|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-590 |
0e+00 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 1225.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 22 VALLVIIAMLQLVPPKVVGIVVDGVTEQHFTTGQILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYYRQLS 101
Cdd:PRK10789 1 VALLIIIAMLQLIPPKVVGIIVDGVTEQHMTTGQILMWIGTMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 102 RQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTQISWQLTLFSLLPMPVMAIMIKRNGDA 181
Cdd:PRK10789 81 RQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTQISWQLTLLALLPMPVMAIMIKRYGDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 182 LHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIG 261
Cdd:PRK10789 161 LHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 262 GGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVNDGSEPVPEGRGELDVNIHQ 341
Cdd:PRK10789 241 GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDVNIRQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 421
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 FSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:PRK10789 401 FSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 502 AVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQSGWYRDMYRYQQLEAALDDAP 581
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALDDAP 560
|
....*....
gi 16128433 582 ENREEAVDA 590
Cdd:PRK10789 561 EIREEAVDA 569
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-575 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 634.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 1 MRLFAQLSWYFRREWRRYLGAVALLVIIAMLQLVPPKVVGIVVDGVTEQHfTTGQILMWIATMVLIAVVVYLLRYVWRVL 80
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG-DLSALLLLLLLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 81 LFGASYQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQL 160
Cdd:COG1132 85 LARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFV-IDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 161 TLFSLLPMPVMAIMIKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARI 240
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 241 DARFDPTIYIAIGMANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPV 320
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 321 VNDGSEPVPEGRGELDVNIHQ--FTYPqTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI 398
Cdd:COG1132 324 IPDPPGAVPLPPVRGEIEFENvsFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 399 PLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQK 478
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 479 QRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLA 558
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL 562
|
570
....*....|....*..
gi 16128433 559 QQSGWYRDMYRYQQLEA 575
Cdd:COG1132 563 ARGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-572 |
2.45e-145 |
|
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: 436.57 E-value: 2.45e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 10 YFRREWRRYLGAVALLVIIAMLQLVPPKVVGIVVDGVTEQHFTTgqILMWIATMVLIAVVV-YLLRYVWRVLLFGASYQL 88
Cdd:COG2274 150 LLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLS--TLWVLAIGLLLALLFeGLLRLLRSYLLLRLGQRI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 89 AVELREDYYRQLSRQHPEFYLRHRTGDLMARAtNDVDRVV-FAAGEGVLTLVDsLVMGCAVLIMMSTqISWQLTLFSLLP 167
Cdd:COG2274 228 DLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIReFLTGSLLTALLD-LLFVLIFLIVLFF-YSPPLALVVLLL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 168 MPVMAIMI----KRNGDALHERFKLAQAAFSSLndrtQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDAR 243
Cdd:COG2274 305 IPLYVLLGllfqPRLRRLSREESEASAKRQSLL----VETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNL 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 244 FDPTIYIAIGMANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVND 323
Cdd:COG2274 381 LSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 324 GSEPV--PEGRGELDV-NIHqFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL 400
Cdd:COG2274 461 GRSKLslPRLKGDIELeNVS-FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 401 TKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQR 480
Cdd:COG2274 540 RQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 481 ISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQ 560
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
570
....*....|..
gi 16128433 561 SGWYRDMYRYQQ 572
Cdd:COG2274 700 KGLYAELVQQQL 711
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
18-311 |
3.34e-132 |
|
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: 387.92 E-value: 3.34e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 18 YLGAVALLVIIAMLQLVPPKVVGIVVDGVTEQHFTTGQILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYY 97
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 98 RQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMsTQISWQLTLFSLLPMPVMAIMIKR 177
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMM-FTISPKLTLIALLPLPLLALLVYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 178 NGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANL 257
Cdd:cd18541 160 LGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 16128433 258 LAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18541 240 IVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1-571 |
4.04e-111 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 344.01 E-value: 4.04e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 1 MRLFAqlswYFRREWRRYLGAVALLVIIAMLQLVPPKVVGIVVDGVTEQhfTTGQILMWIATM-VLIAVVVYLLRYVWRV 79
Cdd:TIGR02203 3 RRLWS----YVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGG--RDRSVLWWVPLVvIGLAVLRGICSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 80 LLFGASYQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMsTQISWQ 159
Cdd:TIGR02203 77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVL-LYYSWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 160 LTLFSLLPMPVMAIMIKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVAR 239
Cdd:TIGR02203 156 LTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 240 IDARFDPTI--YIAIGMANLLAIGGgsWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAE 317
Cdd:TIGR02203 236 AGSISSPITqlIASLALAVVLFIAL--FQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 318 APVVNDGSEPVPEGRGELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD 397
Cdd:TIGR02203 314 PPEKDTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 398 IPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCP-NATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGG 476
Cdd:TIGR02203 394 HDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 477 QKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDV 556
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNE 553
|
570
....*....|....*
gi 16128433 557 LAQQSGWYRDMYRYQ 571
Cdd:TIGR02203 554 LLARNGLYAQLHNMQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-562 |
2.68e-107 |
|
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: 333.65 E-value: 2.68e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 2 RLFAQLswyfRREWRRYLGAVALLVIIAMLQLVPPKVVGIVVDGVTEQHFTTGQILMWIATMVLIAVVVYLLRYVWRVLL 81
Cdd:COG4988 7 RLKRLA----RGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 82 FGASYQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVvfaagEGVLT-----LVDSLVMGCAVLIMMSTqI 156
Cdd:COG4988 83 FRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEAL-----DGYFArylpqLFLAALVPLLILVAVFP-L 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 157 SWQLTLFSLLPMPV----MAIMIKRNGDALHERFklaqAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGK 232
Cdd:COG4988 157 DWLSGLILLVTAPLiplfMILVGKGAAKASRRQW----RALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 233 KNMRVARI--------DarfdptIYIAIGMAnLLAIGGGsWMVVQGSLTLGQ-----LTSFMMYLglmiwPMLALAWMFN 299
Cdd:COG4988 233 RTMKVLRVaflssavlE------FFASLSIA-LVAVYIG-FRLLGGSLTLFAalfvlLLAPEFFL-----PLRDLGSFYH 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 300 IVERGSAAYSRIRAML-AEAPVVNDGSEPVPEGRGeLDVNIHQ--FTYPQtDHPALENVNFALKPGQMLGICGPTGSGKS 376
Cdd:COG4988 300 ARANGIAAAEKIFALLdAPEPAAPAGTAPLPAAGP-PSIELEDvsFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 377 TLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDIL 456
Cdd:COG4988 378 TLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 457 RLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTE 536
Cdd:COG4988 458 ALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ 537
|
570 580
....*....|....*....|....*.
gi 16128433 537 ASEIIVMQHGHIAQRGNHDVLAQQSG 562
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
9-571 |
3.27e-103 |
|
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: 323.58 E-value: 3.27e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 9 WYFRREWR-RYLGAVALLVIIAMLQLVPPKVVGIVVD-GVTEQ--HFTTGQILMWIATMVLIAVVVYLLRYVwrVLLFGA 84
Cdd:TIGR02204 10 WPFVRPYRgRVLAALVALLITAAATLSLPYAVRLMIDhGFSKDssGLLNRYFAFLLVVALVLALGTAARFYL--VTWLGE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 85 syQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFS 164
Cdd:TIGR02204 88 --RVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFI-TSPKLTSLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 165 LLPMPVMAIMIKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTgkknMRVA--RIDA 242
Cdd:TIGR02204 165 LLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKA----YEAArqRIRT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 243 RFDPT---IYIAIGmanllAIGGGSWM----VVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAML 315
Cdd:TIGR02204 241 RALLTaivIVLVFG-----AIVGVLWVgahdVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 316 AEAPVVNDGSEPVP---EGRGELDVNIHQFTYP-QTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG 391
Cdd:TIGR02204 316 QAEPDIKAPAHPKTlpvPLRGEIEFEQVNFAYPaRPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 392 DIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGV 471
Cdd:TIGR02204 396 RILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 472 MLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQR 551
Cdd:TIGR02204 476 TLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQ 555
|
570 580
....*....|....*....|
gi 16128433 552 GNHDVLAQQSGWYRDMYRYQ 571
Cdd:TIGR02204 556 GTHAELIAKGGLYARLARLQ 575
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
72-569 |
1.72e-101 |
|
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: 318.63 E-value: 1.72e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 72 LLRYVWRVLLFGASYQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVD-------RVVFAAGEGVLTlvdSLVM 144
Cdd:COG4987 70 VFRYLERLVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDaldnlylRVLLPLLVALLV---ILAA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 145 gCAVLIMMSTQISWQLTLFSLLPMPVMAIMIKRNGDALHERFKLAQAAfssLNDRTQESLTSIRMIKAFGLEDRQSALFA 224
Cdd:COG4987 147 -VAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAA---LRARLTDLLQGAAELAAYGALDRALARLD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 225 ADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIGGGSWMVVQGSLTLGQLTSF-MMYLGLM-IWPMLALAWMFniVE 302
Cdd:COG4987 223 AAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLvLAALALFeALAPLPAAAQH--LG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 303 RGSAAYSRIRAMLAEAPVVNDGSEPVP-EGRGELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSL 381
Cdd:COG4987 301 RVRAAARRLNELLDAPPAVTEPAEPAPaPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 382 IQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQG 461
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 462 YDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEII 541
Cdd:COG4987 461 LDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL 540
|
490 500
....*....|....*....|....*...
gi 16128433 542 VMQHGHIAQRGNHDVLAQQSGWYRDMYR 569
Cdd:COG4987 541 VLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-582 |
3.82e-96 |
|
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: 305.98 E-value: 3.82e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 2 RLFAQLSWYFRREWRRYLGAVALLVIIAMLQLVPPKVVGIVVDGVTeQHFTTGQILMWIATMVLIAvvvY-LLRYV---- 76
Cdd:COG5265 19 LLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAID-ALLSGAAALLVVPVGLLLA---YgLLRLLsvlf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 77 --WRVLLFG-----ASYQLAVELredyYRQLSRQHPEFYLRHRTGDLmaraTNDVDRVVfaagEGVLTLVDSLVMG---- 145
Cdd:COG5265 95 geLRDALFArvtqrAVRRLALEV----FRHLHALSLRFHLERQTGGL----SRDIERGT----KGIEFLLRFLLFNilpt 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 146 ----CAVLIMMSTQISWQLTLfsllpmpVMAIMIkrngdalherfkLAQAAFS------------SLNDrtQESLTSIRM 209
Cdd:COG5265 163 lleiALVAGILLVKYDWWFAL-------ITLVTV------------VLYIAFTvvvtewrtkfrrEMNE--ADSEANTRA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 210 I---------KAFGLEDRQSALFAADAEDTgkknmRVARIDAR-------FDPTIYIAIGMANLLAIGGgsWMVVQGSLT 273
Cdd:COG5265 222 VdsllnyetvKYFGNEAREARRYDEALARY-----ERAAVKSQtslallnFGQALIIALGLTAMMLMAA--QGVVAGTMT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 274 LGQLT---SFMMylGLMIwPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVND--GSEPVPEGRGEL---DVNihqFTYp 345
Cdd:COG5265 295 VGDFVlvnAYLI--QLYI-PLNFLGFVYREIRQALADMERMFDLLDQPPEVADapDAPPLVVGGGEVrfeNVS---FGY- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 346 QTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDT 425
Cdd:COG5265 368 DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 426 VANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDG 505
Cdd:COG5265 448 IAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 506 RTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQSGWYRDMYRYQQLEAALDDAPE 582
Cdd:COG5265 528 RTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEALA 604
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
342-568 |
5.55e-92 |
|
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: 282.58 E-value: 5.55e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 421
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 FSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:cd03251 88 FNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 502 AVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQSGWYRDMY 568
Cdd:cd03251 168 ALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
338-571 |
4.68e-91 |
|
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: 280.27 E-value: 4.68e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 338 NIHqFTYpQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ 417
Cdd:cd03253 5 NVT-FAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 418 TPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILD 497
Cdd:cd03253 83 DTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128433 498 DALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQSGWYRDMYRYQ 571
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
10-567 |
1.04e-90 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 294.71 E-value: 1.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 10 YFRREWRRYLGAVALLVIIAMLQLVPPKVVGIVVDGV-TEQHFTTGQILMWIATMVLIAVVVYllryvwrVLLFGASYQL 88
Cdd:TIGR00958 155 LSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLgGDKGPPALASAIFFMCLLSIASSVS-------AGLRGGSFNY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 89 AVE-----LREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMsTQISWQLTLF 163
Cdd:TIGR00958 228 TMArinlrIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFM-LWLSPRLTMV 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 164 SLLPMPVMAIMIKRNG---DALHERFklaQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARI 240
Cdd:TIGR00958 307 TLINLPLVFLAEKVFGkryQLLSEEL---QEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 241 DARFDPTIYIaIGMANLLAI-GGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAP 319
Cdd:TIGR00958 384 YAGYLWTTSV-LGMLIQVLVlYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKP 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 320 VV-NDGS-EPVP-EGRGEL-DVNihqFTYP-QTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIR 394
Cdd:TIGR00958 463 NIpLTGTlAPLNlEGLIEFqDVS---FSYPnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 395 FHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLS 474
Cdd:TIGR00958 540 LDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 475 GGQKQRISIARALLVNAEILILDDALSAVDGRTEhQILHNLRQWGqGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNH 554
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECE-QLLQESRSRA-SRTVLLIAHRLSTVERADQILVLKKGSVVEMGTH 697
|
570
....*....|...
