHYQRLLDyiKPDRVHVLYDGRIVKSG 187
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
360-584 |
5.33e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.57 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEyDMNSLRSKIGVV 439
Cdd:PRK13536 42 IDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQ-DTYLFAGTIMDNI----RYGRLDASD-EEVInaakaASAHSFIKhlpnqYETKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:PRK13536 120 PQfDNLDLEFTVRENLlvfgRYFGMSTREiEAVI-----PSLLEFAR-----LESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 514 DADILILDEATSNIDTRTELQIQEGLNNLM-RDRTSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
372-546 |
5.77e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.92 E-value: 5.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDmnslrskigVVLQDTYLfaG--- 448
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---------VAEACHYL--Ghrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 449 ------TIMDNIRY-GRLDASDEEVINAAKAASAHSFIKHLPNQYetkiasegsnLSQGQKQLLAIARAILADADILILD 521
Cdd:PRK13539 83 amkpalTVAENLEFwAAFLGGEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILD 152
|
170 180
....*....|....*....|....*
gi 447166279 522 EATSNIDTRTelqiQEGLNNLMRDR 546
Cdd:PRK13539 153 EPTAALDAAA----VALFAELIRAH 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
362-576 |
7.48e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.16 E-value: 7.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENK---TILKEVSLKARPGETIALVGPTGSGKTT---IINLLTRfydIQQGQIHIDGKNIKEYDMNSLRS- 434
Cdd:PRK11153 4 LKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 435 --KIGVVLQDTYLFAG-TIMDNIRYG-RLDASDEEVINAAKAA-------SAHSfikhlpNQYEtkiasegSNLSQGQKQ 503
Cdd:PRK11153 81 rrQIGMIFQHFNLLSSrTVFDNVALPlELAGTPKAEIKARVTEllelvglSDKA------DRYP-------AQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 504 LLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTI-EKADQILVIKDGSILEKG 576
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVkRICDRVAVIDAGRLVEQG 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
376-571 |
7.56e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.68 E-value: 7.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMN-SLRSKIGVVLQDTYLFAG-TIMDN 453
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 454 IRYGRLDASDEEVINAA------KAASAHSFIKHLPNQYETKIAsegsNLSQGQKQLLAIARAILADADILILDEATSNI 527
Cdd:PRK09700 101 LYIGRHLTKKVCGVNIIdwremrVRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447166279 528 DTRTELQIQEGLNNLMRDRTSFV-IAHRLKTIEK-ADQILVIKDGS 571
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGS 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
357-576 |
7.81e-17 |
|
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: 80.01 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 357 QGHVALENVSFGY-EENKT--ILKEVSLKARPGETIALVGPTGSGKTTIINLLT---RFYDIQQGQIHIDGKNIKEYDMn 430
Cdd:cd03234 1 QRVLPWWDVGLKAkNWNKYarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKPDQF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 431 slRSKIGVVLQDTYLFAG-TIMDNIRYGRLDASDEEVINAAKAASAHSF-IKHLPNqyeTKIASEG-SNLSQGQKQLLAI 507
Cdd:cd03234 80 --QKCVAYVRQDDILLPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVlLRDLAL---TRIGGNLvKGISGGERRRVSI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 508 ARAILADADILILDEATSNIDTRTELQIQEGLNNLMRdRTSFVIAhrlkTIEKA--------DQILVIKDGSILEKG 576
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVIL----TIHQPrsdlfrlfDRILLLSSGEIVYSG 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
363-577 |
9.04e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.90 E-value: 9.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 363 ENVSFGYEEN-----KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIK-EYDMNSLRSKI 436
Cdd:PRK13633 8 KNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQ--DTYLFAGTIMDNIRYG--RLDASDEE----VINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIA 508
Cdd:PRK13633 88 GMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEirerVDESLKKVGMYEYRRHAPHL-----------LSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 509 RAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIEKADQILVIKDGSILEKGN 577
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
376-570 |
9.34e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 9.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGkniKEYDMNS----LRSKIGVVLQDTYLFAG-TI 450
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSprdaIALGIGMVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 451 MDNIRYGrLDASDEEVINAAKAASAhsfIKHLPNQY------ETKIasegSNLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:COG3845 98 AENIVLG-LEPTKGGRLDRKAARAR---IRELSERYgldvdpDAKV----EDLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447166279 525 SNIdtrTELQIQEgLNNLMRD-----RTSFVIAHRLKTI-EKADQILVIKDG 570
Cdd:COG3845 170 AVL---TPQEADE-LFEILRRlaaegKSIIFITHKLREVmAIADRVTVLRRG 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
353-576 |
1.05e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 83.20 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 353 VQNLqghvaleNVSFG-YEENKTILKEVSLKARPGETIALVGPTGSGKT----TIINLLTRFYDIQQGQIHIDGKNI--- 424
Cdd:COG4172 9 VEDL-------SVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 425 KEYDMNSLR-SKIGVVLQD--TYL---FagTIMDNIRygrldasdeEVI---NAAKAASAHSFIKHL------PNQyETK 489
Cdd:COG4172 82 SERELRRIRgNRIAMIFQEpmTSLnplH--TIGKQIA---------EVLrlhRGLSGAAARARALELlervgiPDP-ERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 490 IASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFV--IAHRLKTIEK-ADQILV 566
Cdd:COG4172 150 LDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALllITHDLGVVRRfADRVAV 229
|
250
....*....|
gi 447166279 567 IKDGSILEKG 576
Cdd:COG4172 230 MRQGEIVEQG 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
376-570 |
1.16e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.05 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFY--DIQQGQIHIDG-----KNIKEydmnSLRSKIGVVLQDTYLFAG 448
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGeelqaSNIRD----TERAGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 449 -TIMDNI-------RYGRLDasDEEVINAAKAASAHSFIKHLPNqyeTKIasegSNLSQGQKQLLAIARAILADADILIL 520
Cdd:PRK13549 97 lSVLENIflgneitPGGIMD--YDAMYLRAQKLLAQLKLDINPA---TPV----GNLGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447166279 521 DEATSNI---DTRTELQIQEGLNNlmRDRTSFVIAHRLKTIEK-ADQILVIKDG 570
Cdd:PRK13549 168 DEPTASLtesETAVLLDIIRDLKA--HGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
376-587 |
1.61e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.52 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHI---DGKNIKEYD---------------------MNS 431
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKekekvleklviqktrfkkikkIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 432 LRSKIGVVLQ--DTYLFAGTIMDNIRYG--RLDASDEEvinAAKAASAHSFIKHLPNQYETKiasEGSNLSQGQKQLLAI 507
Cdd:PRK13651 103 IRRRVGVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEE---AKKRAAKYIELVGLDESYLQR---SPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 508 ArAILA-DADILILDEATSNIDTRTELQIQEGLNNLMRD-RTSFVIAHRLKTI-EKADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK13651 177 A-GILAmEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGDTYDILSD 255
|
...
gi 447166279 585 RGF 587
Cdd:PRK13651 256 NKF 258
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
360-583 |
1.65e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.62 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSlRSKIGVV 439
Cdd:PRK13537 8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQ-DTYLFAGTIMDNIR-YGRLdasdeeviNAAKAASAHSFIKHLPN--QYETKIASEGSNLSQGQKQLLAIARAILADA 515
Cdd:PRK13537 86 PQfDNLDPDFTVRENLLvFGRY--------FGLSAAAARALVPPLLEfaKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 516 DILILDEATSNIDTRTELQIQEGLNNLM-RDRTSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESLME 583
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
362-570 |
1.79e-16 |
|
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: 76.33 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNikeydmnslrsKIGVVLQ 441
Cdd:cd03221 3 LENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 dtylfagtimdnirygrldasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQLLAIARAILADADILILD 521
Cdd:cd03221 71 -------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447166279 522 EATSNIDTRTELQIQEGLNNLmrDRTSFVIAH-R--LKTIekADQILVIKDG 570
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
360-587 |
1.80e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.16 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTI----LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDG----KNIKEYDMNS 431
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 432 LRSKIGVVLQ--DTYLFAGTIMDNIRYG--RLDASDEEvinAAKAASAHSFIKHLPNQYETKIASEgsnLSQGQKQLLAI 507
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKEK---AEKIAAEKLEMVGLADEFWEKSPFE---LSGGQMRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 508 ARAILADADILILDEATSNIDTRTELQIQEGLNNLMRD-RTSFVIAHRLKTI-EKADQILVIKDGSILEKGNHESLMEDR 585
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQEV 235
|
..
gi 447166279 586 GF 587
Cdd:PRK13643 236 DF 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
376-570 |
2.10e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYD-MNSLRSKIGVVLQDTYLFAG-TIMDN 453
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAStTAALAAGVAIIYQELHLVPEmTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 454 IRYGRLDASDEEVINAAKAASAHSFIKHL-----PNqyeTKIASegsnLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:PRK11288 100 LYLGQLPHKGGIVNRRLLNYEAREQLEHLgvdidPD---TPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 447166279 529 TRtELQIQEGLNNLMRD--RTSFVIAHRLKTI-EKADQILVIKDG 570
Cdd:PRK11288 173 AR-EIEQLFRVIRELRAegRVILYVSHRMEEIfALCDAITVFKDG 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
360-587 |
2.28e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.79 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTI----LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI----KEYDMNS 431
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 432 LRSKIGVVLQ--DTYLFAGTIMDNIRYG--RLDASDEEVINAAKAASAHSFIKhlpnqyETKIASEGSNLSQGQKQLLAI 507
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 508 ArAILA-DADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRL--KTIEKADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK13649 157 A-GILAmEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLmdDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
...
gi 447166279 585 RGF 587
Cdd:PRK13649 236 VDF 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
323-584 |
3.54e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.83 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 323 TIQAAVAGGERVFEIMDEVPEIKNKKDAFVVQNLQGHvALENVSFgyeenktilkevslKARPGETIALVGPTGSGKTTI 402
Cdd:PRK10261 302 IEQDTVVDGEPILQVRNLVTRFPLRSGLLNRVTREVH-AVEKVSF--------------DLWPGETLSLVGESGSGKSTT 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 403 INLLTRFYDIQQGQIHIDGKNI---KEYDMNSLRSKIGVVLQDTY-------LFAGTIMDNIRYGRLDASDEEvinAAKA 472
Cdd:PRK10261 367 GRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYasldprqTVGDSIMEPLRVHGLLPGKAA---AARV 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 473 ASAHSFIKHLPnQYETKIASEgsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR-TSFV- 550
Cdd:PRK10261 444 AWLLERVGLLP-EHAWRYPHE---FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgIAYLf 519
|
250 260 270
....*....|....*....|....*....|....*
gi 447166279 551 IAHRLKTIEK-ADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK10261 520 ISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
360-584 |
4.80e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.67 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEE----NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI----KEYDMNS 431
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 432 LRSKIGVVLQ--DTYLFAGTIMDNIRYG--RLDASDEEVinaakAASAHSFIKHLpnQYETKIASEGS-NLSQGQKQLLA 506
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEV-----KNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 507 IARAILADADILILDEATSNIDTRTELQIQEGLNNLMRD--RTSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESLME 583
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
.
gi 447166279 584 D 584
Cdd:PRK13646 236 D 236
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
339-588 |
4.95e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.51 E-value: 4.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 339 DEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKTILkevslkarpgetiaLVGPTGSGKTTIIN-----LLTRFYDIQ 413
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYF--------------IIGNSGSGKSTLVThfnglIKSKYGTIQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 414 QGQIHIDGKNIKEYDMNS-----------LRSKIGVVLQ--DTYLFAGTIMDNIRYGRLdASDEEVINAAKAASAHSFIK 480
Cdd:PRK13631 85 VGDIYIGDKKNNHELITNpyskkiknfkeLRRRVSMVFQfpEYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLAKFYLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 481 HLPNQYETKIASEgsnLSQGQKQLLAIArAILA-DADILILDEATSNIDTRTELQIQEG-LNNLMRDRTSFVIAHRL-KT 557
Cdd:PRK13631 164 GLDDSYLERSPFG---LSGGQKRRVAIA-GILAiQPEILIFDEPTAGLDPKGEHEMMQLiLDAKANNKTVFVITHTMeHV 239
|
250 260 270
....*....|....*....|....*....|.
gi 447166279 558 IEKADQILVIKDGSILEKGNHESLMEDRGFY 588
Cdd:PRK13631 240 LEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
61-306 |
9.80e-16 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 78.12 E-value: 9.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 61 PYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQT-FVMVNVALKTIqKIRQDIFEKIQTLSLRFFDVRSQGD 139
Cdd:cd18784 16 PYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGgLFTLAMARLNI-RIRNLLFRSIVSQEIGFFDTVKTGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 140 LMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLVAYSGKNFAKRQKDLGEL 219
Cdd:cd18784 95 ITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 220 NGFIEEAITGAdvttlygkekKTVQNF-NKINEQLRVSATKADTFS-----AFIFPSMNFINNL-GMGLVIGT---GSVM 289
Cdd:cd18784 175 NEVAEETISSI----------RTVRSFaNEDGEANRYSEKLKDTYKlkikeALAYGGYVWSNELtELALTVSTlyyGGHL 244
|
250
....*....|....*..
gi 447166279 290 VLNGMTTVGVIAAFINY 306
Cdd:cd18784 245 VITGQISGGNLISFILY 261
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
328-576 |
1.26e-15 |
|
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: 76.60 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 328 VAGGERVFEIMDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEEnktilkevslkarpGETIALVGPTGSGKTTIINLLT 407
Cdd:cd03267 3 VSNLSKSYRVYSKEPGLIGSLKSLFKRKYREVEALKGISFTIEK--------------GEIVGFIGPNGAGKTTTLKILS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 408 RFYDIQQGQIHIDGkNIKEYDMNSLRSKIGVVL------------QDTYLFAGTIMDnIRYGRLDASDEEVINAAKaasa 475
Cdd:cd03267 69 GLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVFgqktqlwwdlpvIDSFYLLAAIYD-LPPARFKKRLDELSELLD---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 476 hsfIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVI--AH 553
Cdd:cd03267 143 ---LEELLDT-------PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSH 212
|
250 260
....*....|....*....|....
gi 447166279 554 RLKTIEK-ADQILVIKDGSILEKG 576
Cdd:cd03267 213 YMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
362-585 |
1.32e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.58 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIkEYD---MNSLRSKIGV 438
Cdd:PRK13636 8 VEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSrkgLMKLRESVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQ--DTYLFAGTIMDNIRYGRLDAS--DEEVINAAKAASAHSFIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK13636 87 VFQdpDNQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLMR--DRTSFVIAHRLKTIE-KADQILVIKDGSILEKGNHESLMEDR 585
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
375-582 |
2.33e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.16 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 375 ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIK-------------EYDMNSLRSKIGVVLQ 441
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFAG-TIMDNIRYGRLdasdeEVINAAKAASAHSFIKHLpNQYETKIASEG---SNLSQGQKQLLAIARAILADADI 517
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPI-----QVLGLSKQEARERAVKYL-AKVGIDERAQGkypVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 518 LILDEATSNIDTRTELQIQEGLNNLMRD-RTSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESLM 582
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
47-329 |
2.36e-15 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 76.93 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFEKIQT 126
Cdd:cd18561 2 VLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 127 LSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLVAYSG 206
Cdd:cd18561 82 LGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 207 KNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGTG 286
Cdd:cd18561 162 DTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 447166279 287 SVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVA 329
Cdd:cd18561 242 ALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGIS 284
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
362-573 |
4.65e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 78.61 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGY---EENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSL----RS 434
Cdd:PRK10535 7 LKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 435 KIGVVLQDTYLFAG-TIMDNIRYGRLDASDEEvinAAKAASAHSFIKHLpnQYETKIASEGSNLSQGQKQLLAIARAILA 513
Cdd:PRK10535 87 HFGFIFQRYHLLSHlTAAQNVEVPAVYAGLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166279 514 DADILILDEATSNIDTRTELQIQEGLNNLmRDR--TSFVIAHRLKTIEKADQILVIKDGSIL 573
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQL-RDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
61-334 |
5.23e-15 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 75.97 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 61 PYLMGVIIDqYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQ-KIRQDIFEKIQTLSLRFFDVRSQGD 139
Cdd:cd18589 16 PYYTGRMTD-WIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHsRLQGLVFAAVLRQEIAFFDSNQTGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 140 LMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLVAYSgKNFAKR-QKDLGE 218
Cdd:cd18589 95 IVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQ-QSLAVQvQKSLAR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 219 LNgfieeaitgaDVTTLYGKEKKTVQNF-NKINEQLRVSATKADTFS-----AFIFPSMNFINNL-GMGLVIGT---GSV 288
Cdd:cd18589 174 AN----------QVAVETFSAMKTVRSFaNEEGEAQRYRQRLQKTYRlnkkeAAAYAVSMWTSSFsGLALKVGIlyyGGQ 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 447166279 289 MVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18589 244 LVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
372-587 |
7.10e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 74.68 E-value: 7.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRF--YDIQQGQIHIDGKNIKEYDMNsLRSKIGVVLQDTYLFAGT 449
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 450 IMDNIRYGRLDASDEEVINAAKAASAHSFIKHLPNQYE---------TKIASEGsnLSQGQKQLLAIARAILADADILIL 520
Cdd:CHL00131 98 GVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKlvgmdpsflSRNVNEG--FSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166279 521 DEATSNIDTRTELQIQEGLNNLMRDRTSFV-IAH--RLKTIEKADQILVIKDGSILEKGNHE--SLMEDRGF 587
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKGY 247
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
46-334 |
8.71e-15 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 75.26 E-value: 8.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 46 IIFLVFVTTLLGLLGPYLMGVIIDQYIvpkdlSGTARMCLLLIAIYGVTVFL------TWLQTFVMVNVALKTIQKIRQD 119
Cdd:cd18583 1 CFLCLLAERVLNVLVPRQLGIIVDSLS-----GGSGKSPWKEIGLYVLLRFLqsggglGLLRSWLWIPVEQYSYRALSTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 120 IFEKIQTLSLRFFDVRSQGDLMSrvtndidNLNQAltQSVVQIISSAL-----TFIGVAIAM----FALDWILAIVTLIT 190
Cdd:cd18583 76 AFNHVMNLSMDFHDSKKSGEVLK-------AIEQG--SSINDLLEQILfqivpMIIDLVIAIvylyYLFDPYMGLIVAVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 191 VPIMFFVTKKLVAYSgknfAKRQKDLgeLNGFIEEAITGADVTTLYgkekKTVQNFNKIN-EQLRVSAT-----KADTFS 264
Cdd:cd18583 147 MVLYVWSTIKLTSWR----TKLRRDM--IDADREERSILTESLLNW----ETVKYFNREPyEKERYREAvknyqKAERKY 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 265 AFIFPSMNFINNLGM--GLVIGT--GSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18583 217 LFSLNLLNAVQSLILtlGLLAGCflAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
361-565 |
9.79e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.59 E-value: 9.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 361 ALENVSFGYEENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVL 440
Cdd:PRK10247 9 QLQNVGYLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 441 QDTYLFAGTIMDNIRYG---RLDASDEEVInaakAASAHSFikHLPNQYETKIASEgsnLSQGQKQLLAIARAILADADI 517
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFPwqiRNQQPDPAIF----LDDLERF--ALPDTILTKNIAE---LSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447166279 518 LILDEATSNIDTRTELQIQEGLNNLMRDRTSFVI--AHRLKTIEKADQIL 565
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVI 208
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
363-584 |
1.28e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.77 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 363 ENVSFGYEENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNS-LRSKIGVVLQ 441
Cdd:PRK10895 7 KNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFAG-TIMDNIRYG---RLDASDEEVINAAKAASAHSFIKHLPNqyetkiaSEGSNLSQGQKQLLAIARAILADADI 517
Cdd:PRK10895 86 EASIFRRlSVYDNLMAVlqiRDDLSAEQREDRANELMEEFHIEHLRD-------SMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 518 LILDEATSNIDTRTELQIQEGLNNLmRDRTSFVIA--HRLK-TIEKADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLItdHNVReTLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
360-576 |
1.68e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.45 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNikeydMNSLRSK---I 436
Cdd:PRK11000 4 VTLRNVTKAYGDV-VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR-----MNDVPPAergV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAG-TIMDNIRYG-RLDASDEEVINaaKAASAHSFIKHLPNQYETKIASegsnLSQGQKQLLAIARAILAD 514
Cdd:PRK11000 78 GMVFQSYALYPHlSVAENMSFGlKLAGAKKEEIN--QRVNQVAEVLQLAHLLDRKPKA----LSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLMR--DRTSFVIAH-RLKTIEKADQILVIKDGSILEKG 576
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
373-572 |
2.41e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTrFYDIQ----QGQIHIDGKNIkEYDMNSLRSkiGVVLQDTyLFAG 448
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPI-DAKEMRAIS--AYVQQDD-LFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 449 T--------IMDNIRYGRLDASDE------EVINAAKAASAHsfikhlpnqyETKIASEGS--NLSQGQKQLLAIARAIL 512
Cdd:TIGR00955 113 TltvrehlmFQAHLRMPRRVTKKEkrervdEVLQALGLRKCA----------NTRIGVPGRvkGLSGGERKRLAFASELL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 513 ADADILILDEATSNIDTRTELQIQEGLNNL-MRDRTSFVIAHR--LKTIEKADQILVIKDGSI 572
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQpsSELFELFDKIILMAEGRV 245
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
376-584 |
2.72e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 73.33 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDmNSLRSK-IGVVLQDtylfAGTIMD-N 453
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD-YKYRCKhIRMIFQD----PNTSLNpR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 454 IRYGR-LDA--------SDEEvinaakaasAHSFIKH-------LPNQYETKIasegSNLSQGQKQLLAIARAILADADI 517
Cdd:COG4167 104 LNIGQiLEEplrlntdlTAEE---------REERIFAtlrlvglLPEHANFYP----HMLSSGQKQRVALARALILQPKI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 518 LILDEATSNIDTRTELQIQeglnNLM-----RDRTSFV-IAHRLKTIEK-ADQILVIKDGSILEKGNHESLMED 584
Cdd:COG4167 171 IIADEALAALDMSVRSQII----NLMlelqeKLGISYIyVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
374-585 |
3.55e-14 |
|
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: 75.25 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 374 TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFY--DIQQGQIHIDGKNIKEYDM-NSLRSKIGVVLQDTYLFAG-T 449
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVPElS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 450 IMDNIRYG--------RLDasDEEVINAAKAASAHSFIKHLPNqyetkiASEGSNLSQGQKQLLAIARAILADADILILD 521
Cdd:TIGR02633 95 VAENIFLGneitlpggRMA--YNAMYLRAKNLLRELQLDADNV------TRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 522 EATSNIdTRTELQIqegLNNLMRDRTS-----FVIAHRLKTIEK-ADQILVIKDGSILEKGNHESLMEDR 585
Cdd:TIGR02633 167 EPSSSL-TEKETEI---LLDIIRDLKAhgvacVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSEDD 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
376-585 |
5.40e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.65 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYD-MNSLRSKIGVVLQDTYLFAG-TIMDN 453
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpKSSQEAGIGIIHQELNLIPQlTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 454 IRYGRLDASDEEVINAAKA-ASAHSFIKHLPNQYETKIASegSNLSQGQKQLLAIARAILADADILILDEATSNI-DTRT 531
Cdd:PRK10762 100 IFLGREFVNRFGRIDWKKMyAEADKLLARLNLRFSSDKLV--GELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 532 ElQIQEGLNNLMRDRTSFV-IAHRLKTI-EKADQILVIKDGSILEKGNHESLMEDR 585
Cdd:PRK10762 178 E-SLFRVIRELKSQGRGIVyISHRLKEIfEICDDVTVFRDGQFIAEREVADLTEDS 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
363-581 |
5.88e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 363 ENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQ- 441
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 -DTYLFAGTIMDNIRYGRLDAS-DEEVINAAKAASAHSF-IKHLPNQYEtkiasegSNLSQGQKQLLAIARAILADADIL 518
Cdd:PRK13652 87 pDDQIFSPTVEQDIAFGPINLGlDEETVAHRVSSALHMLgLEELRDRVP-------HHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 519 ILDEATSNIDTRTELQIQEGLNNLMRDRTSFVI--AHRLKTI-EKADQILVIKDGSILEKGNHESL 581
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
46-325 |
6.60e-14 |
|
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: 72.62 E-value: 6.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 46 IIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFEKIQ 125
Cdd:cd18566 7 VLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 126 TLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSaLTFIGVAIA-MFALDWILAIVTLITVPIMFFVTkklvAY 204
Cdd:cd18566 87 SLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLD-LPFVLIFLGlIWYLGGKLVLVPLVLLGLFVLVA----IL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 205 SGKNFAKRQKDLGELN----GFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMG 280
Cdd:cd18566 161 LGPILRRALKERSRADerrqNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 447166279 281 LVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQ 325
Cdd:cd18566 241 AVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQ 285
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
364-570 |
7.63e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.39 E-value: 7.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 364 NVSFGYEENKT---ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNikeydMNSLRS------ 434
Cdd:PRK11629 10 NLCKRYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP-----MSKLSSaakael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 435 ---KIGVVLQDTYLFAG-TIMDNIRYGRLdasdeevINAAKAASAHSFIKHLPNQ--YETKIASEGSNLSQGQKQLLAIA 508
Cdd:PRK11629 85 rnqKLGFIYQFHHLLPDfTALENVAMPLL-------IGKKKPAEINSRALEMLAAvgLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 509 RAILADADILILDEATSNIDTRTELQIQEGLNNL-MRDRTSF-VIAHRLKTIEKADQILVIKDG 570
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFlVVTHDLQLAKRMSRQLEMRDG 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
360-586 |
8.33e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.45 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTiLKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNS-LRSKIGV 438
Cdd:PRK11614 6 LSFDKVSAHYGKIQA-LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQDTYLFAG-TIMDNIRYGRLDASDEEVINAAKAAsahsfIKHLPNQYETKIASEGSnLSQGQKQLLAIARAILADADI 517
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWV-----YELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 518 LILDEATSNIDTRTELQIQEGLNNLMRD-RTSFVIAhrlktiEKADQILVIKD-GSILEKGNheSLMEDRG 586
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVE------QNANQALKLADrGYVLENGH--VVLEDTG 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
357-580 |
8.36e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 8.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 357 QGHVALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKI 436
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAGTIMDNI---RYG------RLDASDEEVINAAKAASAHSFIKHlpnqyetkiaSEGSNLSQGQKQLLAI 507
Cdd:PRK15056 84 PQSEEVDWSFPVLVEDVVmmgRYGhmgwlrRAKKRDRQIVTAALARVDMVEFRH----------RQIGELSGGQKKRVFL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 508 ARAILADADILILDEATSNIDTRTELQIQEGLNNLmRD--RTSFVIAHRLKTI-EKADQILVIKdGSILEKGNHES 580
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDegKTMLVSTHNLGSVtEFCDYTVMVK-GTVLASGPTET 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
366-531 |
1.55e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 366 SFGYEEN---KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDgknikeydmnslrskigvVLQD 442
Cdd:COG2401 33 AFGVELRvveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 443 TYLFAGTIMDNIryGRLDASDE--EVINAAKAASAHSFIKHLpnqyetkiasegSNLSQGQKQLLAIARAILADADILIL 520
Cdd:COG2401 95 QFGREASLIDAI--GRKGDFKDavELLNAVGLSDAVLWLRRF------------KELSTGQKFRFRLALLLAERPKLLVI 160
|
170
....*....|.