gi 16128433 555 DVLAQQSGWYRDM 567
Cdd:TIGR00958 698 KQLMEDQGCYKHL 710
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
338-571 |
6.07e-89 |
|
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: 274.80 E-value: 6.07e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 338 NIHqFTYPQ-TDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVS 416
Cdd:cd03249 5 NVS-FRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 417 QTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILIL 496
Cdd:cd03249 84 QEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 497 DDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQSGWYRDMYRYQ 571
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-571 |
7.87e-89 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 286.14 E-value: 7.87e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 11 FRREW---RRY----LGAVALLVIIA-----MLQLVPPkvvgIVVDGVTEqhfTTGQILMWiatMVLIAVVVYLLRYVWR 78
Cdd:PRK11176 13 FRRLWptiAPFkaglIVAGVALILNAasdtfMLSLLKP----LLDDGFGK---ADRSVLKW---MPLVVIGLMILRGITS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 79 vllFGASYQLA-------VELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIM 151
Cdd:PRK11176 83 ---FISSYCISwvsgkvvMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 152 MSTQiSWQLTLFSLLPMPVMAIMIKrngdALHERF----KLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADA 227
Cdd:PRK11176 160 MFYY-SWQLSLILIVIAPIVSIAIR----VVSKRFrnisKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 228 EDTGKKNMRVARIDARFDPTIYIAIGMANLLAIGGGSWMVVQGSLTLGQLTS-FMMYLGLMiWPMLALAWMFNIVERGSA 306
Cdd:PRK11176 235 NRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVvFSSMIALM-RPLKSLTNVNAQFQRGMA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 307 AYSRIRAMLAEAPVVNDGSEPVPEGRGELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHF 386
Cdd:PRK11176 314 ACQTLFAILDLEQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 387 DVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNA-TQQEIEHVARLASVHDDILRLPQGYDTE 465
Cdd:PRK11176 394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 466 VGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQH 545
Cdd:PRK11176 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVED 553
|
570 580
....*....|....*....|....*.
gi 16128433 546 GHIAQRGNHDVLAQQSGWYRDMYRYQ 571
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
7-571 |
8.14e-85 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 278.55 E-value: 8.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 7 LSWY------FRREWRRYLGAVALLVIIAmlqLVPPKVVGIVVDGV-TEQHFTTGQILmwiaTMVLIAVVVYLLRYVW-R 78
Cdd:TIGR01846 127 FSWFipaiirYRKQFREVLLISLALQLFA---LVTPLLFQVVIDKVlVHRGLSTLSVL----ALAMLAVAIFEPALGGlR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 79 VLLFG-ASYQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSL--VMGCAVLIMMSTQ 155
Cdd:TIGR01846 200 TYLFAhLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRELEQIRNFLTGSALTVVLDLLfvVVFLAVMFFYSPT 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 156 ISW----QLTLFSLLPMPVMAIMIKRngdaLHERFKLAQAAFSSLNdrtqESLTSIRMIKAFGLE-------DRQSALFA 224
Cdd:TIGR01846 280 LTGvvigSLVCYALLSVFVGPILRKR----VEDKFERSAAATSFLV----ESVTGIETIKATATEpqfqnrwDRQLAAYV 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 225 AdaedTGKKNMRVARIDARfdptiyiAIGMAN----LLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNI 300
Cdd:TIGR01846 352 A----ASFRVTNLGNIAGQ-------AIELIQkltfAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQD 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 301 VERGSAAYSRIRAMLAEaPVVN--DGSEPVPEGRGELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTL 378
Cdd:TIGR01846 421 FQQTGIALERLGDILNS-PTEPrsAGLAALPELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTL 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 379 LSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRL 458
Cdd:TIGR01846 500 TKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISEL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 459 PQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEAS 538
Cdd:TIGR01846 580 PQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACD 659
|
570 580 590
....*....|....*....|....*....|...
gi 16128433 539 EIIVMQHGHIAQRGNHDVLAQQSGWYRDMYRYQ 571
Cdd:TIGR01846 660 RIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
333-562 |
4.14e-78 |
|
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: 246.37 E-value: 4.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 333 GELDVNIHQFTYpQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL 412
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 413 AVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAE 492
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 493 ILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQSG 562
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
19-543 |
2.03e-75 |
|
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: 249.51 E-value: 2.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAMLQLVppkvvGIVVDGVTEQHFTTGQILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYYR 98
Cdd:TIGR02857 11 LGVLGALLIIAQAWLL-----ARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 99 QLSRQHPEFYLRHRTGDLMARATNDVDRVV-FAAG---EGVLTLVDSLVMGCAVLimmstQISWQLTLFSLLPMPVMAIM 174
Cdd:TIGR02857 86 AVAALGPRWLQGRPSGELATLALEGVEALDgYFARylpQLVLAVIVPLAILAAVF-----PQDWISGLILLLTAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 175 IKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARID------ARFDPTI 248
Cdd:TIGR02857 161 MILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAflssavLELFATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 249 YIA-----IGMaNLLAiggGSWMVVQGSLTLGQLTSFmmYLglmiwPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVND 323
Cdd:TIGR02857 241 SVAlvavyIGF-RLLA---GDLDLATGLFVLLLAPEF--YL-----PLRQLGAQYHARADGVAAAEALFAVLDAAPRPLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 324 GSEPVPEGR-GELDVNIHQFTYPQTDhPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK 402
Cdd:TIGR02857 310 GKAPVTAAPaSSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 403 LQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRIS 482
Cdd:TIGR02857 389 ADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLA 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 483 IARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVM 543
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
342-547 |
5.93e-71 |
|
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: 225.73 E-value: 5.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 421
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 FSDTVANNIalgcpnatqqeiehvarlasvhddilrlpqgydtevgergvmLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:cd03228 88 FSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128433 502 AVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGH 547
Cdd:cd03228 126 ALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-587 |
8.48e-71 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 238.71 E-value: 8.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 11 FRREWR--RYLGAVALLVII--------AMLQLVPPKVVGIVVDGVTEQHFTTGQILMW-------IATMVLIAVVVYLL 73
Cdd:PRK13657 4 FRLYARvlQYLGAEKRLGILlavanvllAAATFAEPILFGRIIDAISGKGDIFPLLAAWagfglfnIIAGVLVARHADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 74 RYVWRVLLFGASYQLAVELREDYYRQlsrqhpefylRHrTGDL---MARATNDVDRVVFAAGEGVLTLVDSLVmgcaVLI 150
Cdd:PRK13657 84 AHRRRLAVLTEYFERIIQLPLAWHSQ----------RG-SGRAlhtLLRGTDALFGLWLEFMREHLATLVALV----VLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 151 MMSTQISWQLTLFsLLPMPVMAIMIKRngdALHERFKLAQAA----FSSLNDRTQESLTSIRMIKAF--------GLEDR 218
Cdd:PRK13657 149 PLALFMNWRLSLV-LVVLGIVYTLITT---LVMRKTKDGQAAveehYHDLFAHVSDAIGNVSVVQSYnrieaetqALRDI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 219 QSALFAAdaedtgkkNMRV------ARIDARFDPTIYIaigMANLLAiggGSWMVVQGSLTLGQLTSFMMYLGLMIWPML 292
Cdd:PRK13657 225 ADNLLAA--------QMPVlswwalASVLNRAASTITM---LAILVL---GAALVQKGQLRVGEVVAFVGFATLLIGRLD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 293 ALAWMFNIVERGSAAYSRIRAMLAEAPVVNDGSEPVPEGRGELDVNIHQ--FTYPQTdHPALENVNFALKPGQMLGICGP 370
Cdd:PRK13657 291 QVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDvsFSYDNS-RQGVEDVSFEAKPGQTVAIVGP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 371 TGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLAS 450
Cdd:PRK13657 370 TGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 451 VHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHR 530
Cdd:PRK13657 450 AHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHR 529
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 531 LSALTEASEIIVMQHGHIAQRGNHDVLAQQSGWYRDMYRYQQL--EAALDDAPENREEA 587
Cdd:PRK13657 530 LSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGMlqEDERRKQPAAEGAN 588
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
18-311 |
9.23e-70 |
|
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: 226.93 E-value: 9.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 18 YLGAVALLVIIAMLQLVPPKVVGIVVDGVTEQHFTTgQILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYY 97
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRE-LLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 98 RQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVMAIMIKR 177
Cdd:cd18542 80 DHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFS-INWKLTLISLAIIPFIALFSYV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 178 NGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANL 257
Cdd:cd18542 159 FFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 16128433 258 LAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18542 239 LVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
342-571 |
9.44e-70 |
|
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: 225.06 E-value: 9.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 421
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 FSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:cd03252 88 FNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 502 AVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQSGWYRDMYRYQ 571
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
63-568 |
2.29e-65 |
|
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: 226.93 E-value: 2.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 63 MVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATnDVDRVVFAAGEGVLTLVDSL 142
Cdd:TIGR01193 202 LIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 143 VMGCAVLIMMSTQISwQLTLFSLLPMPVMAIMI--------KRNGDALherfklaQAAfSSLNDRTQESLTSIRMIKAFG 214
Cdd:TIGR01193 281 WILVIVGLFLVRQNM-LLFLLSLLSIPVYAVIIilfkrtfnKLNHDAM-------QAN-AVLNSSIIEDLNGIETIKSLT 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 215 LEDRQSALFAADAEDTGKKNMRVARIDArfdptIYIAIGMA-----NLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIW 289
Cdd:TIGR01193 352 SEAERYSKIDSEFGDYLNKSFKYQKADQ-----GQQAIKAVtklilNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLT 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 290 PMLALAWMFNIVERGSAAYSRiramLAEAPVVNdgSEPVPEGR--------GELDVNIHQFTYPQTDhPALENVNFALKP 361
Cdd:TIGR01193 427 PLENIINLQPKLQAARVANNR----LNEVYLVD--SEFINKKKrtelnnlnGDIVINDVSYSYGYGS-NILSDISLTIKM 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 362 GQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGC-PNATQQ 440
Cdd:TIGR01193 500 NSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 441 EIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWgQ 520
Cdd:TIGR01193 580 EIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-Q 658
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 16128433 521 GRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQSGWYRDMY 568
Cdd:TIGR01193 659 DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
333-548 |
4.62e-64 |
|
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: 209.37 E-value: 4.62e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 333 GELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL 412
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 413 AVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAE 492
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 493 ILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHI 548
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
314-569 |
7.65e-64 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 219.70 E-value: 7.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 314 MLAEAPVVNDGSEPVPEGRGELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI 393
Cdd:PRK11160 318 TEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 394 RFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVarLASVH-DDILRLPQGYDTEVGERGVM 472
Cdd:PRK11160 398 LLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEV--LQQVGlEKLLEDDKGLNAWLGEGGRQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 473 LSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRG 552
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQG 555
|
250
....*....|....*..