gi 447166279 521 DEATSNIDTRT 531
Cdd:COG2401 161 DEFCSHLDRQT 171
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
364-588 |
1.86e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 71.68 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 364 NVSFGYEE-NKTILKEVSLKARPGETIALVGPTGSGKT----TIINLLTRFYDIQqGQIHIDGK---NIKEYDMNSLRS- 434
Cdd:PRK09473 19 RVTFSTPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGReilNLPEKELNKLRAe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 435 KIGVVLQDT------YLFAGT-----IMDNIRYGRLDASDEEV--INAAKAASAHSFIKHLPNQYetkiasegsnlSQGQ 501
Cdd:PRK09473 98 QISMIFQDPmtslnpYMRVGEqlmevLMLHKGMSKAEAFEESVrmLDAVKMPEARKRMKMYPHEF-----------SGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 502 KQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRD-RTSFV-IAHRLKTIEK-ADQILVIKDGSILEKGNH 578
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNA 246
|
250
....*....|
gi 447166279 579 ESLmedrgFY 588
Cdd:PRK09473 247 RDV-----FY 251
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
376-570 |
1.92e-13 |
|
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: 70.19 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLrskigVVLQDTYLFAG-TIMDNI 454
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 455 rygrldasdeevinaakAASAHSFIKHLPNQYETKIASEG--------------SNLSQGQKQLLAIARAILADADILIL 520
Cdd:TIGR01184 76 -----------------ALAVDRVLPDLSKSERRAIVEEHialvglteaadkrpGQLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447166279 521 DEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRL-KTIEKADQILVIKDG 570
Cdd:TIGR01184 139 DEPFGALDALTRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
360-576 |
3.17e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.04 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKtILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGK--NIKEYDMNSLRSKIG 437
Cdd:PRK13638 2 LATSDLWFRYQDEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 438 VVLQD--TYLFAGTIMDNIRYG--RLDASDEEVI----NAAKAASAHSFiKHLPNQYetkiasegsnLSQGQKQLLAIAR 509
Cdd:PRK13638 81 TVFQDpeQQIFYTDIDSDIAFSlrNLGVPEAEITrrvdEALTLVDAQHF-RHQPIQC----------LSHGQKKRVAIAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 510 AILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVI-AHRLKTI-EKADQILVIKDGSILEKG 576
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIyEISDAVYVLRQGQILTHG 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
360-528 |
5.09e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.75 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI---KEYDMNSLRSKI 436
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAG-TIMDNIRYGRL--DASDEEVINAAKAASAHSFI----KHLPNQyetkiasegsnLSQGQKQLLAIAR 509
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIPLIiaGASGDDIRRRVSAALDKVGLldkaKNFPIQ-----------LSGGEQQRVGIAR 150
|
170
....*....|....*....
gi 447166279 510 AILADADILILDEATSNID 528
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLD 169
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
360-581 |
5.81e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.96 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFgyEENKTILKEVSLKARPGETIALVGPTGSGKT----TIINLLTRFYDIQQGQIHIDGKnikEYDMNSLRSK 435
Cdd:PRK10418 5 IELRNIAL--QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGK---PVAPCALRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 IgvvlqdtylfAGTIMDNIR-------------------YGRL--DASDEEVINAAKAASAHSFIKHLPNQyetkiaseg 494
Cdd:PRK10418 80 K----------IATIMQNPRsafnplhtmhtharetclaLGKPadDATLTAALEAVGLENAARVLKLYPFE--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 495 snLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTS--FVIAHRLKTIEK-ADQILVIKDGS 571
Cdd:PRK10418 141 --MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGR 218
|
250
....*....|
gi 447166279 572 ILEKGNHESL 581
Cdd:PRK10418 219 IVEQGDVETL 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
373-589 |
6.17e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.52 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNsLRSK--IGVVLQDTYLFAG-T 449
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMH-KRARlgIGYLPQEASIFRKlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 450 IMDNI-------------RYGRLDASDEEvinaakaasahsF-IKHLPNQYetkiaseGSNLSQGQKQLLAIARAILADA 515
Cdd:COG1137 95 VEDNIlavlelrklskkeREERLEELLEE------------FgITHLRKSK-------AYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 516 DILILDEATSNIDTRTELQIQEGLNNLmRDR-TSFVIA-HR----LKTIEKAdqiLVIKDGSILEKGNHESLMED---RG 586
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHL-KERgIGVLITdHNvretLGICDRA---YIISEGKVLAEGTPEEILNNplvRK 231
|
...
gi 447166279 587 FYF 589
Cdd:COG1137 232 VYL 234
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
47-330 |
8.02e-13 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 69.18 E-value: 8.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 47 IFLVFVTTLLGLLGPYLMGVIIDQyiVPKDLSGTARMCLLLIAIYGVTVFLT----WLQTFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18560 2 LLLLILGKACNVLAPLFLGRAVNA--LTLAKVKDLESAVTLILLYALLRFSSkllkELRSLLYRRVQQNAYRELSLKTFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGV-AIAMFALDWILAIVTLITVPIMFFVTKKL 201
Cdd:cd18560 80 HLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVsVVFAFHFGAWLALIVFLSVLLYGVFTIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 202 VAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGL 281
Cdd:cd18560 160 TEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 447166279 282 VIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAG 330
Cdd:cd18560 240 GLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTD 288
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
379-576 |
8.49e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.48 E-value: 8.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 379 VSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLrSKIGVV--LQDTYLFAG-TIMDNI- 454
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVrtFQHVRLFREmTVIENLl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 455 -------------------RYGRldaSDEEVINAAKAASAHSFIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILADA 515
Cdd:PRK11300 103 vaqhqqlktglfsgllktpAFRR---AESEALDRAATWLERVGLLEHANR-------QAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 516 DILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTI-EKADQILVIKDGSILEKG 576
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVmGISDRIYVVNQGTPLANG 236
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
87-334 |
8.76e-13 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 69.11 E-value: 8.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 87 LIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSA 166
Cdd:cd18574 48 LLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 167 LTFIGVAIAMFALDWILAIVTLITVPIMFFV----TKKLVAYSGKnfAKRQkdLGELNGFIEEAITgaDVTTL--YGKEK 240
Cdd:cd18574 128 TQTVGCVVSLYLISPKLTLLLLVIVPVVVLVgtlyGSFLRKLSRR--AQAQ--VAKATGVADEALG--NIRTVraFAMED 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 241 KTVQNFNKINEQLRVSATKADT----FSAFifpSMNFINNLGMGlVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQ 316
Cdd:cd18574 202 RELELYEEEVEKAAKLNEKLGLgigiFQGL---SNLALNGIVLG-VLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQ 277
|
250
....*....|....*...
gi 447166279 317 FATLMNTIQAAVAGGERV 334
Cdd:cd18574 278 LSVLFGQYVKGKSAGARV 295
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
43-199 |
1.41e-12 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 68.68 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFE 122
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 123 KIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVTK 199
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQR 157
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
350-572 |
2.59e-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: 65.53 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 350 AFVVQNLQGHVALENVSFgyeenktilkevslKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDM 429
Cdd:cd03215 4 VLEVRGLSVKGAVRDVSF--------------EVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 430 -NSLRSKIGVVLQD---TYLFAG-TIMDNIRYGRLdasdeevinaakaasahsfikhlpnqyetkiasegsnLSQGQKQL 504
Cdd:cd03215 70 rDAIRAGIAYVPEDrkrEGLVLDlSVAENIALSSL-------------------------------------LSGGNQQK 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 505 LAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIahrLKT-----IEKADQILVIKDGSI 572
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
356-594 |
2.82e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 67.35 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 356 LQGHVALENVSFGYEENKTiLKEVSLKARPGETIALVGPTGSGKTTIINLLTRFY---DIQQGQIHIDGKNIKE-----Y 427
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQA-LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQRegrlaR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 428 DMNSLRSKIGVVLQDTYLFAG-TIMDNIRYGRLDAS----------DEEVINAAKAASAHSFIKHLPNQyetkiasEGSN 496
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLVNRlSVLENVLIGALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQ-------RVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 497 LSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLK-TIEKADQILVIKDGSIL 573
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVF 232
|
250 260
....*....|....*....|..