gi 16128433 553 NHDVLAQQSGWYRDMYR 569
Cdd:PRK11160 556 THQELLAQQGRYYQLKQ 572
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
342-548 |
2.02e-60 |
|
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: 200.00 E-value: 2.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYP-QTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 420
Cdd:cd03248 19 FAYPtRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 421 LFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:cd03248 99 LFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128433 501 SAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHI 548
Cdd:cd03248 179 SALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
19-311 |
2.32e-60 |
|
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: 202.40 E-value: 2.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAMLQLVPPKVVGIVVDGVTEQHfTTGQILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYYR 98
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAG-DLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 99 QLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVMAIMIKRN 178
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFY-LNWKLTLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 179 GDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLL 258
Cdd:cd07346 160 RRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 259 AIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
15-580 |
1.31e-59 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 208.80 E-value: 1.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 15 WRRYLG-AVALLVIIAMLQLVPPKVVGIVVDG-VTEQHFTTGQILMWIATMVLIAVVVYLLRYvWRVLLFG-ASYQLAVE 91
Cdd:PRK10790 21 WRKPLGlAVLMLWVAAAAEVSGPLLISYFIDNmVAKGNLPLGLVAGLAAAYVGLQLLAAGLHY-AQSLLFNrAAVGVVQQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 92 LREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVM 171
Cdd:PRK10790 100 LRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFS-LDWRMALVAIMIFPAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 172 AIMIkrngdALHERF-----KLAQAAFSSLNDRTQESLTSIRMIKAFgledRQSALFAADAEDTGKKN----MRVARIDA 242
Cdd:PRK10790 179 LVVM-----VIYQRYstpivRRVRAYLADINDGFNEVINGMSVIQQF----RQQARFGERMGEASRSHymarMQTLRLDG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 243 ---RFDPTIYIAIGMANLLAIGGGSwmvVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAmLAEAP 319
Cdd:PRK10790 250 fllRPLLSLFSALILCGLLMLFGFS---ASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFE-LMDGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 320 VVNDGSEPVPEGRGELDVNIHQFTYpQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIP 399
Cdd:PRK10790 326 RQQYGNDDRPLQSGRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 400 LTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGcPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQ 479
Cdd:PRK10790 405 LSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG-RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 480 RISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQ 559
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLA 563
|
570 580
....*....|....*....|.
gi 16128433 560 QSGWYRDMYRYQQLEAALDDA 580
Cdd:PRK10790 564 AQGRYWQMYQLQLAGEELAAS 584
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-559 |
5.00e-59 |
|
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: 206.52 E-value: 5.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 12 RREWRRYLGAVALL-VIIAMLQLVPPkvvgI----VVDGV-TEQHFTTgqiLMWIATMVLIAVVVY-LLRYVWRVLLFGA 84
Cdd:COG4618 15 LRACRRAFLSVGLFsFFINLLMLTPP----LymlqVYDRVlTSRSVDT---LLMLTLLALGLYAVMgLLDAVRSRILVRV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 85 SYQLAVELREDYYRQLSRQHpefylRHRTGDLMARATNDVDRV-VFAAGEGVLTLVDS--LVMGCAVLIMMSTQISWqLT 161
Cdd:COG4618 88 GARLDRRLGPRVFDAAFRAA-----LRGGGGAAAQALRDLDTLrQFLTGPGLFALFDLpwAPIFLAVLFLFHPLLGL-LA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 162 LFSLLPMPVMAIMikrNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARID 241
Cdd:COG4618 162 LVGALVLVALALL---NERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 242 ARFDPTIYIAIGMANLLAIGGGSWMVVQGSLTLGQL--TSFMMYLGL-----MI--WPMLALAWmfnivergsAAYSRIR 312
Cdd:COG4618 239 GGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMiaASILMGRALapieqAIggWKQFVSAR---------QAYRRLN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 313 AMLAEAPVVNDGSePVPEGRGELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD 392
Cdd:COG4618 310 ELLAAVPAEPERM-PLPRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 393 IRFHDIPLtklqlDSW-RSRLAV----VSQTPFLFSDTVANNIA-LGCPNAtqQEIEHVARLASVHDDILRLPQGYDTEV 466
Cdd:COG4618 389 VRLDGADL-----SQWdREELGRhigyLPQDVELFDGTIAENIArFGDADP--EKVVAAAKLAGVHEMILRLPDGYDTRI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 467 GERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTE---HQILHNLRQwgQGRTVIISAHRLSALTEASEIIVM 543
Cdd:COG4618 462 GEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEaalAAAIRALKA--RGATVVVITHRPSLLAAVDKLLVL 539
|
570
....*....|....*..
gi 16128433 544 QHGHIAQRGNHD-VLAQ 559
Cdd:COG4618 540 RDGRVQAFGPRDeVLAR 556
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
72-531 |
1.97e-58 |
|
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: 204.13 E-value: 1.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 72 LLRYVWRVLLFGASYQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVD-------RVVFAAGEGVLTLVDSlVM 144
Cdd:TIGR02868 68 VFRYLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDalqdlyvRVIVPAGVALVVGAAA-VA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 145 GCAVLIMMSTQISWQLTLFSLLPMPVMAIMIKRNGDALherfklAQAAFSSLNDRTQESLTSIRMIKAFGLEDRqsalFA 224
Cdd:TIGR02868 147 AIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQA------LARLRGELAAQLTDALDGAAELVASGALPA----AL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 225 ADAEDTGKKNMRVARIDARF----DPTIYIAIGMANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNI 300
Cdd:TIGR02868 217 AQVEEADRELTRAERRAAAAtalgAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 301 VERGSAAYSRIRAMLAEAPVVNDGSEPVPEGRGELDVNIH----QFTYPQtDHPALENVNFALKPGQMLGICGPTGSGKS 376
Cdd:TIGR02868 297 LTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLElrdlSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 377 TLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDIL 456
Cdd:TIGR02868 376 TLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLR 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 457 RLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRL 531
Cdd:TIGR02868 456 ALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
342-546 |
5.27e-57 |
|
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: 190.37 E-value: 5.27e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYP---QTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHdipltklqldswrSRLAVVSQT 418
Cdd:cd03250 8 FTWDsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP-------------GSIAYVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 419 PFLFSDTVANNIALGCP-NatQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILD 497
Cdd:cd03250 75 PWIQNGTIRENILFGKPfD--EERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128433 498 DALSAVDGRTEHQILHN--LRQWGQGRTVIISAHRLSALTEASEIIVMQHG 546
Cdd:cd03250 153 DPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
348-574 |
1.72e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 191.98 E-value: 1.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQrHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVA 427
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL-GFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 NNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRT 507
Cdd:PRK11174 441 DNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 508 EHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQSGWYRDMYRYQQLE 574
Cdd:PRK11174 521 EQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
341-553 |
1.92e-53 |
|
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: 181.54 E-value: 1.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 341 QFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 420
Cdd:cd03244 9 SLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 421 LFSDTVANNIalgCPN--ATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDD 498
Cdd:cd03244 89 LFSGTIRSNL---DPFgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 499 ALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGN 553
Cdd:cd03244 166 ATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-311 |
2.85e-53 |
|
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: 183.51 E-value: 2.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAMLQLVPPKVVGIVVDGVTEQHFTTGQILmwiaTMVLIAVVVYLLRYV---WRVLLFG-ASYQLAVELRE 94
Cdd:cd18778 2 ILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLL----GLALLLLGAYLLRALlnfLRIYLNHvAEQKVVADLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 95 DYYRQLSRQHPEFYLRHRTGDLMARATNDVD---RVVFAAGEGVLTLVDSLVMGCAVLImmstQISWQLTLFSLLPMPVM 171
Cdd:cd18778 78 DLYDKLQRLSLRYFDDRQTGDLMSRVINDVAnveRLIADGIPQGITNVLTLVGVAIILF----SINPKLALLTLIPIPFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 172 AIMIKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIA 251
Cdd:cd18778 154 ALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 252 IGMANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18778 234 TSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
19-311 |
1.66e-52 |
|
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: 181.53 E-value: 1.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAML-QLVPPKVVGIVVDGVTEQHfTTGQILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYY 97
Cdd:cd18543 1 LILALLAALLATLaGLAIPLLTRRAIDGPIAHG-DRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 98 RQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMStqISWQLTLFSLLPMPVMAIMIKR 177
Cdd:cd18543 80 AHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVVMLV--LSPPLALVALASLPPLVLVARR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 178 NGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYI--AIGMA 255
Cdd:cd18543 158 FRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEAlpELGLA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 256 NLLAIGGgsWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18543 238 AVLALGG--WLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
13-559 |
3.19e-51 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 184.86 E-value: 3.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 13 REWRRYLGAVALL-VIIAMLQLVPPKVVGIVVDGVTEQhfTTGQILMWIATMVLIAVVVY-LLRYVWRVLLFGASYQLAV 90
Cdd:TIGR01842 2 AKVKRTFIIVGLFsFVINILMLAPPLYMLQVYDRVLTS--GSVPTLLMLTVLALGLYLFLgLLDALRSFVLVRIGEKLDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 91 ELREDYYRQLSRQHpefyLRHRTGDlMARATNDVDRV-VFAAGEGVLTLVDS-------------------LVMGCAVLI 150
Cdd:TIGR01842 80 ALNQPIFAASFSAT----LRRGSGD-GLQALRDLDQLrQFLTGPGLFAFFDApwmpiyllvcfllhpwigiLALGGAVVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 151 MmstqiswQLTLFSllpmpvMAIMIKRNGDALHERFKLAQAAFSSLndRTQESLTSIRMIKAFG--LEDRQSALFAADAE 228
Cdd:TIGR01842 155 V-------GLALLN------NRATKKPLKEATEASIRANNLADSAL--RNAEVIEAMGMMGNLTkrWGRFHSKYLSAQSA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 229 DTGKKNM-----RVARIdarfdptiyiaigMANLLAIGGGSWMVVQGSLTLGqltsfMMYLGLMIWPMlALAWMFNIVE- 302
Cdd:TIGR01842 220 ASDRAGMlsnlsKYFRI-------------VLQSLVLGLGAYLAIDGEITPG-----MMIAGSILVGR-ALAPIDGAIGg 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 303 -----RGSAAYSRIRAMLAEAPVvNDGSEPVPEGRGELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKST 377
Cdd:TIGR01842 281 wkqfsGARQAYKRLNELLANYPS-RDPAMPLPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKST 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 378 LLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILR 457
Cdd:TIGR01842 360 LARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILR 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 458 LPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQW-GQGRTVIISAHRLSALTE 536
Cdd:TIGR01842 440 LPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGC 519
|
570 580
....*....|....*....|....
gi 16128433 537 ASEIIVMQHGHIAQRGNHD-VLAQ 559
Cdd:TIGR01842 520 VDKILVLQDGRIARFGERDeVLAK 543
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
18-311 |
9.01e-51 |
|
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: 176.84 E-value: 9.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 18 YLGAVALLVIIAMLQLVPPKVVGIVVDGVTEQHftTGQILMWIATMVLIAVVVY-LLRYVWRVLLFGASYQLAVELREDY 96
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEK--DLEALLLVPLAIIGLFLLRgLASYLQTYLMAYVGQRVVRDLRNDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 97 YRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLV-DSLVMGCAVLIMMStqISWQLTLFSLLPMPVMAIMI 175
Cdd:cd18552 79 FDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVrDPLTVIGLLGVLFY--LDWKLTLIALVVLPLAALPI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 176 KRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYI--AIG 253
Cdd:cd18552 157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELlgAIA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 254 MANLLAIGGgsWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18552 237 IALVLWYGG--YQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
252-569 |
4.83e-50 |
|
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: 182.40 E-value: 4.83e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 252 IGMANLLAIGggSWMVVQGSLTLGQLTSFMMYLGLMIWpmlALAWMFNIVERGSAAYSRIRAMLAEAPVVNDGSEP---- 327
Cdd:TIGR01192 252 ISMMCILVIG--TVLVIKGELSVGEVIAFIGFANLLIG---RLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPadap 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 328 -VPEGRGELDVNIHQFTYPQTDHpALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLD 406
Cdd:TIGR01192 327 eLPNVKGAVEFRHITFEFANSSQ-GVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 407 SWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARA 486
Cdd:TIGR01192 406 SLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARA 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 487 LLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQSGWYRD 566
Cdd:TIGR01192 486 ILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYK 565
|
...
gi 16128433 567 MYR 569
Cdd:TIGR01192 566 LLR 568
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-311 |
2.20e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 173.47 E-value: 2.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAMLQLVPPKVVGIVVDGVTEQH-------------FTTGQILMWIA-TMVLIAVVVYLLRYVWRVLLFGA 84
Cdd:cd18564 2 ALALLALLLETALRLLEPWPLKVVIDDVLGDKplpgllglapllgPDPLALLLLAAaALVGIALLRGLASYAGTYLTALV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 85 SYQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMStQISWQLTLFS 164
Cdd:cd18564 82 GQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMF-WLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 165 LLPMPVMAIMIKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARF 244
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 245 DPTIYIAIGMANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-311 |
9.80e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 171.54 E-value: 9.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAMLQLVPPKVVGIVVDGV---TEQHFTTGQILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELRED 95
Cdd:cd18563 2 ILGFLLMLLGTALGLVPPYLTKILIDDVliqLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 96 YYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVMAIMI 175
Cdd:cd18563 82 LYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFS-LNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 176 KRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMA 255
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 256 NLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-311 |
1.92e-41 |
|
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: 151.95 E-value: 1.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 18 YLGAVALLVIIAMLQLVPPKVVGIVVDGVTEQHF--------------TTGQILMWIATMVLIAVVVYLLRYVWRVLLFG 83
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEAsflplvpaslgpadPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 84 ASYQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRV-VF---AAGEGVLTLVDSLVMGcAVLIMMStqisWQ 159
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLeRFlddGANSIIRVVVTVLGIG-AILFYLN----WQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 160 LTLFSLLPMPVMAIMIKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVAR 239
Cdd:cd18565 156 LALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 240 IDARFDPTIYIAIGMANLLAIGGGSWMVVQG------SLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18565 236 LRAAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
342-547 |
6.16e-41 |
|
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: 147.61 E-value: 6.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF- 420
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPDd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 421 -LFSDTVANNIALGCPNA--TQQEIEHVAR--LASVHDDIL--RLPQgydtevgergvMLSGGQKQRISIARALLVNAEI 493
Cdd:cd03225 87 qFFGPTVEEEVAFGLENLglPEEEIEERVEeaLELVGLEGLrdRSPF-----------TLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 494 LILDDALSAVDGRTEHQILHNLRQW-GQGRTVIISAHRLS-ALTEASEIIVMQHGH 547
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
19-311 |
1.11e-40 |
|
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: 149.46 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAMLQLVPPKVVGIVVDG-VTEQHFTTGQILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYY 97
Cdd:cd18544 2 ILALLLLLLATALELLGPLLIKRAIDDyIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 98 RQLSRQHPEFYLRHRTGDLMARATNDVDRV--VFAagEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVMAIMI 175
Cdd:cd18544 82 SHIQRLPLSFFDRTPVGRLVTRVTNDTEALneLFT--SGLVTLIGDLLLLIGILIAMFL-LNWRLALISLLVLPLLLLAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 176 KRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYI--AIG 253
Cdd:cd18544 159 YLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELlsSLA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 254 MANLLAIGGgsWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18544 239 LALVLWYGG--GQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
335-552 |
1.11e-40 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 145.53 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 335 LDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSRLAV 414
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 415 VSQTPFLFSDTVANNIalgcpnatqqeiehvarlasvhddilrlpqgydtevGERgvmLSGGQKQRISIARALLVNAEIL 494
Cdd:cd03247 80 LNQRPYLFDTTLRNNL------------------------------------GRR---FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 495 ILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRG 552
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
19-311 |
2.40e-40 |
|
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: 148.35 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAMLQLVPPKVVGIVVDGVTEQHFTTGqilmWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYYR 98
Cdd:cd18551 2 ILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGG----LLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 99 QLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVMAIMIKRN 178
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFL-LDWVLTLVTLAVVPLAFLIILPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 179 GDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLL 258
Cdd:cd18551 157 GRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 259 AIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18551 237 VLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
26-310 |
5.75e-40 |
|
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: 147.60 E-value: 5.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 26 VIIAMLQLVPPKVVGIVVDGVTEQHfTTGQILMWIATMVLIAVVVYLLRYVwrVLLFGASYQLAVE--LREDYYRQLSRQ 103
Cdd:cd18549 12 VLIAALDLVFPLIVRYIIDDLLPSK-NLRLILIIGAILLALYILRTLLNYF--VTYWGHVMGARIEtdMRRDLFEHLQKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 104 HPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVMAI-MIKRNGdAL 182
Cdd:cd18549 89 SFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLT-INVPLTLIVFALLPLMIIfTIYFNK-KM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 183 HERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIGG 262
Cdd:cd18549 167 KKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVLVA 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 16128433 263 GSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSR 310
Cdd:cd18549 247 GGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
339-548 |
2.01e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.42 E-value: 2.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 339 IHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT 418
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 419 PFLFSDTVANNIALGCPNATQQEIEHVAR--LASVH--DDILrlpqgyDTEVGErgvmLSGGQKQRISIARALLVNAEIL 494
Cdd:COG4619 83 PALWGGTVRDNLPFPFQLRERKFDRERALelLERLGlpPDIL------DKPVER----LSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 495 ILDDALSAVDGRTEHQILHNLRQW--GQGRTVIISAH-RLSALTEASEIIVMQHGHI 548
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
18-311 |
2.52e-39 |
|
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: 145.69 E-value: 2.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 18 YLGAVALLVIIAML-QLVPPKVVGIVVDGVTEQHFTTGqILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDY 96
Cdd:cd18545 1 KLLLALLLMLLSTAaSLAGPYLIKIAIDEYIPNGDLSG-LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 97 YRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLV-DSLVMGCAVLIMMStqISWQLTLFSLLPMPVMAIMI 175
Cdd:cd18545 80 FSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIpDLLTLVGIVIIMFS--LNVRLALVTLAVLPLLVLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 176 KRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMA 255
Cdd:cd18545 158 FLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALG 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 256 NLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18545 238 TALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
79-569 |
7.31e-39 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 153.56 E-value: 7.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 79 VLLFGASYQLAV-------ELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSL--VMGCAVL 149
Cdd:TIGR00957 1020 FAVFGYSMAVSIggiqasrVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLfnVIGALIV 1099
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 150 IMMSTQISWQLtlfsLLPMPVMAIMIKRNGDALHERFK-LAQAAFSSLNDRTQESLTSIRMIKAFglEDRQSALFAADAE 228
Cdd:TIGR00957 1100 ILLATPIAAVI----IPPLGLLYFFVQRFYVASSRQLKrLESVSRSPVYSHFNETLLGVSVIRAF--EEQERFIHQSDLK 1173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 229 -DTGKKNMRVARIDARfdptiYIAIGM---ANLLAIGGGSWMVV-QGSLTLGqLTSFMMYLGLMIwpMLALAWMFNI--- 300
Cdd:TIGR00957 1174 vDENQKAYYPSIVANR-----WLAVRLecvGNCIVLFAALFAVIsRHSLSAG-LVGLSVSYSLQV--TFYLNWLVRMsse 1245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 301 VERGSAAYSRIRAML---AEAPVVNDGSEPvPEG---RGELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSG 374
Cdd:TIGR00957 1246 METNIVAVERLKEYSeteKEAPWQIQETAP-PSGwppRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAG 1324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 375 KSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIAlgcP--NATQQEIEHVARLASVH 452
Cdd:TIGR00957 1325 KSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD---PfsQYSDEEVWWALELAHLK 1401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 453 DDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLS 532
Cdd:TIGR00957 1402 TFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLN 1481
|
490 500 510
....*....|....*....|....*....|....*..