gi 447166279 574 EKGNHESLMEDRgfyFD-LYTS 594
Cdd:PRK09984 233 YDGSSQQFDNER---FDhLYRS 251
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
360-565 |
3.25e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALEN--VSFGyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeydmnsLRskIG 437
Cdd:PRK09544 5 VSLENvsVSFG---QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 438 VVLQDTYLFAGTIMDNIRYGRL--DASDEEVINAAKAASAhsfiKHLPNQYETKiasegsnLSQGQKQLLAIARAILADA 515
Cdd:PRK09544 71 YVPQKLYLDTTLPLTVNRFLRLrpGTKKEDILPALKRVQA----GHLIDAPMQK-------LSGGETQRVLLARALLNRP 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447166279 516 DILILDEATSNIDTRTELQIQEGLNNLMRDRTSFV--IAHRLKTI-EKADQIL 565
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVlmVSHDLHLVmAKTDEVL 192
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
371-587 |
4.55e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.35 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLT--RFYDIQQGQIHIDGKNIKEYDMNSlRSKIGVVLQDTY---- 444
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIFMAFQYpvei 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 445 ------LFAGTIMDNIRYGR----LDASDEEVINAAKAAsahsfIKHLPNQYETKIASEGsnLSQGQKQLLAIARAILAD 514
Cdd:PRK09580 91 pgvsnqFFLQTALNAVRSYRgqepLDRFDFQDLMEEKIA-----LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIA---HRLKTIEKADQILVIKDGSILEKGNHESL--MEDRGF 587
Cdd:PRK09580 164 PELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDFTLVkqLEEQGY 241
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
40-334 |
6.05e-12 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 66.73 E-value: 6.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 40 KAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGtarMCLLLIAIYGVTVF---LTWLQTFVMVNVALKTIQKI 116
Cdd:cd18569 1 RSALLFVVLAGLLLVIPGLVIPVFSRIFIDDILVGGLPDW---LRPLLLGMALTALLqglLTWLQQYYLLRLETKLALSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 117 RQDIFEKIQTLSLRFFDVRSQGDLMSRVtndidnlnqALTQSVVQIISSAL--TFIGV------AIAMFALDWILAIVTL 188
Cdd:cd18569 78 SSRFFWHVLRLPVEFFSQRYAGDIASRV---------QSNDRVANLLSGQLatTVLNLvmavfyALLMLQYDVPLTLIGI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 189 ITVPIMFFVTKKLVAYSGKNFAKRQKDLGELNGFIEEAI--------TGAD------VTTLYGKEKKTVQNFNKINEQLR 254
Cdd:cd18569 149 AIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTTMSGLqmietlkaSGAEsdffsrWAGYQAKVLNAQQELGRTNQLLG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 255 VSATkadtfsafifpsmnFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18569 229 ALPT--------------LLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
371-577 |
6.43e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.87 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikeydMNSLrskIGVvlqdtylfaGTI 450
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---LEL---------GAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 451 M-------DNIR-YGR-LDASDEEVinAAKAASAHSF----------IKHlpnqYetkiasegsnlSQGQKQLLAIARAI 511
Cdd:COG1134 99 FhpeltgrENIYlNGRlLGLSRKEI--DEKFDEIVEFaelgdfidqpVKT----Y-----------SSGMRARLAFAVAT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 512 LADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIA-HRLKTIEK-ADQILVIKDGSILEKGN 577
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVsHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
361-583 |
6.63e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.96 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 361 ALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVL 440
Cdd:PRK10575 13 ALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 441 QDTYLFAGTIMDNI----RY------GRLDASDEEVINAAKAASAhsfIKHLPNQYEtkiasegSNLSQGQKQLLAIARA 510
Cdd:PRK10575 92 QQLPAAEGMTVRELvaigRYpwhgalGRFGAADREKVEEAISLVG---LKPLAHRLV-------DSLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 511 ILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAhRLKTIEKA----DQILVIKDGSILEKGNHESLME 583
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELMR 237
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
338-571 |
1.09e-11 |
|
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: 64.76 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 338 MDEVPEIKNKKDAFVVQNLQGhvalenvsfgyeenKTI--LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQG 415
Cdd:COG4778 1 MTTLLEVENLSKTFTLHLQGG--------------KRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 416 QIHIDGKN-------IKEYDMNSLRSK-IGVVLQdtylFAGTIMdniRYGRLD----------ASDEEVINAAKAASAHS 477
Cdd:COG4778 67 SILVRHDGgwvdlaqASPREILALRRRtIGYVSQ----FLRVIP---RVSALDvvaepllergVDREEARARARELLARL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 478 FIK----HLPNqyetkiasegSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFV-IA 552
Cdd:COG4778 140 NLPerlwDLPP----------ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIF 209
|
250 260
....*....|....*....|
gi 447166279 553 HRLKTIEK-ADQILVIKDGS 571
Cdd:COG4778 210 HDEEVREAvADRVVDVTPFS 229
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
385-528 |
1.19e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 66.44 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 385 PGETI-ALVGPTGSGKTTIINL---LTRfydIQQGQIHIDGKNIKEYDMN-SL---RSKIGVVLQDTYLFAG-TIMDNIR 455
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAisgLTR---PQKGRIVLNGRVLFDAEKGiCLppeKRRIGYVFQDARLFPHyKVRGNLR 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 456 YGrLDASDEEVINAAKAASAhsfIKHLPNQYEtkiasegSNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:PRK11144 99 YG-MAKSMVAQFDKIVALLG---IEPLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
343-583 |
1.25e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.40 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 343 EIKNKKDAFvvqnlQGHVALENVSFgyeenkTILKevslkarpGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGK 422
Cdd:PRK11607 21 EIRNLTKSF-----DGQHAVDDVSL------TIYK--------GEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 423 NIKeyDMNSLRSKIGVVLQDTYLFAG-TIMDNIRYG-RLDASDEEVINAAKA---ASAH--SFIKHLPNQyetkiasegs 495
Cdd:PRK11607 82 DLS--HVPPYQRPINMMFQSYALFPHmTVEQNIAFGlKQDKLPKAEIASRVNemlGLVHmqEFAKRKPHQ---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 496 nLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQ-EGLNNLMR-DRTSFVIAH-RLKTIEKADQILVIKDGSI 572
Cdd:PRK11607 150 -LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKF 228
|
250
....*....|.
gi 447166279 573 LEKGNHESLME 583
Cdd:PRK11607 229 VQIGEPEEIYE 239
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
362-582 |
1.48e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGyeenkTILKEVSLKARPGETIALVGPTGSGKTTiinLLTRFYDI--QQGQIHIDGKNIKEYDMNSL-RSKIGV 438
Cdd:PRK03695 3 LNDVAVS-----TRLGPLSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAAELaRHRAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 439 VLQDTYLFAgtiMDNIRYgrLDASDEEVINAAKAASAHSFIKHLPnQYETKIASEGSNLSQGQKQ-------LLAIARAI 511
Cdd:PRK03695 75 SQQQTPPFA---MPVFQY--LTLHQPDKTRTEAVASALNEVAEAL-GLDDKLGRSVNQLSGGEWQrvrlaavVLQVWPDI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 512 LADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIA-HRL-KTIEKADQILVIKDGSILEKGNHESLM 582
Cdd:PRK03695 149 NPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSsHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
376-574 |
1.78e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.74 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDI--QQGQIHIDG-----KNIKEydmnSLRSKIGVVLQD----TY 444
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGevcrfKDIRD----SEALGIVIIHQElaliPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 445 LfagTIMDNI-------RYGRLDAsdEEVINAAKAASAHSFIKHLPnqyETKIasegSNLSQGQKQLLAIARAILADADI 517
Cdd:NF040905 93 L---SIAENIflgneraKRGVIDW--NETNRRARELLAKVGLDESP---DTLV----TDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 518 LILDEATSNI---DTRTELQIQEGLnnlmRDR--TSFVIAHRLKTIEK-ADQILVIKDGSILE 574
Cdd:NF040905 161 LILDEPTAALneeDSAALLDLLLEL----KAQgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
387-591 |
2.40e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.96 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 387 ETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIkEYDMNSLRSKIGVVLQDTYLFAG-TIMDNIR-YGRLDA-SD 463
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILfYAQLKGrSW 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 464 EEVINAAKAASAHSFIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLM 543
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHHKRNE-------EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR 1108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447166279 544 RDRTSFVIAHRLKTIE-KADQILVIKDGSILEKGNHESLME--DRGFYFDL 591
Cdd:TIGR01257 1109 SGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLKNcfGTGFYLTL 1159
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
361-581 |
3.83e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.88 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 361 ALENVSFGY---EENKTILKEVSLKARPGETIALVGPTGSGKT----TIINLL-TRFYDIQQGQIHIDGKNIKEYDMNSL 432
Cdd:PRK15134 7 AIENLSVAFrqqQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLHASEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 433 R----SKIGVVLQDTyLFAGTIMDNI-----------RYGRLDASDEEVINAAKAASAHSFIKHL---PNQyetkiaseg 494
Cdd:PRK15134 87 RgvrgNKIAMIFQEP-MVSLNPLHTLekqlyevlslhRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQ--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 495 snLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--DRTSFVIAHRLKTIEK-ADQILVIKDGS 571
Cdd:PRK15134 157 --LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGR 234
|
250
....*....|
gi 447166279 572 ILEKGNHESL 581
Cdd:PRK15134 235 CVEQNRAATL 244
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
376-577 |
4.57e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 63.66 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIkEYDMNSLRS-KIGVVLQD--TYLFA----G 448
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRSqRIRMIFQDpsTSLNPrqriS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 449 TIMD-NIRYG-RLDASD-EEVINAAKAAsahsfIKHLP---NQYETKIASegsnlsqGQKQLLAIARAILADADILILDE 522
Cdd:PRK15112 108 QILDfPLRLNtDLEPEQrEKQIIETLRQ-----VGLLPdhaSYYPHMLAP-------GQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447166279 523 ATSNIDTRTELQIQeglnNLMRDRTS-------FVIAHRLKTIEKADQILVIKDGSILEKGN 577
Cdd:PRK15112 176 ALASLDMSMRSQLI----NLMLELQEkqgisyiYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
360-572 |
4.59e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.54 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENkTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIhIDGKNikeyDMNSLRSKIGVV 439
Cdd:PRK11247 13 LLLNAVSKRYGER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTA----PLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQDTYLFA-GTIMDNIRYG-----RLDAsdEEVINAAKAASAhsfikhlpnqyetkiASE-GSNLSQGQKQLLAIARAIL 512
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGlkgqwRDAA--LQALAAVGLADR---------------ANEwPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 513 ADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRL-KTIEKADQILVIKDGSI 572
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
40-325 |
5.55e-11 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 63.72 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 40 KAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGtarMCLLLIAIYGVTVF---LTWLQTFVMVNVALKTIQKI 116
Cdd:cd18779 1 PGLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDL---LGVLGLGLAALVLTqllAGLLRSHLLLRLRTRLDTQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 117 RQDIFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTL----ITVP 192
Cdd:cd18779 78 TLGFLEHLLRLPYRFFQQRSTGDLLMRL-SSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLglaaLQVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 193 IMFFVTKKLVAYSGKNFAKRqkdlGELNGFIEEAITGADVTTLYGKEKKTVQNF-NKINEQLRVSATKAdTFSAFIFPSM 271
Cdd:cd18779 157 LLLATRRRVRELMARELAAQ----AEAQSYLVEALSGIETLKASGAEDRALDRWsNLFVDQLNASLRRG-RLDALVDALL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447166279 272 NFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLsqfATLMNTIQ 325
Cdd:cd18779 232 ATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPL---ASLVGTAQ 282
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
42-334 |
6.33e-11 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 63.51 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 42 ALTFIIFLVFVTTLLgllgPYLMGVIID----QYIVPKDLSGTARMCLLLIaiyGVTVFLTWLQTFVMVNVAlKTIQKIR 117
Cdd:cd18590 1 AFLFLTLAVICETFI----PYYTGRVIDilggEYQHNAFTSAIGLMCLFSL---GSSLSAGLRGGLFMCTLS-RLNLRLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 118 QDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFV 197
Cdd:cd18590 73 HQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 198 TKKLVAYSGKNFAKRQKDLGELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNL 277
Cdd:cd18590 153 QKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 278 GMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAAVAGGERV 334
Cdd:cd18590 233 VQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
358-572 |
8.19e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.65 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 358 GHVALE--NVSfgyeeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKnikEYDMNSLRSK 435
Cdd:COG1129 253 GEVVLEveGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK---PVRIRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 436 I--GVVL-----QDTYLFAG-TIMDNI---------RYGRLDASDEEvinaakaASAHSFIKhlpnQYETKIASEG---S 495
Cdd:COG1129 325 IraGIAYvpedrKGEGLVLDlSIRENItlasldrlsRGGLLDRRRER-------ALAEEYIK----RLRIKTPSPEqpvG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 496 NLSQGQKQLLAIARAILADADILILDEATSNID--TRTELQiqeglnNLMRDrtsfvIAHRLKTI-----------EKAD 562
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEIY------RLIRE-----LAAEGKAVivisselpellGLSD 462
|
250
....*....|
gi 447166279 563 QILVIKDGSI 572
Cdd:COG1129 463 RILVMREGRI 472
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
360-583 |
1.05e-10 |
|
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: 64.44 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLL--TRFYDIQQGQI-----------HID------ 420
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgYVErpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 421 ------GKNIKEYDMN----------SLRSKIGVVLQDTYLFAG--TIMDNIrygrLDASDEEVINAAKAAS-AHSFIKH 481
Cdd:TIGR03269 80 epcpvcGGTLEPEEVDfwnlsdklrrRIRKRIAIMLQRTFALYGddTVLDNV----LEALEEIGYEGKEAVGrAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 482 LpnQYETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIE 559
Cdd:TIGR03269 156 V--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIE 233
|
250 260
....*....|....*....|....*
gi 447166279 560 K-ADQILVIKDGSILEKGNHESLME 583
Cdd:TIGR03269 234 DlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
373-537 |
1.66e-10 |
|
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: 60.97 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 373 KTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAGTIMD 452
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 453 NIRYGRLDASDEEVINAAKAASAHSFiKHLPNQYetkiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTE 532
Cdd:cd03231 93 NLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
....*
gi 447166279 533 LQIQE 537
Cdd:cd03231 162 ARFAE 166
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
362-533 |
1.83e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 362 LENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDgknikeydmnslrSKIGVVLQ 441
Cdd:PRK11147 322 MENVNYQIDG-KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-------------TKLEVAYF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 442 DTYLFA----GTIMDNIRYGRldasdEEV-INAAKaasAH------SFIKHlPNQYETKIASegsnLSQGQKQLLAIARA 510
Cdd:PRK11147 388 DQHRAEldpeKTVMDNLAEGK-----QEVmVNGRP---RHvlgylqDFLFH-PKRAMTPVKA----LSGGERNRLLLARL 454
|
170 180
....*....|....*....|....