gi 16128433 533 ALTEASEIIVMQHGHIAQRGNHDVLAQQSGWYRDMYR 569
Cdd:TIGR00957 1482 TIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
342-560 |
1.65e-38 |
|
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: 141.32 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQtDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLI---QRHfdvSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT 418
Cdd:COG1122 8 FSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLnglLKP---TSGEVLVDGKDITKKNLRELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 419 PF--LFSDTVANNIALGCPNA--TQQEIEHVAR--LASVH-DDIL-RLPQgydtevgergvMLSGGQKQRISIARALLVN 490
Cdd:COG1122 84 PDdqLFAPTVEEDVAFGPENLglPREEIRERVEeaLELVGlEHLAdRPPH-----------ELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128433 491 AEILILDDALSAVDGRTEHQILHNLRQWGQ-GRTVIISAHRLSALTE-ASEIIVMQHGHIAQRGN-HDVLAQQ 560
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTpREVFSDY 225
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
19-311 |
2.02e-38 |
|
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: 143.01 E-value: 2.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAMLQLVPPKVVGIVVD-GVTEQHFTTgqiLMWIATMVLIAVVVYLLRYVWRVLLFG-ASYQLAVELREDY 96
Cdd:cd18546 2 ALALLLVVVDTAASLAGPLLVRYGIDsGVRAGDLGV---LLLAAAAYLAVVLAGWVAQRAQTRLTGrTGERLLYDLRLRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 97 YRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVMAIMIK 176
Cdd:cd18546 79 FAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLV-LDPRLALVALAALPPLALATR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 177 RNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMAN 256
Cdd:cd18546 158 WFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLAT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 257 LLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18546 238 AAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
352-501 |
7.22e-38 |
|
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: 137.01 E-value: 7.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TVANNI 430
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 431 ALGCPNATQQEIEHVARLASVHDDiLRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
271-559 |
5.52e-37 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 147.48 E-value: 5.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 271 SLTLGQLTSfmMYLGLMIWPmlalawmfNIVE--RGSAAYSRIRAMLAEAPVV--NDGSEPVPEGRGELDVNIhQFTY-P 345
Cdd:PTZ00265 326 SILLGVLIS--MFMLTIILP--------NITEymKSLEATNSLYEIINRKPLVenNDDGKKLKDIKKIQFKNV-RFHYdT 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 346 QTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI-PLTKLQLDSWRSRLAVVSQTPFLFSD 424
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSN 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 TVANNIALGC----------------PNATQQ-----------------------------------------EIEHVAR 447
Cdd:PTZ00265 475 SIKNNIKYSLyslkdlealsnyynedGNDSQEnknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSK 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 448 LASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEH---QILHNLRQwGQGRTV 524
Cdd:PTZ00265 555 KVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYlvqKTINNLKG-NENRIT 633
|
330 340 350
....*....|....*....|....*....|....*
gi 16128433 525 IISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQ 559
Cdd:PTZ00265 634 IIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGE 668
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
19-311 |
9.00e-37 |
|
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: 138.69 E-value: 9.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAMLQLVPPKVVGIVVDGVTEQHFTTGQ-----ILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELR 93
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGvdfsgLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 94 EDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVMAI 173
Cdd:cd18547 82 KDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLY-ISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 174 MIKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAA---DAEDTGKKNMRVARIdarFDPTI-- 248
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEineELYKASFKAQFYSGL---LMPIMnf 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 249 -----YIAIGMAnllaiggGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18547 238 innlgYVLVAVV-------GGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
281-569 |
1.04e-36 |
|
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: 147.01 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 281 MMYLGLMIWPMLalawMFNIVErGSAAYSRIRAMLAEAPVVNDGSE--PVPEGRGElDVNIHQ--FTYPQTDHPALENVN 356
Cdd:TIGR00957 585 ILRFPLNILPMV----ISSIVQ-ASVSLKRLRIFLSHEELEPDSIErrTIKPGEGN-SITVHNatFTWARDLPPTLNGIT 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 357 FALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFhdipltklqldswRSRLAVVSQTPFLFSDTVANNIALGC-- 434
Cdd:TIGR00957 659 FSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-------------KGSVAYVPQQAWIQNDSLRENILFGKal 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 435 -PNATQQEIEHVARLAsvhdDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILH 513
Cdd:TIGR00957 726 nEKYYQQVLEACALLP----DLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 514 NL---RQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQSGWYRDMYR 569
Cdd:TIGR00957 802 HVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLR 860
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
342-548 |
1.09e-36 |
|
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: 134.65 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 421
Cdd:cd03246 8 FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 FSDTVANNIalgcpnatqqeiehvarlasvhddilrlpqgydtevgergvmLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:cd03246 88 FSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128433 502 AVDGRTEHQILHNLRQW-GQGRTVIISAHRLSALTEASEIIVMQHGHI 548
Cdd:cd03246 126 HLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
333-552 |
2.74e-36 |
|
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: 134.46 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 333 GELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL 412
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 413 AVVSQTPFLFSDTVANNIAlgcPNATQQEIEHVARLasvhddilrlpqgydtEVGERGVMLSGGQKQRISIARALLVNAE 492
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLD---PFDEYSDEEIYGAL----------------RVSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 493 ILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRG 552
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
339-547 |
2.28e-35 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 130.44 E-value: 2.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 339 IHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQt 418
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 419 pflfsdtvannialgcpnatqqeiehvarlasvhddilrlpqgydtevgergvmLSGGQKQRISIARALLVNAEILILDD 498
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128433 499 ALSAVDGRTEHQILHNLRQWGQ-GRTVIISAHRLSALTEAS-EIIVMQHGH 547
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
21-311 |
2.82e-35 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 134.15 E-value: 2.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 21 AVALLVIIAMLQLVPPKVVGIVVDGVTEQHFTT---GQILMWIATMVLIAVVVYllryvWRVLLFG-ASYQLAVELREDY 96
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTAslnQIALLLLGLFLLQAVFSF-----FRIYLFArVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 97 YRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVM--GCAVLIMmstQISWQLTLFSLLPMPVMAIM 174
Cdd:cd18576 76 YRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTliGGVVLLF---FISWKLTLLMLATVPVVVLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 175 IKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAI-- 252
Cdd:cd18576 153 AVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLfg 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 253 GMANLLAIGGGswMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18576 233 AIVAVLWYGGR--LVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
19-311 |
3.80e-35 |
|
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: 134.06 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAMLQLVPPKVVGIVVD-GVTEQHftTGQILMWIATMVLIAVVVYLLRYVwrVLLFGA--SYQLAVELRED 95
Cdd:cd18548 2 ILAPLFKLLEVLLELLLPTLMADIIDeGIANGD--LSYILRTGLLMLLLALLGLIAGIL--AGYFAAkaSQGFGRDLRKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 96 YYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVMAIMI 175
Cdd:cd18548 78 LFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFR-INPKLALILLVAIPILALVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 176 KRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMA 255
Cdd:cd18548 157 FLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 256 NLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18548 237 IVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
333-569 |
1.33e-34 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 131.57 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 333 GELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL 412
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 413 AVVSQTPFLFSDTVANNI--ALGCPNATQQEIEHVARLASVhddILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVN 490
Cdd:cd03288 98 SIILQDPILFSGSIRFNLdpECKCTDDRLWEALEIAQLKNM---VKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 491 AEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGN-HDVLAQQSGWYRDMYR 569
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTpENLLAQEDGVFASLVR 254
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
21-311 |
1.63e-34 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 132.30 E-value: 1.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 21 AVALLVIIAMLQLVPPKVVGIVVDGVTEQhFTTGQILMWIATMVLIAVVVYLLRYVwRVLLFG-ASYQLAVELREDYYRQ 99
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKG-GDLDVLNELALILLAIYLLQSVFTFV-RYYLFNiAGERIVARLRRDLFSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 100 LSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVMAIMIKRNG 179
Cdd:cd18557 79 LLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFI-LSWKLTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 180 DALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLA 259
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 16128433 260 IGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18557 238 LWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
348-552 |
1.72e-34 |
|
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: 129.95 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqLDSWRSRLAVVSQTPFLFSD-TV 426
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG--VPPERRNIGMVFQDYALFPHlTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALGC-----PNATQQEIEHvARLASVHDDIL--RLPQgydtevgergvMLSGGQKQRISIARALLVNAEILILDDA 499
Cdd:cd03259 90 AENIAFGLklrgvPKAEIRARVR-ELLELVGLEGLlnRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 500 LSAVDGRTEHQILHNLR--QWGQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:cd03259 158 LSALDAKLREELREELKelQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
21-307 |
2.70e-34 |
|
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: 131.51 E-value: 2.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 21 AVALLVIIAMLQLVPPKVVGIVVDGVTEQhFTTGQILMWIATMVLIAVVVYLLRYvWRVLLFGASYQ-LAVELREDYYRQ 99
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVAD-GSREAFYRAVLLLLLLSVLSGLFSG-LRGGCFSYAGTrLVRRLRRDLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 100 LSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVMAIMIKRNG 179
Cdd:cd18572 79 LLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFS-LSWRLTLLAFITVPVIALITKVYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 180 DALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLA 259
Cdd:cd18572 158 RYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 16128433 260 IGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAA 307
Cdd:cd18572 238 LFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGA 285
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
336-552 |
6.91e-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: 128.78 E-value: 6.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 336 DVNIHqFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRL 412
Cdd:cd03257 6 NLSVS-FPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrLRKIRRKEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 413 AVVSQTPFL---FSDTVANNIA-----LGCPNATQQEIEHVARLASVHDDILRLPQGYDTEvgergvmLSGGQKQRISIA 484
Cdd:cd03257 85 QMVFQDPMSslnPRMTIGEQIAeplriHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHE-------LSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 485 RALLVNAEILILDDALSAVDGRTEHQILHNLR--QWGQGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
348-560 |
9.17e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 128.64 E-value: 9.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTPFLFSD-TV 426
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYPDlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIAL-----GCPNATQQEieHVARLAsvhdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:COG1131 91 RENLRFfarlyGLPRKEARE--RIDELL----ELFGLTDAADRKVGT----LSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128433 502 AVD--GRTE-HQILHNLRQwgQGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRGNHDVLAQQ 560
Cdd:COG1131 161 GLDpeARRElWELLRELAA--EGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-548 |
3.05e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 136.26 E-value: 3.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 7 LSWYFRREWRRYLGAVALLVII-------AMLQLVPPKVVGIVVDGVTEQHFTTGQILMWIATMVLIAVVVYLLRYVWrv 79
Cdd:PLN03232 896 ISWNVLMRYNKAVGGLWVVMILlvcylttEVLRVSSSTWLSIWTDQSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFW-- 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 80 lLFGASYQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDV---DRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqi 156
Cdd:PLN03232 974 -LISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIgdiDRNVANLMNMFMNQLWQLLSTFALIGTVST-- 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 157 swqLTLFSLLPMPVM---AIMIKRNGDalHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDtgkk 233
Cdd:PLN03232 1051 ---ISLWAIMPLLILfyaAYLYYQSTS--REVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDN---- 1121
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 234 NMRVARIDARFDPTIYIaigmaNLLAIGG------GSWMVVQGSLTLGQlTSFMMYLGLMIWPMLALAWMF-NIVERGSA 306
Cdd:PLN03232 1122 NIRFTLANTSSNRWLTI-----RLETLGGvmiwltATFAVLRNGNAENQ-AGFASTMGLLLSYTLNITTLLsGVLRQASK 1195
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 307 AYSRIRA---------MLAEAPVVNDGSEPVP--EGRGELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGK 375
Cdd:PLN03232 1196 AENSLNSvervgnyidLPSEATAIIENNRPVSgwPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGK 1275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 376 STLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARlASVHDDI 455
Cdd:PLN03232 1276 SSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALER-AHIKDVI 1354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 456 LRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALT 535
Cdd:PLN03232 1355 DRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTII 1434
|
570
....*....|...
gi 16128433 536 EASEIIVMQHGHI 548
Cdd:PLN03232 1435 DCDKILVLSSGQV 1447
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
21-311 |
4.45e-33 |
|
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: 128.40 E-value: 4.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 21 AVALLVIIAMLQLVPPKVVGIVVDGVTEQHFTTGQILMWIATMVLIAVVVYLL----RYVwRVLLFG-ASYQLAVELRED 95
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALALLGVFVVgaaaNFG-RVYLLRiAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 96 YYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVMAIMI 175
Cdd:cd18573 80 LFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLY-ISPKLTLVMLLVVPPIAVGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 176 KRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMA 255
Cdd:cd18573 159 VFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 256 NLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18573 239 LLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
300-559 |
4.88e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 132.72 E-value: 4.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 300 IVERGSAA-YSRIRAMLAEAPVVNDGSEPVPEGRGE----LDV-NIHqFTYPQ---TDHPALENVNFALKPGQMLGICGP 370
Cdd:COG1123 221 IVEDGPPEeILAAPQALAAVPRLGAARGRAAPAAAAaeplLEVrNLS-KRYPVrgkGGVRAVDDVSLTLRRGETLGLVGE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 371 TGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPF--LF-SDTVANNIALGCPN---ATQQE 441
Cdd:COG1123 300 SGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRELRRRVQMVFQDPYssLNpRMTVGDIIAEPLRLhglLSRAE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 442 IEHVAR--LASVH---DDILRLPQgydtevgergvMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLR 516
Cdd:COG1123 380 RRERVAelLERVGlppDLADRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLR 448
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16128433 517 QWGQ--GRTVIISAHRLSALTE-ASEIIVMQHGHIAQRGN-HDVLAQ 559
Cdd:COG1123 449 DLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPtEEVFAN 495
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
347-546 |
6.02e-33 |
|
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: 125.91 E-value: 6.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 347 TDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR----LAVVSQTPFLF 422
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 SDTVANNIALGCPnATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSA 502
Cdd:cd03290 92 NATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128433 503 VDGR-TEHQILHNLRQWGQG--RTVIISAHRLSALTEASEIIVMQHG 546
Cdd:cd03290 171 LDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
148-565 |
9.33e-33 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 134.77 E-value: 9.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 148 VLIMMSTQISWQ--------LTLFSLLPMPVMAIM--IKRNGDALHERFKLAQAAFSSLNDR---------TQESLTSIR 208
Cdd:PTZ00265 954 VLFLVSMVMSFYfcpivaavLTGTYFIFMRVFAIRarLTANKDVEKKEINQPGTVFAYNSDDeifkdpsflIQEAFYNMN 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 209 MIKAFGLEDRQSALF--AADAEDTGKKnmRVARIDAR---FDPTIYIAIgmaNLLAIGGGSWMVVQGSLtlgQLTSFMMY 283
Cdd:PTZ00265 1034 TVIIYGLEDYFCNLIekAIDYSNKGQK--RKTLVNSMlwgFSQSAQLFI---NSFAYWFGSFLIRRGTI---LVDDFMKS 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 284 LGLMIWPMLALAWMFNI---VERGSAAYSRIRAMLAEAP---VVNDGSEPVPEG---RGELDVNIHQFTY-PQTDHPALE 353
Cdd:PTZ00265 1106 LFTFLFTGSYAGKLMSLkgdSENAKLSFEKYYPLIIRKSnidVRDNGGIRIKNKndiKGKIEIMDVNFRYiSRPNVPIYK 1185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 354 NVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDV--------------------------------------------- 388
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkegg 1265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 389 ---------SEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDDILRLP 459
Cdd:PTZ00265 1266 sgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLP 1345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 460 QGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTEA 537
Cdd:PTZ00265 1346 NKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRS 1425
|
490 500 510
....*....|....*....|....*....|....
gi 16128433 538 SEIIVMQH----GHIAQ-RGNHD-VLAQQSGWYR 565
Cdd:PTZ00265 1426 DKIVVFNNpdrtGSFVQaHGTHEeLLSVQDGVYK 1459
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
339-543 |
9.13e-32 |
|
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: 122.26 E-value: 9.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 339 IHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldswRSRLAVVSQT 418
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 419 ---PFLFSDTVANNIALGC-------PNATQQEIEHVAR-LASVhdDIlrlpqgydTEVGERGV-MLSGGQKQRISIARA 486
Cdd:cd03235 77 rsiDRDFPISVRDVVLMGLyghkglfRRLSKADKAKVDEaLERV--GL--------SELADRQIgELSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 487 LLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ-GRTVIISAHRLSALTEASEIIVM 543
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDRVLL 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
348-560 |
1.25e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.89 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLI---QRHfdvSEGDIRFHDIPLTKLqldswRSRLAVVSQTPFLFSD 424
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIlglLPP---TSGTVRLFGKPPRRA-----RRRIGYVPQRAEVDWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 ---TVANNIALGC-------PNATQQEIEHVAR-LASVH-DDILRLPqgydteVGErgvmLSGGQKQRISIARALLVNAE 492
Cdd:COG1121 90 fpiTVRDVVLMGRygrrglfRRPSRADREAVDEaLERVGlEDLADRP------IGE----LSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 493 ILILDDALSAVDGRTEHQILHNLRQW-GQGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRGNHDVLAQQ 560
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLVAHGPPEEVLTPE 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
342-557 |
2.25e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 122.46 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPqtDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 421
Cdd:COG1120 9 VGYG--GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 -FSDTVANNIALGC-------PNATQQEIEHVAR-LASVHDDILRlpqgyDTEVGErgvmLSGGQKQRISIARALLVNAE 492
Cdd:COG1120 87 pFGLTVRELVALGRyphlglfGRPSAEDREAVEEaLERTGLEHLA-----DRPVDE----LSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 493 ILILDDALSAVDGRTEHQILHNLRQW--GQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGN-HDVL 557
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPpEEVL 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
342-552 |
4.41e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 119.08 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQtdHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQtpfl 421
Cdd:cd03214 7 VGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 fsdtvanniALgcpnaTQQEIEHVArlasvhddilrlpqgydtevgERGVM-LSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:cd03214 81 ---------AL-----ELLGLAHLA---------------------DRPFNeLSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 501 SAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
348-548 |
8.56e-31 |
|
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: 118.27 E-value: 8.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTPFLFSD-TV 426
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIalgcpnatqqeiehvarlasvhddilrlpqgydtevgergvMLSGGQKQRISIARALLVNAEILILDDALSAVD-- 504
Cdd:cd03230 91 RENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDpe 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128433 505 GRTE-HQILHNLRQwgQGRTVIISAHRLSALTE-ASEIIVMQHGHI 548
Cdd:cd03230 130 SRREfWELLRELKK--EGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
337-547 |
8.98e-31 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 118.44 E-value: 8.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 337 VNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS--WRSRLAV 414
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 415 VSQTPFLFSD-TVANNIALGcpnatqqeiehvarlasvhddilrlpqgydtevgergvmLSGGQKQRISIARALLVNAEI 493
Cdd:cd03229 81 VFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 494 LILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLS-ALTEASEIIVMQHGH 547
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
333-550 |
9.00e-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: 121.50 E-value: 9.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 333 GELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHDIPLTKLQLDSWRSRL 412
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 413 AVVSQTPFLFSDTVANNI-ALGCPNatQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNA 491
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLdPYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 492 EILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQ 550
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
342-552 |
1.53e-30 |
|
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: 119.22 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQT 418
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 419 PFLFSD-TVANNIALgcPnatqQEIEHVARlASVHDDILRL---------PQGYDTEvgergvmLSGGQKQRISIARALL 488
Cdd:cd03258 91 FNLLSSrTVFENVAL--P----LEIAGVPK-AEIEERVLELlelvgledkADAYPAQ-------LSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 489 VNAEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEG 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
348-588 |
1.70e-30 |
|
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: 119.58 E-value: 1.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTPFLFSD-TV 426
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVLPDERGLYDRlTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALGCPNATQQEIEHVARLASVhDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDDALSAVDGR 506
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEEL-IELLGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 507 TEHQILHNLRQWG-QGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRGNHDVLAQQsgwyrdmYRYQQLEAALDDAPENR 584
Cdd:COG4555 167 ARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE-------IGEENLEDAFVALIGSE 239
|
....
gi 16128433 585 EEAV 588
Cdd:COG4555 240 EGEA 243
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
149-567 |
1.80e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 127.78 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 149 LIMMSTQISWQLTLFSLLPMPVMAIMIKRNGDALHERFKLAQAAFSSLNDR---TQESLTSIRMIKAFGLEDR-QSALFA 224
Cdd:PLN03232 428 IIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRvgiINEILASMDTVKCYAWEKSfESRIQG 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 225 ADAEDTGKknMRVARIDARFDPTIYIAIGMANLLaIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERG 304
Cdd:PLN03232 508 IRNEELSW--FRKAQLLSAFNSFILNSIPVVVTL-VSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 305 SAAYSRIRAMLAEAPVVNDGSEPVPEGRGELDVNIHQFTY-PQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQ 383
Cdd:PLN03232 585 NVSLQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 384 ---RHFDVSEGDIRfhdipltklqldswrSRLAVVSQTPFLFSDTVANNIALGCPNATQQEIEHVARLASVHDdiLRLPQ 460
Cdd:PLN03232 665 gelSHAETSSVVIR---------------GSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHD--LDLLP 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 461 GYD-TEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHN-LRQWGQGRTVIISAHRLSALTEAS 538
Cdd:PLN03232 728 GRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMD 807
|
410 420
....*....|....*....|....*....
gi 16128433 539 EIIVMQHGHIAQRGNHDVLAQQSGWYRDM 567
Cdd:PLN03232 808 RIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
21-291 |
2.07e-30 |
|
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: 120.44 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 21 AVALLVIIAMLQLVPPKVVGIVVDGVTEQ----HFTTGQILMWIATMVLIAVVVYLLR-YVWRVllfgASYQLAVELRED 95
Cdd:pfam00664 4 AILLAILSGAISPAFPLVLGRILDVLLPDgdpeTQALNVYSLALLLLGLAQFILSFLQsYLLNH----TGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 96 YYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTQiSWQLTLFSLLPMPVMAIMI 175
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY-GWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 176 KRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMA 255
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 16128433 256 NLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPM 291
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-559 |
3.55e-30 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 124.25 E-value: 3.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 335 LDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQR---HFDVSEGDIRFHDIPLTKLQLDSWRSR 411
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 412 LAVVSQTPF--LFSDTVANNIALGCPN--ATQQEIEHVAR--LASVHddILRLPQGYDTEvgergvmLSGGQKQRISIAR 485
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAEALENlgLSRAEARARVLelLEAVG--LERRLDRYPHQ-------LSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 486 ALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTE-ASEIIVMQHGHIAQRGN-HDVLAQ 559
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPpEEILAA 233
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
343-548 |
6.98e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 117.85 E-value: 6.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 343 TYPqTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTP 419
Cdd:COG3638 11 RYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLRRRIGMIFQQF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 FLFSD-TVANNIALGC-----------PNATQQEIEHVAR-LASVhdDIL-RLPQgydtevgeRGVMLSGGQKQRISIAR 485
Cdd:COG3638 90 NLVPRlSVLTNVLAGRlgrtstwrsllGLFPPEDRERALEaLERV--GLAdKAYQ--------RADQLSGGQQQRVAIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 486 ALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLS-ALTEASEIIVMQHGHI 548
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDlARRYADRIIGLRDGRV 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
340-549 |
1.12e-29 |
|
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: 117.60 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 340 HQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 419
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 FLFSD---TVANNIA-----LGCPNaTQQEIEHVARLASVHDDIL-RLPQgydtevgergvMLSGGQKQRISIARALLVN 490
Cdd:COG1124 89 YASLHprhTVDRILAeplriHGLPD-REERIAELLEQVGLPPSFLdRYPH-----------QLSGGQRQRVAIARALILE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128433 491 AEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTEASE-IIVMQHGHIA 549
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLCDrVAVMQNGRIV 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
342-548 |
2.35e-29 |
|
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: 115.66 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTD--HPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSR-LAVV 415
Cdd:cd03255 8 KTYGGGGekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekELAAFRRRhIGFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 416 SQTPFLFSD-TVANNIALGCPNATQQEIEHVARLASVHdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEIL 494
Cdd:cd03255 88 FQSFNLLPDlTALENVELPLLLAGVPKKERRERAEELL-ERVGLGDRLNHYPSE----LSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 495 ILDDALSAVDGRTEHQILHNLRQW--GQGRTVIISAHRLSALTEASEIIVMQHGHI 548
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
343-548 |
4.15e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 115.14 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 343 TYPQ--TDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLI---QRhfdVSEGDIRFHDIPLTKL---QLDSWRSR-LA 413
Cdd:COG1136 13 SYGTgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILgglDR---PTSGEVLIDGQDISSLserELARLRRRhIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 414 VVSQTPFLFSD-TVANNIALGC------PNATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARA 486
Cdd:COG1136 90 FVFQFFNLLPElTALENVALPLllagvsRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128433 487 LLVNAEILILDDALSAVDGRTEHQILHNLRQW--GQGRTVIISAHRLSALTEASEIIVMQHGHI 548
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
273-548 |
7.07e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 122.92 E-value: 7.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 273 TLGQLTSFMMYLGLMIWPMLALAWM----FNIVERgSAAYSRIRAmlaEAPVVNDGSEPVP--EGRGELDVNIHQFTYPQ 346
Cdd:PLN03130 1174 TMGLLLSYALNITSLLTAVLRLASLaensLNAVER-VGTYIDLPS---EAPLVIENNRPPPgwPSSGSIKFEDVVLRYRP 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 347 TDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTV 426
Cdd:PLN03130 1250 ELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTV 1329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIAlgcPNATQQEIEHVARLASVH--DDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVD 504
Cdd:PLN03130 1330 RFNLD---PFNEHNDADLWESLERAHlkDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 16128433 505 GRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHI 548
Cdd:PLN03130 1407 VRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRV 1450
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
342-552 |
9.61e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 115.22 E-value: 9.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLlsliQRHFDV----SEGDIRFHDI-PLTKLQLDSWRSRLAVVS 416
Cdd:TIGR04520 8 FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTL----AKLLNGlllpTSGKVTVDGLdTLDEENLWEIRKKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 417 QTPflfsD------TVANNIALGCPNA------TQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIA 484
Cdd:TIGR04520 84 QNP----DnqfvgaTVEDDVAFGLENLgvpreeMRKRVDEALKLVGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 485 RALLVNAEILILDDALSAVD--GRTE-HQILHNLRQwGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRG 552
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDpkGRKEvLETIRKLNK-EEGITVISITHDMEEAVLADRVIVMNKGKIVAEG 218
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
352-590 |
2.79e-28 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 121.04 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldsWRSR-LAVVSQTPFLFSDTVANNI 430
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAERsIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 431 ALGCPNATQQeIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQ 510
Cdd:PTZ00243 742 LFFDEEDAAR-LADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 511 ILHN-LRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQSgwyrdmyRYQQLEAALDDAPENREEAVD 589
Cdd:PTZ00243 821 VVEEcFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-------LYATLAAELKENKDSKEGDAD 893
|
.