gi 447166279 511 ILADADILILDEATSNIDTRT-EL 533
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETlEL 478
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
360-544 |
2.13e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.55 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIkeydmNSLRSK---I 436
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-----NELEPAdrdI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 437 GVVLQDTYLFAG-TIMDNIRYG----RLDAS--DEEVINAAKAASAHSFIKHLPNQyetkiasegsnLSQGQKQLLAIAR 509
Cdd:PRK11650 79 AMVFQNYALYPHmSVRENMAYGlkirGMPKAeiEERVAEAARILELEPLLDRKPRE-----------LSGGQRQRVAMGR 147
|
170 180 190
....*....|....*....|....*....|....*
gi 447166279 510 AILADADILILDEATSNIDTRteLQIQeglnnlMR 544
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAK--LRVQ------MR 174
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
376-570 |
2.21e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.21 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI-----KEydmnSLRSKIGVVLQDTYLFAG-T 449
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkssKE----ALENGISMVHQELNLVLQrS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 450 IMDNIRYGR-----LDASDEEVINAAKAASAHSFIKHLPNQyetKIAsegsNLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:PRK10982 90 VMDNMWLGRyptkgMFVDQDKMYRDTKAIFDELDIDIDPRA---KVA----TLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447166279 525 SNIdTRTELQIQEGLNNLMRDRTSFV--IAHRLKTIEK-ADQILVIKDG 570
Cdd:PRK10982 163 SSL-TEKEVNHLFTIIRKLKERGCGIvyISHKMEEIFQlCDEITILRDG 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
348-581 |
2.92e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.95 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 348 KDAFVVQNLqghvaleNVSFGYEENKT-ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIH-------- 418
Cdd:PRK10261 10 RDVLAVENL-------NIAFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 419 -----IDGKNIKEYDMNSLR-SKIGVVLQD-------TYLFAGTIMDNIRYGRlDASDEEVINAAK-------AASAHSF 478
Cdd:PRK10261 83 rsrqvIELSEQSAAQMRHVRgADMAMIFQEpmtslnpVFTVGEQIAESIRLHQ-GASREEAMVEAKrmldqvrIPEAQTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 479 IKHLPNQyetkiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFV--IAHRLK 556
Cdd:PRK10261 162 LSRYPHQ-----------LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMG 230
|
250 260
....*....|....*....|....*.
gi 447166279 557 TI-EKADQILVIKDGSILEKGNHESL 581
Cdd:PRK10261 231 VVaEIADRVLVMYQGEAVETGSVEQI 256
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
40-327 |
3.10e-10 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 61.38 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 40 KAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQD 119
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTL-----ITVPIM 194
Cdd:cd18783 81 TFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLafsalIALIIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 195 FFVtkklvaysgKNFAKRQKDL----GELNGFIEEAITGAD-VTTLyGKEKKTVQNFNKINEQLRVSATKADTFSAFIFP 269
Cdd:cd18783 160 AFL---------PPFRRRLQALyraeGERQAFLVETVHGIRtVKSL-ALEPRQRREWDERVARAIRARFAVGRLSNWPQT 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 270 SMNFINNLGMGLVIGTGSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAA 327
Cdd:cd18783 230 LTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEA 287
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
86-263 |
3.25e-10 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 61.52 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 86 LLIAIYGVTVFLT-WLQTFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIIS 164
Cdd:cd18558 63 YYYLIIGAIVLITaYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 165 SALTFIGVAIAMFALDWILAIVTLITVPIMFFV----TKKLVAYSGKNfakrQKDLGELNGFIEEAITGADVTTLYGKEK 240
Cdd:cd18558 143 NIATFGTGFIIGFIRGWKLTLVILAISPVLGLSavvwAKILSGFTDKE----KKAYAKAGAVAEEVLEAFRTVIAFGGQQ 218
|
170 180
....*....|....*....|....
gi 447166279 241 KTVQNFNK-INEQLRVSATKADTF 263
Cdd:cd18558 219 KEETRYAQnLEIAKRNGIKKAITF 242
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
110-303 |
3.62e-10 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 61.34 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 110 LKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLI 189
Cdd:cd18585 64 FRLLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 190 TVPIMFFVTKKLVAYSGKNFAKRQKDL-GELNGFIEEAITGADVTTLYGKEKKTVQNFNKINEQLRVSATKADTFSAFIF 268
Cdd:cd18585 144 GLLLAGVVIPLLFYRLGKKIGQQLVQLrAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQ 223
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 447166279 269 PSMNFINNLGMGLVIGTGSVMVLNG--------MTTVGVIAAF 303
Cdd:cd18585 224 ALMILLSGLTVWLVLWLGAPLVQNGaldgallaMLVFAVLASF 266
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
374-528 |
3.62e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 59.68 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 374 TILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIkeydmnslrSKIGVVLQDTYLFAG----- 448
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL---------AEQRDEPHENILYLGhlpgl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 449 ----TIMDNIR-YGRLDASDEEVINAAKAASAHSFIKHLPNQYetkiasegsnLSQGQKQLLAIARAILADADILILDEA 523
Cdd:TIGR01189 85 kpelSALENLHfWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEP 154
|
....*
gi 447166279 524 TSNID 528
Cdd:TIGR01189 155 TTALD 159
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
371-570 |
4.57e-10 |
|
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: 59.18 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYD--IQQGQIHIDGKNIKEydmnSLRSKIGVVLQ-DTYLFA 447
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDK----NFQRSTGYVEQqDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 448 GTIMDNIRYgrldasdeevinaakaaSAhsfikhlpnqyetkiASEGsnLSQGQKQLLAIARAILADADILILDEATSNI 527
Cdd:cd03232 94 LTVREALRF-----------------SA---------------LLRG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447166279 528 DTRTELQIQEGLNNLMRD-RTSFVIAHR--LKTIEKADQILVIKDG 570
Cdd:cd03232 140 DSQAAYNIVRFLKKLADSgQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
371-590 |
5.05e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.20 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRfyDIQ----QGQIHIDGKNIKEYDMNslrsKIGVVLQDTYLF 446
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RIQgnnfTGTILANNRKPTKQILK----RTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 447 AG-TIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLP-NQYETKIASEG--SNLSQGQKQLLAIARAILADADILILDE 522
Cdd:PLN03211 153 PHlTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGlTKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 523 ATSNIDTRTELQIQEGLNNLmrdrtsfviAHRLKTI------------EKADQILVIKDGSILEKGNHESLMedrgFYFD 590
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSL---------AQKGKTIvtsmhqpssrvyQMFDSVLVLSEGRCLFFGKGSDAM----AYFE 299
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
378-576 |
6.06e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 60.32 E-value: 6.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 378 EVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSL---------RSKIGVVLQDTylfag 448
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHP----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 449 tiMDNIR--------------------YGRL--DASD--EEV-INAAKaasahsfIKHLPNQYetkiasegsnlSQGQKQ 503
Cdd:PRK11701 99 --RDGLRmqvsaggnigerlmavgarhYGDIraTAGDwlERVeIDAAR-------IDDLPTTF-----------SGGMQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 504 LLAIARAILADADILILDEATSNIDtrteLQIQEGLNNLMRDRTS------FVIAH-----RLktieKADQILVIKDGSI 572
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLD----VSVQARLLDLLRGLVRelglavVIVTHdlavaRL----LAHRLLVMKQGRV 230
|
....
gi 447166279 573 LEKG 576
Cdd:PRK11701 231 VESG 234
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
45-214 |
1.54e-09 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 59.42 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 45 FIIFLVFVTTLLGLLGPYLMGVIIdQYIVPKDLSGTARMCLLLIAIYGVTVFLT------WLQTFVM---VNVALKTIqk 115
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLI-SYLSSYPDEPLSEGYLLALALFLVSLLQSlllhqyFFLSFRLgmrVRSALSSL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 116 irqdIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALtQSVVQIISSALTFIGVAIAMFA-LDW-ILA--IVTLITV 191
Cdd:cd18579 78 ----IYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLYRlLGWaALAglGVLLLLI 152
|
170 180
....*....|....*....|...