gi 16128433 590 A 590
Cdd:PTZ00243 894 A 894
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
343-552 |
2.95e-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: 113.05 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 343 TYPQtDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ---LDSWRSRLAVVSQTP 419
Cdd:cd03256 9 TYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQIGMIFQQF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 FLFSD-TVANNIALGcpnatqqeiehvaRLASVH--DDILRLPQGYDTE--------VG------ERGVMLSGGQKQRIS 482
Cdd:cd03256 88 NLIERlSVLENVLSG-------------RLGRRStwRSLFGLFPKEEKQralaalerVGlldkayQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128433 483 IARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDlAREYADRIVGLKDGRIVFDG 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
345-557 |
4.20e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 120.23 E-value: 4.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 345 PQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIqrhfdvsegdirFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD 424
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM------------LGELPPRSDASVVIRGTVAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 TVANNIALGCPnATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVD 504
Cdd:PLN03130 694 TVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128433 505 GRTEHQILHN-LRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRGNHDVL 557
Cdd:PLN03130 773 AHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
342-552 |
1.82e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 111.62 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP-- 419
Cdd:PRK13632 15 FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPdn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 -FLFSdTVANNIALGC------PNATQQEIEHVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARALLVNAE 492
Cdd:PRK13632 95 qFIGA-TVEDDIAFGLenkkvpPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128433 493 ILILDDALSAVDGRTEH---QILHNLRQWGQgRTVIISAHRLSALTEASEIIVMQHGHIAQRG 552
Cdd:PRK13632 163 IIIFDESTSMLDPKGKReikKIMVDLRKTRK-KTLISITHDMDEAILADKVIVFSEGKLIAQG 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
329-550 |
2.10e-27 |
|
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: 118.09 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 329 PEGrGELDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHDIPLTKLQLDSW 408
Cdd:TIGR01271 1213 PSG-GQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTW 1290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 409 RSRLAVVSQTPFLFSDTVANNIAlgcPNA--TQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARA 486
Cdd:TIGR01271 1291 RKAFGVIPQKVFIFSGTFRKNLD---PYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARS 1367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128433 487 LLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQ 550
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
348-552 |
2.33e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 113.27 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldSWRSRLAVVSQTPFLFSD-TV 426
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP--PEKRNVGMVFQDYALFPHlTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIA-----LGCPNATQQEIehVARLAsvhdDILRLpqgydTEVGERGV-MLSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:COG3842 95 AENVAfglrmRGVPKAEIRAR--VAELL----ELVGL-----EGLADRYPhQLSGGQQQRVALARALAPEPRVLLLDEPL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 501 SAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:COG3842 164 SALDAKLREEMREELRRLQRelGITFIYVTHDQEeALALADRIAVMNDGRIEQVG 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
340-551 |
2.66e-27 |
|
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: 109.87 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 340 HQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldswRSRLAVVSQTP 419
Cdd:cd03293 8 KTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDRGYVFQQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 FLFS-DTVANNIALGCpnatqqEIEHVARlasvhDDILRLPQGYDTEVGERGV------MLSGGQKQRISIARALLVNAE 492
Cdd:cd03293 83 ALLPwLTVLDNVALGL------ELQGVPK-----AEARERAEELLELVGLSGFenayphQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 493 ILILDDALSAVDGRTEHQiLHN--LRQWGQ-GRTVIISAHRLS-ALTEASEIIVM--QHGHIAQR 551
Cdd:cd03293 152 VLLLDEPFSALDALTREQ-LQEelLDIWREtGKTVLLVTHDIDeAVFLADRVVVLsaRPGRIVAE 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
343-548 |
4.84e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 108.99 E-value: 4.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 343 TYPQtDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTP 419
Cdd:COG2884 10 RYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRRIGVVFQDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 FLFSD-TVANNIAL-----GcpnATQQEIEHVARlasvhdDILRLpqgydteVGERGVM------LSGGQKQRISIARAL 487
Cdd:COG2884 89 RLLPDrTVYENVALplrvtG---KSRKEIRRRVR------EVLDL-------VGLSDKAkalpheLSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 488 LVNAEILILDDALSAVDGRTEHQI---LHNLRQwgQGRTVIISAHRLSALTEA-SEIIVMQHGHI 548
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEImelLEEINR--RGTTVLIATHDLELVDRMpKRVLELEDGRL 215
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
348-552 |
7.52e-27 |
|
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: 108.81 E-value: 7.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDV-----SEGDIRF--HDIPLTKLQLDSWRSRLAVVSQTPF 420
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLdgKDIYDLDVDVLELRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 421 LFSDTVANNIALGCP-------NATQQEIEHVARLASVHDDILRLPQGYDtevgergvmLSGGQKQRISIARALLVNAEI 493
Cdd:cd03260 92 PFPGSIYDNVAYGLRlhgiklkEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRLCLARALANEPEV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 494 LILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:cd03260 163 LLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFG 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
340-543 |
9.02e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 109.41 E-value: 9.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 340 HQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldswRSRLAVVSQTP 419
Cdd:COG1116 15 KRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPDRGVVFQEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 FLFS-DTVANNIALGCPNATQQEIEHVARLasvhDDILRLpqgydteVGERGVM------LSGGQKQRISIARALLVNAE 492
Cdd:COG1116 90 ALLPwLTVLDNVALGLELRGVPKAERRERA----RELLEL-------VGLAGFEdayphqLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 493 ILILDDALSAVDGRTEHQiLHN--LRQWGQ-GRTVIISAHRLS-ALTEASEIIVM 543
Cdd:COG1116 159 VLLMDEPFGALDALTRER-LQDelLRLWQEtGKTVLFVTHDVDeAVFLADRVVVL 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
348-540 |
1.52e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 107.18 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTPFLFSD-TV 426
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALGC----PNATQQEIEHVArlasvhdDILRLPQGYDTEVGergvMLSGGQKQRISIARALLVNAEILILDDALSA 502
Cdd:COG4133 93 RENLRFWAalygLRADREAIDEAL-------EAVGLAGLADLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 16128433 503 VDGRTEHQILHNLRQW-GQGRTVIISAHRLSALTEASEI 540
Cdd:COG4133 162 LDAAGVALLAELIAAHlARGGAVLLTTHQPLELAAARVL 200
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-295 |
2.45e-26 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 109.11 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAMLQLVPPKVVGIVVD-GVTEQHFttgQILMWIA-TMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDY 96
Cdd:cd18550 2 ALVLLLILLSALLGLLPPLLLREIIDdALPQGDL---GLLVLLAlGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 97 YRQLSRQHPEFYLRHRTGDLMARATNDVDRVvfaagEGVLT-----LVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVM 171
Cdd:cd18550 79 YAHLQRMSLAFFTRTRTGEIQSRLNNDVGGA-----QSVVTgtltsVVSNVVTLVATLVAMLA-LDWRLALLSLVLLPLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 172 AIMIKRNGDALHERFKLAQAAFSSLNDRTQESLT--SIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIY 249
Cdd:cd18550 153 VLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 16128433 250 IAIGMANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALA 295
Cdd:cd18550 233 LFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLL 278
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
352-553 |
3.03e-26 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 107.42 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQTPFLFSD-TVANNI 430
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 431 ALGCPNATQQEIEHVARLASVHDDIlrlpqGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQ 510
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128433 511 ILHNLRQWGQ--GRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGN 553
Cdd:cd03299 168 LREELKKIRKefGVTVLHVTHDFEeAWALADKVAIMLNGKLIQVGK 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
300-552 |
3.11e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 112.86 E-value: 3.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 300 IVERGSAA---------YSRirAMLA-----EAPVVNDGSEPVPEGRgelDVNIHqftYPQ---------TDHPALENVN 356
Cdd:COG4172 235 IVEQGPTAelfaapqhpYTR--KLLAaeprgDPRPVPPDAPPLLEAR---DLKVW---FPIkrglfrrtvGHVKAVDGVS 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 357 FALKPGQMLGICGPTGSGKSTL----LSLIQrhfdvSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPF-------LF 422
Cdd:COG4172 307 LTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGLsrrALRPLRRRMQVVFQDPFgslsprmTV 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 SDTVANNIALGCPNATQQEIEhvARLAsvhdDILRlpqgydtEVG-ERGVM------LSGGQKQRISIARALLVNAEILI 495
Cdd:COG4172 382 GQIIAEGLRVHGPGLSAAERR--ARVA----EALE-------EVGlDPAARhrypheFSGGQRQRIAIARALILEPKLLV 448
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128433 496 LDDALSAVDGRTEHQILHNLRQWgQGRT----VIISaHRLS---ALteASEIIVMQHGHIAQRG 552
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDL-QREHglayLFIS-HDLAvvrAL--AHRVMVMKDGKVVEQG 508
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
350-546 |
3.48e-26 |
|
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: 108.41 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfHDipltklqldswrSRLAVVSQTPFLFSDTVANN 429
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-HS------------GRISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 430 IALGCpNATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEH 509
Cdd:cd03291 118 IIFGV-SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128433 510 QILHN-LRQWGQGRTVIISAHRLSALTEASEIIVMQHG 546
Cdd:cd03291 197 EIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
335-552 |
3.68e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.18 E-value: 3.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 335 LDVNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAV 414
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 415 VSQTP---FLFSdTVANNIALGCPNatqQEIEHVARLASVHDDILRLP-QGYDTEVGERgvmLSGGQKQRISIARALLVN 490
Cdd:PRK13635 86 VFQNPdnqFVGA-TVQDDVAFGLEN---IGVPREEMVERVDQALRQVGmEDFLNREPHR---LSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128433 491 AEILILDDALSAVDGRTEHQILHNLRQWG--QGRTVIISAHRLSALTEASEIIVMQHGHIAQRG 552
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQADRVIVMNKGEILEEG 222
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
348-555 |
4.58e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.34 E-value: 4.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVA 427
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 NNIALgcPNATQQEIEHVARLAsvhDDILRLpqGYDTEVGERGVM-LSGGQKQRISIARALLVNAEILILDDALSAVD-- 504
Cdd:PRK10247 99 DNLIF--PWQIRNQQPDPAIFL---DDLERF--ALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDes 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 505 -GRTEHQILHNLRQwGQGRTVIISAHRLSALTEASEIIVMQ-HGHIAQRGNHD 555
Cdd:PRK10247 172 nKHNVNEIIHRYVR-EQNIAVLWVTHDKDEINHADKVITLQpHAGEMQEARYE 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
348-548 |
5.34e-26 |
|
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: 106.07 E-value: 5.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT--KLQLDSWRSRLAVVSQTPFLFSD- 424
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKVGMVFQQFNLFPHl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 TVANNIALGcP----NATQQEIEHVAR--LASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDD 498
Cdd:cd03262 92 TVLENITLA-PikvkGMSKAEAEERALelLEKV---------GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16128433 499 ALSAVDGRTEHQILHNLRQWGQ-GRTVIISAHRLS-ALTEASEIIVMQHGHI 548
Cdd:cd03262 162 PTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGfAREVADRVIFMDDGRI 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
352-552 |
5.62e-26 |
|
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: 105.33 E-value: 5.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLI--QRHFDVSEGDIRFHDIPLTKlqlDSWRSRLAVVSQTPFLFsdtvann 429
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILH------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 430 ialgcPNATQQE-IEHVARLasvhddilrlpqgydtevgeRGvmLSGGQKQRISIARALLVNAEILILDDALSAVDGRTE 508
Cdd:cd03213 95 -----PTLTVREtLMFAAKL--------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128433 509 HQILHNLRQWGQ-GRTVIISAHRLSALTEAS--EIIVMQHGHIAQRG 552
Cdd:cd03213 148 LQVMSLLRRLADtGRTIICSIHQPSSEIFELfdKLLLLSQGRVIYFG 194
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
21-311 |
6.82e-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: 6.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 21 AVALLVIIAMLQLVPPKVVGIVVD-GVTEQHftTGQILMWIATMVLIAVVVYL---LRYVWrVLLFGAsyQLAVELREDY 96
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDqGFAAGN--TALLNRAFLLLLAVALVLALasaLRFYL-VSWLGE--RVVADLRKAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 97 YRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTQiSWQLTLFSLLPMPVMAIMIK 176
Cdd:cd18575 76 FAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFIT-SPKLTLLVLLVIPLVVLPII 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 177 RNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRvaRIDAR-FDPTIYIAIGMA 255
Cdd:cd18575 155 LFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALR--RIRARaLLTALVIFLVFG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 256 nllAIGGGSWM----VVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18575 233 ---AIVFVLWLgahdVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
349-555 |
8.72e-26 |
|
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: 106.23 E-value: 8.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 349 HPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TVA 427
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHmTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 NNIAL-----GCPnatQQEIEHVAR--LASVHDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:cd03295 94 ENIALvpkllKWP---KEKIRERADelLALVGLDPAEFADRYPHE-------LSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 501 SAVDGRTEHQILHNLRQWGQ--GRTVIISAHRL-SALTEASEIIVMQHGHIAQRGNHD 555
Cdd:cd03295 164 GALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPD 221
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
343-559 |
1.34e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.86 E-value: 1.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 343 TYPQTDHP--ALENVNFALKPGQMLGICGPTGSGKSTLLSLI---QRhfdVSEGDIRFHDIPLTKL---QLDSWRSRLAV 414
Cdd:COG1135 10 TFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInllER---PTSGSVLVDGVDLTALserELRAARRKIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 415 VSQTPFLF-SDTVANNIAL-----GCPNAtqqEIEH-VARLasvhddiLRLpqgydteVG--ERGVM----LSGGQKQRI 481
Cdd:COG1135 87 IFQHFNLLsSRTVAENVALpleiaGVPKA---EIRKrVAEL-------LEL-------VGlsDKADAypsqLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 482 SIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTE-ASEIIVMQHGHIAQRGN-HDVL 557
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPvLDVF 229
|
..