gi 447166279 192 PIMFFVTKKLVAYSGKNFAKRQK 214
Cdd:cd18579 153 PLQAFLAKLISKLRKKLMKATDE 175
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
375-584 |
2.15e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 375 ILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNsLRSKIGVVL--QDTYLFAG-TIM 451
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIYLvpQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 452 DNIRYGRLDASDEEVINAAKAASAHSfikHLpnqyetKIASEGSNLSQGQKQLLAIARAILADADILILDEATSN---ID 528
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQLLAALGC---QL------DLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASltpAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 529 TRTEL-QIQEGLNnlmRDRTSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK15439 176 TERLFsRIRELLA---QGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTD 230
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
40-189 |
2.66e-09 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 58.61 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 40 KAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQD 119
Cdd:cd18571 1 KKLILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNFIYLILIAQLVLFLGSTSIEFIRSWILLHISSRINISIISD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 120 IFEKIQTLSLRFFDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLI 189
Cdd:cd18571 81 FLIKLMRLPISFFDTKMTGDILQRI-NDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLI 149
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
44-338 |
6.69e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 57.48 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 44 TFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYG----VTVFLTWLQTFVMVNVALKTIQKIRQD 119
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEVSVLYYLGIYAlislLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 120 IFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMFFVtk 199
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYI-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 200 klvaysGKNFAKRQKDLGELN--------GFIEEAITGadVTTL--YGKEKK-TVQNFNKINEQLRVSatkadtfsaFIF 268
Cdd:cd18604 160 ------GRLYLRASRELKRLEsvarspilSHFGETLAG--LVTIraFGAEERfIEEMLRRIDRYSRAF---------RYL 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 269 PSMNF-----INNLGMGLVIGTGSVMVLNGMTTVGvIAAF-INYSRQFSRPLSQFATLMNTIQA---AVaggERVFEIM 338
Cdd:cd18604 223 WNLNRwlsvrIDLLGALFSFATAALLVYGPGIDAG-LAGFsLSFALGFSSAILWLVRSYNELELdmnSV---ERIQEYL 297
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
360-586 |
1.43e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.59 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 360 VALENVSFGYEeNKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTrfydiqqGQIHIDGKNIKEydmnSLRSKIGVV 439
Cdd:PRK15064 320 LEVENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-------GELEPDSGTVKW----SENANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 440 LQD-TYLFAG--TIMDNIRYGRLDASDEEVINAAKAasahsfiKHLPNQYETKiaSEGSNLSQGQKQLLAIARAILADAD 516
Cdd:PRK15064 388 AQDhAYDFENdlTLFDWMSQWRQEGDDEQAVRGTLG-------RLLFSQDDIK--KSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 517 ILILDEATSNIDtrteLQIQEGLNN--LMRDRTSFVIAH-RLKTIEKADQILVIKDGSILE-KGNHESLMEDRG 586
Cdd:PRK15064 459 VLVMDEPTNHMD----MESIESLNMalEKYEGTLIFVSHdREFVSSLATRIIEITPDGVVDfSGTYEEYLRSQG 528
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
372-572 |
2.42e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-QGQIHIDGKNIK-EYDMNSLRSKIGVVLQDTYLFaG- 448
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKiRNPQQAIAQGIAMVPEDRKRD-Gi 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 449 -TIMD---NIRYGRLDA-SDEEVIN-AAKAASAHSFIKHLpnqyETKIAS---EGSNLSQGQKQLLAIARAILADADILI 519
Cdd:PRK13549 353 vPVMGvgkNITLAALDRfTGGSRIDdAAELKTILESIQRL----KVKTASpelAIARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 520 LDEATSNIDTRTELQIQEGLNNLMRDRTS-FVIAHRLKTI-EKADQILVIKDGSI 572
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQLVQQGVAiIVISSELPEVlGLSDRVLVMHEGKL 483
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
369-566 |
2.52e-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: 55.11 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 369 YEENKTILKEVSLKARPG-----ETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIK--------EYDMNS---L 432
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikaDYEGTVrdlL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 433 RSKIGVVLQDTYLfagtimdnirygrldasDEEVINaakaasahsfikhlPNQYETKIASEGSNLSQGQKQLLAIARAIL 512
Cdd:cd03237 83 SSITKDFYTHPYF-----------------KTEIAK--------------PLQIEQILDREVPELSGGELQRVAIAACLS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 513 ADADILILDEATSNIDTRTELQIQEGLNNLM--RDRTSFVIAHRLKTIEK-ADQILV 566
Cdd:cd03237 132 KDADIYLLDEPSAYLDVEQRLMASKVIRRFAenNEKTAFVVEHDIIMIDYlADRLIV 188
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
385-572 |
2.84e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.15 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 385 PGETIALVGPTGSGKTTIINLLTRFYDIQQGQIH-IDGKNIKEYDMNSLRskigvvlqdtylfagtimdnirygrldasd 463
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 464 eevinaakaasahsfikhlpnqyETKIASEGSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQE------ 537
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrl 107
|
170 180 190
....*....|....*....|....*....|....*
gi 447166279 538 GLNNLMRDRTSFVIAHRLKTIEKADQILVIKDGSI 572
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRI 142
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
364-528 |
3.81e-08 |
|
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: 56.10 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 364 NVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINlltrfydIQQGqihIDgkniKEYDMNSLRS---KIGVVL 440
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD----KDFNGEARPQpgiKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 441 QDTYLFAG-TIMDNIRYG---RLDASDE-EVINAAKAASAHSFIKHLPNQ--YETKIASEG------------------- 494
Cdd:TIGR03719 75 QEPQLDPTkTVRENVEEGvaeIKDALDRfNEISAKYAEPDADFDKLAAEQaeLQEIIDAADawdldsqleiamdalrcpp 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 447166279 495 -----SNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:TIGR03719 155 wdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
378-572 |
3.98e-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: 55.99 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 378 EVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQ-QGQIHIDGKNIKEYD-MNSLRSKIGVVLQDTYLfAGTIMD--- 452
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRKR-HGIVPIlgv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 453 --NIRYGRLDA-SDEEVINAAKAASAhsfIKHLPNQYETKIASEG---SNLSQGQKQLLAIARAILADADILILDEATSN 526
Cdd:TIGR02633 357 gkNITLSVLKSfCFKMRIDAAAELQI---IGSAIQRLKVKTASPFlpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 447166279 527 IDTRTELQIQEGLNNLMRDRTSF-VIAHRL-KTIEKADQILVIKDGSI 572
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQEGVAIiVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
332-584 |
3.99e-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: 55.96 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 332 ERVFEIMDEVPEIKNKKDAFVVQNLqghVALENVSFGY-EENKTILKEV---SLKARPGETIALVGPTGSGKTTIINLLT 407
Cdd:TIGR03269 255 EVVAVFMEGVSEVEKECEVEVGEPI---IKVRNVSKRYiSVDRGVVKAVdnvSLEVKEGEIFGIVGTSGAGKTTLSKIIA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 408 RFYDIQQGQIHID-GKN----IKEYDMNSLRSK--IGVVLQDTYLFA-GTIMDNIRYG-RLDASDE----EVINAAKAAS 474
Cdd:TIGR03269 332 GVLEPTSGEVNVRvGDEwvdmTKPGPDGRGRAKryIGILHQEYDLYPhRTVLDNLTEAiGLELPDElarmKAVITLKMVG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 475 -----AHSFIKHLPNQyetkiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRD--RT 547
Cdd:TIGR03269 412 fdeekAEEILDKYPDE-----------LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQT 480
|
250 260 270
....*....|....*....|....*....|....*...
gi 447166279 548 SFVIAHRLKTI-EKADQILVIKDGSILEKGNHESLMED 584
Cdd:TIGR03269 481 FIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
354-584 |
5.92e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.39 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 354 QNLQGHVALENVSFGyEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSL- 432
Cdd:PRK11831 2 QSVANLVDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 433 --RSKIGVVLQDTYLFAG-TIMDNIRY-----GRLDAS--DEEVINAAKAASAHSFIKHLPnqyetkiasegSNLSQGQK 502
Cdd:PRK11831 81 tvRKRMSMLFQSGALFTDmNVFDNVAYplrehTQLPAPllHSTVMMKLEAVGLRGAAKLMP-----------SELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 503 QLLAIARAILADADILILDEATSNIDTRTE---LQIQEGLNNLMrDRTSFVIAHRL-KTIEKADQILVIKDGSILEKGNH 578
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMgvlVKLISELNSAL-GVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSA 228
|
....*.
gi 447166279 579 ESLMED 584
Cdd:PRK11831 229 QALQAN 234
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
382-566 |
6.04e-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: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 382 KARPGETIALVGPTGSGKTTIINLLTrfydiqqGQIHIDGKNIKEydmnslRSKIGVVLQdtYL---FAGTIMDNIRygr 458
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILA-------GVLKPDEGEVDE------DLKISYKPQ--YIspdYDGTVEEFLR--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 459 ldasdeeviNAAKAASAHSFIKH-------LPNQYETKIasegSNLSQGQKQLLAIARAILADADILILDEATSNIDTRT 531
Cdd:COG1245 424 ---------SANTDDFGSSYYKTeiikplgLEKLLDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180 190
....*....|....*....|....*....|....*...
gi 447166279 532 ELQIQEGLNNLM--RDRTSFVIAHRLKTIEK-ADQILV 566
Cdd:COG1245 491 RLAVAKAIRRFAenRGKTAMVVDHDIYLIDYiSDRLMV 528
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
378-529 |
7.24e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 7.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 378 EVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIkeydmnslrSKIGVVLQDTYLFAG--------- 448
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI---------RRQRDEYHQDLLYLGhqpgiktel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 449 TIMDNIR-YGRL--DASDEEVINAAKAASAHSFiKHLPnqyetkiaseGSNLSQGQKQLLAIARAILADADILILDEATS 525
Cdd:PRK13538 90 TALENLRfYQRLhgPGDDEALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
....
gi 447166279 526 NIDT 529
Cdd:PRK13538 159 AIDK 162
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
385-528 |
1.52e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 385 PGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMN---SLRSKIGVVLQDTylfagTIMDNIRYgrlda 461
Cdd:PRK13543 36 AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSrfmAYLGHLPGLKADL-----STLENLHF----- 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447166279 462 sdeevINAAKAASAhsfiKHLPNQYETKIASEG------SNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:PRK13543 106 -----LCGLHGRRA----KQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
371-542 |
1.59e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 371 ENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYD---IQQGQIHIDGKNIKEydmnSLRSKIGVVLQ-DTYLF 446
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDS----SFQRSIGYVQQqDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 447 AGTIMDNIRYGRLDASDEEVINAAKAASAHSFIKHLP-NQY-ETKIASEGSNLSQGQKQLLAIARAILADADILI-LDEA 523
Cdd:TIGR00956 850 TSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170
....*....|....*....
gi 447166279 524 TSNIDTRTELQIQEGLNNL 542
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKL 948
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
376-585 |
1.81e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKE-VSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIkeyDMNSLRSKI--GVVL------QDTYLF 446
Cdd:PRK11288 268 LREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI---DIRSPRDAIraGIMLcpedrkAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 447 AGTIMDNI---------RYGRLdasdeevINAAK-AASAHSFIKHL----PNQyETKIAsegsNLSQGQKQLLAIARAIL 512
Cdd:PRK11288 345 VHSVADNInisarrhhlRAGCL-------INNRWeAENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447166279 513 ADADILILDEATSNIDTRTELQIQEGLNNLM-RDRTSFVIAHRL-KTIEKADQILVIKDGSILEKGNHESLMEDR 585
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELAaQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQATERQ 487
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
372-570 |
2.92e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.11 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLL---TRFYDIQQGQIHIDGKNIKEYDMNSLRSKIGVVLQDTYLFAG 448
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 449 TImdnirygrldasdEEVINAAKAASAHSFIKhlpnqyetkiasegsNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:cd03233 99 TV-------------RETLDFALRCKGNEFVR---------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447166279 529 TRTELQIQEGLNNLMR--DRTSFVIAHR--LKTIEKADQILVIKDG 570
Cdd:cd03233 151 SSTALEILKCIRTMADvlKTTTFVSLYQasDEIYDLFDKVLVLYEG 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
383-566 |
3.49e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 383 ARPGETIALVGPTGSGKTTIINLLTrfydiqqGQIHIDGKNIKeydmnslrSKIGVVLQDTYL---FAGTIMDNIRygrl 459
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLA-------GVLKPDEGEVD--------PELKISYKPQYIkpdYDGTVEDLLR---- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 460 dasdeevinAAKAASAHSFIKH-------LPNQYETKIasegSNLSQGQKQLLAIARAILADADILILDEATSNIDTRTE 532
Cdd:PRK13409 423 ---------SITDDLGSSYYKSeiikplqLERLLDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
170 180 190
....*....|....*....|....*....|....*..
gi 447166279 533 LQIQEGLNNLM--RDRTSFVIAHRLKTIEK-ADQILV 566
Cdd:PRK13409 490 LAVAKAIRRIAeeREATALVVDHDIYMIDYiSDRLMV 526
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
384-567 |
3.87e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 384 RPGETIALVGPTGSGKTTIINLLTrfydiqqGQI------------------HIDGKNIKEYdMNSLRS-KIGVVLQDTY 444
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILS-------GELipnlgdyeeepswdevlkRFRGTELQNY-FKKLYNgEIKVVHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 445 L------FAGTIMDNIR----YGRLDasdeEVINAAKaasahsfIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILAD 514
Cdd:PRK13409 169 VdlipkvFKGKVRELLKkvdeRGKLD----EVVERLG-------LENILDR-------DISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447166279 515 ADILILDEATSNIDTRTELQIQEGLNNLMRDRTSFVIAHRLKTIEK-ADQILVI 567
Cdd:PRK13409 231 ADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
384-567 |
8.21e-07 |
|
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: 52.09 E-value: 8.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 384 RPGETIALVGPTGSGKTTIINLLTrfydiqqGQI------------------HIDGKNIKEYdMNSLRSK-IGVVLQDTY 444
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------GELkpnlgdydeepswdevlkRFRGTELQDY-FKKLANGeIKVAHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 445 ------LFAGTIMDnirygRLDASDE-----EVINAAKaasahsfIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILA 513
Cdd:COG1245 169 vdlipkVFKGTVRE-----LLEKVDErgkldELAEKLG-------LENILDR-------DISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 514 DADILILDEATSNIDTRTELQIQEGLNNLMR-DRTSFVIAHRLKTIEK-ADQILVI 567
Cdd:COG1245 230 DADFYFFDEPSSYLDIYQRLNVARLIRELAEeGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
141-570 |
1.43e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 51.29 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 141 MSRVTNDIDNLNQALTQSVVQI-ISSALTFIGVAIAMfaLDWILAIVTLIT------VPIMF---FVTKKLVAYSGKNFA 210
Cdd:TIGR00954 187 VSNLDSRIQNPDQLLTQDVEKFcDSVVELYSNLTKPI--LDVILYSFKLLTalgsvgPAGLFaylFATGVVLTKLRPPIG 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 211 K----RQKDLGELNGFIEEAITGADVTTLYG---KEKKTVQN-FNKINEQLRvsatKADTFSAfifpSMNFINNL----- 277
Cdd:TIGR00954 265 KltveEQALEGEYRYVHSRLIMNSEEIAFYQgnkVEKETVMSsFYRLVEHLN----LIIKFRF----SYGFLDNIvakyt 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 278 --GMGLVIGTGSVMVLNGMTTVG-----VIAAFINYSR---QFSRPLSQFATLMNTIQAAVAGGERVFEIMDEVPEIK-- 345
Cdd:TIGR00954 337 wsAVGLVAVSIPIFDKTHPAFLEmseeeLMQEFYNNGRlllKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKsg 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 346 NKKDAFVVQNLQGH---------------------VALENVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIIN 404
Cdd:TIGR00954 417 NFKRPRVEEIESGReggrnsnlvpgrgiveyqdngIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFR 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 405 LLTRFYDIQQGQIHIDGKNikeydmnslrsKIGVVLQDTYLFAGTIMDNIRYGrlDASDEEVinaAKAASAHSFIKHLPN 484
Cdd:TIGR00954 497 ILGELWPVYGGRLTKPAKG-----------KLFYVPQRPYMTLGTLRDQIIYP--DSSEDMK---RRGLSDKDLEQILDN 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 485 QYETKIASEGSN----------LSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLmrDRTSFVIAHR 554
Cdd:TIGR00954 561 VQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHR 638
|
490
....*....|....*.
gi 447166279 555 lKTIEKADQILVIKDG 570
Cdd:TIGR00954 639 -KSLWKYHEYLLYMDG 653
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
376-583 |
2.12e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.09 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTrfyDI---QQGQIHIDGKNIKEyDMNSLRSKIGVV------------L 440
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT---GIlvpTSGEVRVLGYVPFK-RRKEFARRIGVVfgqrsqlwwdlpA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 441 QDTYLFAGTImdnirYgRLDASD-EEVINaakaasahSFIKHLpnQYETKIASEGSNLSQGQKQLLAIARAILADADILI 519
Cdd:COG4586 114 IDSFRLLKAI-----Y-RIPDAEyKKRLD--------ELVELL--DLGELLDTPVRQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 520 LDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESLME 583
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
335-574 |
2.58e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 335 FEIMDEVPEIKNKKDAFVVQNLQGHvalenvsfgyeENKTIlKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQ 414
Cdd:PRK09700 250 FNAMKENVSNLAHETVFEVRNVTSR-----------DRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 415 GQIHIDGKNIK---EYDmnSLRSKIGVVLQ---DTYLFAG-TIMDNIR-------------YGRLDASDEEVInaAKAAS 474
Cdd:PRK09700 318 GEIRLNGKDISprsPLD--AVKKGMAYITEsrrDNGFFPNfSIAQNMAisrslkdggykgaMGLFHEVDEQRT--AENQR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 475 AHSFIK-HLPNQYETKiasegsnLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRD-RTSFVIA 552
Cdd:PRK09700 394 ELLALKcHSVNQNITE-------LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVS 466
|
250 260
....*....|....*....|...
gi 447166279 553 HRLKTI-EKADQILVIKDGSILE 574
Cdd:PRK09700 467 SELPEIiTVCDRIAVFCEGRLTQ 489
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
358-528 |
3.27e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 358 GHVALE----NVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTI-INLLTRFY--DIQqGQIHIDGKNIkeyDMN 430
Cdd:NF040905 254 GEVVFEvknwTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYgrNIS-GTVFKDGKEV---DVS 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 431 SLRSKI--------------GVVLQDTylfagtIMDNIRYGRLDA-SDEEVINAAK-AASAHSFIKHL----PNQYEtki 490
Cdd:NF040905 330 TVSDAIdaglayvtedrkgyGLNLIDD------IKRNITLANLGKvSRRGVIDENEeIKVAEEYRKKMniktPSVFQ--- 400
|
170 180 190
....*....|....*....|....*....|....*...
gi 447166279 491 asEGSNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:NF040905 401 --KVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
384-555 |
3.93e-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: 48.52 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 384 RPGETIALVGPTGSGKTTIINLLT--------RFYDIQQGQIHID---GKNIKEYDMNSLRSKIGVVLQDTYL------F 446
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIVKPQYVdlipkaV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 447 AGTIMDNirygrLDASDE-----EVINAAKaasahsfIKHLPNQyetkiasEGSNLSQGQKQLLAIARAILADADILILD 521
Cdd:cd03236 104 KGKVGEL-----LKKKDErgkldELVDQLE-------LRHVLDR-------NIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190
....*....|....*....|....*....|....*
gi 447166279 522 EATSNIDTRTELQIQEGLNNLMRD-RTSFVIAHRL 555
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAEDdNYVLVVEHDL 199
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
47-327 |
4.89e-06 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 48.78 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 47 IFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTArMCLLLIAIYGVTVFL-----------TWLQTFVMVNVALKTIQK 115
Cdd:cd18581 2 LLLLAAGRVVNVLVPILYKKIVDSLTPDSADSPLA-FPWALILLYVFLKFLqgggsgsvgllSNLRSFLWIPVQQFTTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 116 IRQDIFEKIQTLSLRFFDVRSQGDL---MSRVTNDIDNLNQALTQSVV-QIISsaltfIGVAIAMF--ALDWILAIVTLI 189
Cdd:cd18581 81 ISVKLFAHLHSLSLRWHLSRKTGEVlrvMDRGTSSINSLLSYVLFNIGpTIAD-----IIIAIIYFaiAFNPWFGLIVFV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 190 TVPIMFFVTKKLVAYSGK--------NFAKRQKDLGELNGFieeaitgaDVTTLYGKEKKTVQNFNKINEQLRVSATKAD 261
Cdd:cd18581 156 TMALYLILTIIITEWRTKfrremnklDNEKRAKAVDSLLNF--------ETVKYYNAERFEVERYRRAIDDYQVAEWKSN 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 262 TFSAFIFPSMNFInnLGMGLVIGT--GSVMVLNGMTTVGVIAAFINYSRQFSRPLSQFATLMNTIQAA 327
Cdd:cd18581 228 ASLNLLNTAQNLI--ITIGLLAGSllCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQS 293
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
364-535 |
5.77e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.25 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 364 NVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEyDMNSLRSKIGVVLQDT 443
Cdd:PRK13540 6 ELDFDYHD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 444 ----YLfagTIMDNIRYG-RLDASDEEVINAAKAASAHSFIkhlpnQYETKIasegsnLSQGQKQLLAIARAILADADIL 518
Cdd:PRK13540 84 ginpYL---TLRENCLYDiHFSPGAVGITELCRLFSLEHLI-----DYPCGL------LSSGQKRQVALLRLWMSKAKLW 149
|
170
....*....|....*..
gi 447166279 519 ILDEATSNIDTRTELQI 535
Cdd:PRK13540 150 LLDEPLVALDELSLLTI 166
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
340-524 |
8.65e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 340 EVPEIKNKKDAfvvqnLQGHVALE--NVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQI 417
Cdd:COG3845 241 EVLLRVEKAPA-----EPGEVVLEveNLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 418 HIDGKNIKEYDMNSLR-SKIGVVLQDTY---LFAG-TIMDNI---RYGRLDASDEEVINAAKaasAHSFIKHLPNQYETK 489
Cdd:COG3845 316 RLDGEDITGLSPRERRrLGVAYIPEDRLgrgLVPDmSVAENLilgRYRRPPFSRGGFLDRKA---IRAFAEELIEEFDVR 392
|
170 180 190
....*....|....*....|....*....|....*...
gi 447166279 490 IASEG---SNLSQGQKQLLAIARAILADADILILDEAT 524
Cdd:COG3845 393 TPGPDtpaRSLSGGNQQKVILARELSRDPKLLIAAQPT 430
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
40-302 |
9.75e-06 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 47.60 E-value: 9.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 40 KAALTFIIFLVFVTTLLGLLGPYLMGVIIDQYIVPKDLSGTARMCLLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQD 119
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 120 IFEKIQTLSLrffDVRSQGDLMSRVtNDIDNLNQALTQSVVQIISSALTFIGVAIAMFALDWILAIVTLITVPIMF---- 195
Cdd:cd18586 81 VFRAVLELPL---ESRPSGYWQQLL-RDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVglaw 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 196 ---FVTKKLVAYSGKNFAKRqkdlgelNGFIEEAITGADVTTLYGK--------EKKTVQNfnkINEQLRVSaTKADTFS 264
Cdd:cd18586 157 lnhRATRKPLGEANEAQAAR-------DALAAETLRNAETIKALGMlgnlrrrwEARHAET---LELQIRAS-DLAGAIS 225
|
250 260 270
....*....|....*....|....*....|....*...
gi 447166279 265 AFIFPSMNFINNlgmgLVIGTGSVMVLNGMTTVGVIAA 302
Cdd:cd18586 226 AIGKTLRMALQS----LILGVGAYLVIDGELTIGALIA 259
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
357-522 |
1.62e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 357 QGHVALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRfyDIQQG---QIHIDGK---------NI 424
Cdd:PRK10938 258 EPRIVLNNGVVSYND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysnDLTLFGRrrgsgetiwDI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 425 KeydmnslrSKIGVV---LQDTYLFAGTIMDNIRYGRLDAsdeevINAAKAASAHSfiKHLPNQYETKIASEGS------ 495
Cdd:PRK10938 335 K--------KHIGYVsssLHLDYRVSTSVRNVILSGFFDS-----IGIYQAVSDRQ--QKLAQQWLDILGIDKRtadapf 399
|
170 180
....*....|....*....|....*...
gi 447166279 496 -NLSQGQKQLLAIARAILADADILILDE 522
Cdd:PRK10938 400 hSLSWGQQRLALIVRALVKHPTLLILDE 427
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
88-196 |
2.91e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 46.31 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 88 IAIYG----VTVFLTWLQTFVMVNVALKTIQKIRQDIFEKIqtlsLR----FFDVRSQGDLMSRVTNDIDNLNQALTQSV 159
Cdd:cd18606 38 IGIYAglgvLQAIFLFLFGLLLAYLGIRASKRLHNKALKRV----LRapmsFFDTTPLGRILNRFSKDTDVLDNELPDSL 113
|
90 100 110
....*....|....*....|....*....|....*...
gi 447166279 160 VQIISSALTFIGVAIAMFA-LDWILAIVtlitVPIMFF 196
Cdd:cd18606 114 RMFLYTLSSIIGTFILIIIyLPWFAIAL----PPLLVL 147
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
166-327 |
4.53e-05 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 45.51 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 166 ALTFIGVaIAMFAldWILAIVTLITVPIM----FFVTKKLVAYSGKNF-AKRQKdlgelNGFIEEAITGADVTTLYGKEK 240
Cdd:cd18587 128 VLLFLAV-IALIG--GPLALVPLVAIPLVllygLLLQKPLRRLVEESMrESAQK-----NALLVESLSGLETIKALGAEG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 241 KTVQNFNKINEQLRVSATKADTFSAFIFPSMNFINNLGMGLVIGTGSVMVLNG-MTTVGVIAAFINYSRQFSrPLSQFAT 319
Cdd:cd18587 200 RMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGeLTMGGLIACVILSGRALA-PLGQIAG 278
|
....*...
gi 447166279 320 LMNTIQAA 327
Cdd:cd18587 279 LLTRYQQA 286
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
360-425 |
5.04e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 5.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 360 VALENVSFGYEEnKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIdGKNIK 425
Cdd:PRK10636 313 LKMEKVSAGYGD-RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK 376
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
364-528 |
5.77e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 364 NVSFGYEENKTILKEVSLKARPGETIALVGPTGSGKTTIINlltrfydIQQGqihIDgkniKEYDMNSLRS---KIGVVL 440
Cdd:PRK11819 11 RVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------IMAG---VD----KEFEGEARPApgiKVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 441 QDTYLFAG-TIMDNIRYG---RLDASDE-EVINAAKAASAHSFIKHLPNQ--YETKIASEG------------------- 494
Cdd:PRK11819 77 QEPQLDPEkTVRENVEEGvaeVKAALDRfNEIYAAYAEPDADFDALAAEQgeLQEIIDAADawdldsqleiamdalrcpp 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 447166279 495 -----SNLSQGQKQLLAIARAILADADILILDEATSNID 528
Cdd:PRK11819 157 wdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
496-570 |
6.43e-05 |
|
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: 44.14 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 496 NLSQGQKQL------LAIARAILADADILILDEATSNIDtrtELQIQEGLNNLMRDRTSF------VIAHRLKTIEKADQ 563
Cdd:cd03240 115 RCSGGEKVLasliirLALAETFGSNCGILALDEPTTNLD---EENIEESLAEIIEERKSQknfqliVITHDEELVDAADH 191
|
....*...
gi 447166279 564 IL-VIKDG 570
Cdd:cd03240 192 IYrVEKDG 199
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
372-570 |
8.76e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 372 NKTILKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMN-SLRSKIGVVLQD---TYLFA 447
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeAINHGFALVTEErrsTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 448 ------GTIMDNIR-----YGRLD----ASDEE-VINAAKAASAhsfikhlpnQYETKIASegsnLSQGQKQLLAIARAI 511
Cdd:PRK10982 340 yldigfNSLISNIRnyknkVGLLDnsrmKSDTQwVIDSMRVKTP---------GHRTQIGS----LSGGNQQKVIIGRWL 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447166279 512 LADADILILDEATSNIDTRTELQIQEGLNNLM-RDRTSFVIAHRL-KTIEKADQILVIKDG 570
Cdd:PRK10982 407 LTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMpELLGITDRILVMSNG 467
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
376-582 |
1.80e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 376 LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYD-MNSLRSKI----------GVVL---- 440
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIvyisedrkrdGLVLgmsv 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 441 -QDTYLFAGTIMDNiRYGRLDASDEEvinaakaASAHSFIK----HLPNQyETKIAsegsNLSQGQKQLLAIARAILADA 515
Cdd:PRK10762 348 kENMSLTALRYFSR-AGGSLKHADEQ-------QAVSDFIRlfniKTPSM-EQAIG----LLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447166279 516 DILILDEATSNIDTRTELQIQEGLNNLMRDRTS--FVIAHRLKTIEKADQILVIKDGSI-----LEKGNHESLM 582
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSiiLVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
88-254 |
2.01e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 43.62 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 88 IAIYG----VTVFLTWLQTFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQII 163
Cdd:cd18603 44 LGVYGalglGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 164 SSALTFIGVAIA-MFALDWILAIVTLITVpIMFFVTKKLVAYSgknfakRQkdLGELNG--------FIEEAITGADVTT 234
Cdd:cd18603 124 NCLFQVISTLVViSISTPIFLVVIIPLAI-LYFFIQRFYVATS------RQ--LKRLESvsrspiysHFSETLQGASTIR 194
|
170 180
....*....|....*....|.
gi 447166279 235 LYGKEKKTV-QNFNKINEQLR 254
Cdd:cd18603 195 AYGVQERFIrESDRRVDENQR 215
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
496-570 |
5.18e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.40 E-value: 5.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 496 NLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMR--DRTSFVIAHRLKTIEKADQILVIKDG 570
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
377-572 |
5.63e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.73 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 377 KEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNIKEYDMNSlRSKIGVVL-----QDTYLF----- 446
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVYlpedrQSSGLYldapl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 447 ---AGTIMDN-----IRYGRLDASDEEVINAAKAASAHsfikhlPNQyetkiasEGSNLSQGQKQLLAIARAILADADIL 518
Cdd:PRK15439 359 awnVCALTHNrrgfwIKPARENAVLERYRRALNIKFNH------AEQ-------AARTLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 519 ILDEATSNIDTRTELQIQEGLNNLMRDRTSFV-IAHRLKTIEK-ADQILVIKDGSI 572
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEI 481
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
336-401 |
5.83e-04 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 41.94 E-value: 5.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 336 EIMDEVPEIKNKKDAfvVQNLQGHVAlENVSFGYEENkTILKEvslkarpGETIALVGPTGSGKTT 401
Cdd:TIGR03499 155 ELLEKLPEDADAEDA--WRWLREALE-GMLPVKPEED-PILEQ-------GGVIALVGPTGVGKTT 209
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
389-572 |
7.31e-04 |
|
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.
Pssm-ID: 459814 [Multi-domain] Cd Length: 193 Bit Score: 40.99 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 389 IALVGPTGSGKTTIINLLTRFYdIQQGQihidgknikeydmnslrsKIGVVLQDTYlfagtimdnirygRLDASDEEVIN 468
Cdd:pfam00448 3 ILLVGLQGSGKTTTIAKLAAYL-KKKGK------------------KVLLVAADTF-------------RAAAIEQLKQL 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 469 AAKAASAhsFIKHLPNQYETKIASEgsnlsqgqkqllAIARAILADADILIldeatsnIDTRTELQIQEGLNNLMRDrts 548
Cdd:pfam00448 51 AEKLGVP--VFGSKTGADPAAVAFD------------AVEKAKAENYDVVL-------VDTAGRLQNDKNLMDELKK--- 106
|
170 180
....*....|....*....|....
gi 447166279 549 fviahrLKTIEKADQILVIKDGSI 572
Cdd:pfam00448 107 ------IKRVVAPDEVLLVLDATT 124
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
497-582 |
1.60e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.94 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 497 LSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNLMRDR--TSFVIAHRLKTIEK-ADQILVIKDGSIL 573
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLYCGQTV 238
|
....*....
gi 447166279 574 EKGNHESLM 582
Cdd:PRK15093 239 ETAPSKELV 247
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
88-200 |
1.85e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 40.77 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 88 IAIYGVTVFLTWL----QTFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTQSVVQII 163
Cdd:cd18601 62 LGIYAGLTAATFVfgflRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFL 141
|
90 100 110
....*....|....*....|....*....|....*...
gi 447166279 164 SSALTFIGVAIAMFALD-WILaiVTLITVPIMFFVTKK 200
Cdd:cd18601 142 QLLLQVVGVVLLAVVVNpWVL--IPVIPLVILFLFLRR 177
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
43-199 |
3.03e-03 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 39.93 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 43 LTFIIFLVFVTTLLGLLGPYLMGVIIDQyiVPKDLSGTARMCLLLIAIYGVTVFLT--------WLQTFVMVNVALKTIQ 114
Cdd:cd18556 4 FFSILFISLLSSILISISPVILAKITDL--LTSSSSDSYNYIVVLAALYVITISATkllgflslYLQSSLRVELIISISS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 115 KIRQDIFEKIQTlslrFFDVRSQGDLMSRV---TNDI----DNLNQALTQSVVQIISSaltfigVAIAMFALDWILAIVT 187
Cdd:cd18556 82 SYFRYLYEQPKT----FFVKENSGDITQRLnqaSNDLytlvRNLSTNILPPLLQLIIA------IVVILSSGDYFVAALF 151
|
170
....*....|..
gi 447166279 188 LITVpIMFFVTK 199
Cdd:cd18556 152 LLYA-VLFVINN 162
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
336-403 |
3.13e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 40.26 E-value: 3.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447166279 336 EIMDEVPEIKNKKDAFVVQNLQGHVAlenvsfgyeenKTILKEVSLKARPGETIALVGPTGSGKTTII 403
Cdd:PRK05703 182 KLLKLLLEHMPPRERTAWRYLLELLA-----------NMIPVRVEDILKQGGVVALVGPTGVGKTTTL 238
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
495-553 |
3.27e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 3.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 447166279 495 SNLSQGQKQLLAIARAILADADILILDEATSNIDTRTELQIQEGLNNlmRDRTSFVIAH 553
Cdd:PRK15064 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISH 210
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
360-424 |
6.13e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.72 E-value: 6.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447166279 360 VALENVSFGYeeNKTI-LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGKNI 424
Cdd:NF033858 2 ARLEGVSHRY--GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM 65
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
388-425 |
6.78e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.83 E-value: 6.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 447166279 388 TIALVGPTGSGKTTIINLLTRFY-----------DIQQGQIHIDGKNIK 425
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKaivsdypgttrDPNEGRLELKGKQII 49
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
371-584 |
7.66e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 7.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 371 ENKTI--LKEVSLKARPGETIALVGPTGSGKTTIINLLTRFYDIQQGQIHIDGknikeyDMNSLRSKIGVVLQDTYlfag 448
Cdd:PRK13546 33 KNKTFfaLDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQLTG---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 449 tiMDNIRYGRL---------DASDEEVINAAKAAsahSFIKHLPNQYetkiasegsnlSQGQKQLLAIARAILADADILI 519
Cdd:PRK13546 103 --IENIEFKMLcmgfkrkeiKAMTPKIIEFSELG---EFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447166279 520 LDEATSNID-TRTELQIQEGLNNLMRDRTSFVIAHRLKTIEK-ADQILVIKDGSILEKGNHESLMED 584
Cdd:PRK13546 167 IDEALSVGDqTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
85-284 |
8.98e-03 |
|
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group represents the transmembrane (TM) domain of an active lipid-linked oligosaccharides flippase PglK (protein glycosylation K), which is a homodimeric ABC transporter that flips a lipid-linked oligosaccharide that serves as a glycan donor in N-linked protein glycosylation. Pglk mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. This TM subunit exhibits 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. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 349997 Cd Length: 300 Bit Score: 38.30 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 85 LLLIAIYGVTVFLTWLQTFVMVNVALKTIQKIRQDIFEKIQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALtQSVVQIIS 164
Cdd:cd18553 58 IILIGFYIFRSLYNIFYTYLLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNLSQVI-QSFLFILS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 165 SALTFIGVAIAMFALDWILAIVTLITVPIMFFVTKKLVAYSGKNFA-KRQKDLGELNGFIEEAITGADVTTLYGKEKKTV 243
Cdd:cd18553 137 EIFVILFIYSLLLYVNWKITLVLTLFLGLNVFFITKIVSKKIKKQGkKREESQKKFYKILSETFGNFKIIKLKSNEKEIL 216
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 447166279 244 QNFNKINEQLRVSATKADTFSAfiFPSmNFINNLGMGLVIG 284
Cdd:cd18553 217 KNFSQASLKFAKANIINQTLQT--VPR-LILETIGFSLLIL 254
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
48-215 |
9.01e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 38.30 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 48 FLVFVTTLLGLLGPYLMGVIIDQYivpKDLSGTARM-CLLLIAIYGVTVFLTWLQT---FVMVNVALKTIQKIRQDIFEK 123
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFL---EDSSEPLSDgYLYALGLVLSSLLGALLSShynFQMNKVSLKVRAALVTAVYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 124 IQTLSLRFFDVRSQGDLMSRVTNDIDNLNQALTqSVVQIISSALTfigVAIAMFAL-----DWILA--IVTLITVPIMFF 196
Cdd:cd18598 81 ALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCP-SFHDLWSLPLQ---IIVALYLLyqqvgVAFLAglVFALVLIPINKW 156
|
170
....*....|....*....
gi 447166279 197 VTKKLVAYSGKNFAkrQKD 215
Cdd:cd18598 157 IAKRIGALSEKMMK--HKD 173
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
326-404 |
9.34e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447166279 326 AAVAGGERVFEimDEVPEIKNKKDAFVVQNLQGHVALENVSFGYEENKTI----------LKEVSLKARPGETIALVGPT 395
Cdd:TIGR00630 566 AGEHGGEVVAS--GTPEEILANPDSLTGQYLSGRKKIEVPAERRPGNGKFltlkgarennLKNITVSIPLGLFTCITGVS 643
|
....*....
gi 447166279 396 GSGKTTIIN 404
Cdd:TIGR00630 644 GSGKSTLIN 652
|
|
| |