gi 16128433 558 AQ 559
Cdd:COG1135 230 AN 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
350-547 |
1.35e-25 |
|
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: 112.31 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfHDipltklqldswrSRLAVVSQTPFLFSDTVANN 429
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-HS------------GRISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 430 IALGcpnATQQEIEH--VARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRT 507
Cdd:TIGR01271 507 IIFG---LSYDEYRYtsVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16128433 508 EHQILHN-LRQWGQGRTVIISAHRLSALTEASEIIVMQHGH 547
Cdd:TIGR01271 584 EKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
15-295 |
2.05e-25 |
|
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: 106.41 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 15 WRRYLGAVALLVIIAMLQLVPPKVVGIVVDGVTEQHFTTGQ---ILMWIATMVLIAVVVYLL-RYVWRVllfgaSYQLAV 90
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLtgfILLYLGLILIQALSVFLFiRLAGKI-----EMGVSY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 91 ELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVvfaaGE----GVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLL 166
Cdd:cd18540 76 DLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRL----GEiiswGLVDLVWGITYMIGILIVMLI-LNWKLALIVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 167 PMPVMAI--------MIKRNGDALHERFKLAqAAFSslndrtqESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVA 238
Cdd:cd18540 151 VVPVLAVvsiyfqkkILKAYRKVRKINSRIT-GAFN-------EGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAA 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 239 RIDARFDPTIYIAIGMANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALA 295
Cdd:cd18540 223 RLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLA 279
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
348-553 |
2.16e-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: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklQLDSWRSRLAVVSQTPFLFSD-TV 426
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVNTVFQNYALFPHlTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALGC------PNATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:cd03300 90 FENIAFGLrlkklpKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 501 SAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGN 553
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
348-552 |
3.75e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 106.77 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLI---QRHfdvSEGDIRFHDIPLTkLQLDSWRSRLAVVSQTPFLFSD 424
Cdd:COG1118 14 SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaglETP---DSGRIVLNGRDLF-TNLPPRERRVGFVFQHYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 -TVANNIA--LGCPNATQQEIEHVAR--LASVHDDIL--RLP-QgydtevgergvmLSGGQKQRISIARALLVNAEILIL 496
Cdd:COG1118 90 mTVAENIAfgLRVRPPSKAEIRARVEelLELVQLEGLadRYPsQ------------LSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 497 DDALSAVDG--RTEhqilhnLRQW------GQGRTVIISAH-RLSALTEASEIIVMQHGHIAQRG 552
Cdd:COG1118 158 DEPFGALDAkvRKE------LRRWlrrlhdELGGTTVFVTHdQEEALELADRVVVMNQGRIEQVG 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
351-553 |
3.03e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.82 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT--KLQLDSWRSRLAVVSQTP--FLFSDTV 426
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALGCPN--ATQQEIEHVARLASvhdDILRLPqgYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVD 504
Cdd:PRK13637 102 EKDIAFGPINlgLSEEEIENRVKRAM---NIVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16128433 505 GRTEHQILHNLRQWGQ--GRTVIISAHRLSALTE-ASEIIVMQHGHIAQRGN 553
Cdd:PRK13637 177 PKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
348-552 |
3.93e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 101.22 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT--KLQLDSWRSRLAVVSQTPFLFSD- 424
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRRKVGMVFQQFNLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 TVANNIALGcP----NATQQEIEHVAR--LASVH--DDILRLPQgydtevgergvMLSGGQKQRISIARALLVNAEILIL 496
Cdd:COG1126 93 TVLENVTLA-PikvkKMSKAEAEERAMelLERVGlaDKADAYPA-----------QLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 497 DDALSAVDGRTEHQIL---HNLRQwgQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:COG1126 161 DEPTSALDPELVGEVLdvmRDLAK--EGMTMVVVTHEMGfAREVADRVVFMDGGRIVEEG 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
352-543 |
5.12e-24 |
|
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: 100.02 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdswRSRLAVVSQTP--FLFSDTVANN 429
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER---RKSIGYVMQDVdyQLFTDSVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 430 IALGCPNA--TQQEIEHVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARALLVNAEILILDDALSAVDGRT 507
Cdd:cd03226 93 LLLGLKELdaGNEQAETVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 16128433 508 EHQILHNLRQ-WGQGRTVIISAHRLSALTEASEIIVM 543
Cdd:cd03226 162 MERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLL 198
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
342-562 |
9.42e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.98 E-value: 9.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYpQTDHP-ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP- 419
Cdd:PRK13648 15 FQY-QSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 --FLFSdTVANNIALGCPNATQQEIEHVARLASVHDDILRLPQGyDTEVGErgvmLSGGQKQRISIARALLVNAEILILD 497
Cdd:PRK13648 94 nqFVGS-IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERA-DYEPNA----LSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 498 DALSAVDGRTEHQILHNLRQWGQGRTV-IIS-AHRLSALTEASEIIVMQHGHIAQRGN-HDVLAQQSG 562
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSEHNItIISiTHDLSEAMEADHVIVMNKGTVYKEGTpTEIFDHAEE 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
348-552 |
1.18e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 102.46 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklQLDSWRSRLAVVSQTPFLF-SDTV 426
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT--DLPPKDRNIAMVFQSYALYpHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALGCPNA--TQQEIEH-VARLAsvhdDILRLpqgydTEVGERGV-MLSGGQKQRISIARALLVNAEILILD----- 497
Cdd:COG3839 93 YENIAFPLKLRkvPKAEIDRrVREAA----ELLGL-----EDLLDRKPkQLSGGQRQRVALGRALVREPKVFLLDeplsn 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 498 -DALSAVDGRTE----HQILhnlrqwgqGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:COG3839 164 lDAKLRVEMRAEikrlHRRL--------GTTTIYVTHDQVeAMTLADRIAVMNDGRIQQVG 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
351-552 |
1.86e-23 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 98.42 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGqMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQ--------TPFLF 422
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQefgvypnfTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 SDTVAnnIALGCPNATQ-QEIEHVarLASVHddilrLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:cd03264 93 LDYIA--WLKGIPSKEVkARVDEV--LELVN-----LGDRAKKKIGS----LSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16128433 502 AVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-552 |
3.10e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 105.25 E-value: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 6 QLSWYFRREWRRYLGAVALLVIIamlqlvppkvvgIVVDGVTEQhFTTGQIL---MWIATMVLIAVVVYLLRYVWRVLLF 82
Cdd:PTZ00243 945 SVPWSTYVAYLRFCGGLHAAGFV------------LATFAVTEL-VTVSSGVwlsMWSTRSFKLSAATYLYVYLGIVLLG 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 83 GASYQL------------AVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLV-MGCAVL 149
Cdd:PTZ00243 1012 TFSVPLrfflsyeamrrgSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFsICSSIL 1091
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 150 IMMSTQiswQLTLFSLLPMPVM--AIMIKRNGdALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDR--QSALFAA 225
Cdd:PTZ00243 1092 VTSASQ---PFVLVALVPCGYLyyRLMQFYNS-ANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLvmQEALRRL 1167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 226 DAEDTGK--KNMRVARIDARFDPTIYIAIGMANLLAIGGGSWMVVQGSLTLGQL--TSFMMYLGLMIWPMLALAWM---F 298
Cdd:PTZ00243 1168 DVVYSCSylENVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATSQEIGLVSLslTMAMQTTATLNWLVRQVATVeadM 1247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 299 NIVER------------------GSAAYSRIRAMLAEA-------PVVNDGSEPVPEGRGELDVNIHQFTYPQTDHPALE 353
Cdd:PTZ00243 1248 NSVERllyytdevphedmpeldeEVDALERRTGMAADVtgtvviePASPTSAAPHPVQAGSLVFEGVQMRYREGLPLVLR 1327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 354 NVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIAlg 433
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-- 1405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 434 cP--NATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILIL-DDALSAVDGRTEHQ 510
Cdd:PTZ00243 1406 -PflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQ 1484
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 16128433 511 ILHNLRQWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRG 552
Cdd:PTZ00243 1485 IQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMG 1526
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
348-557 |
3.50e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 98.63 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT--KLQLDSWRSRLAVVSQTPFLFSDT 425
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 426 VA-NNIALGcP----NATQQEIEHVAR--LASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDD 498
Cdd:PRK09493 93 TAlENVMFG-PlrvrGASKEEAEKQARelLAKV---------GLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 499 ALSAVDGRTEHQILHNLRQWG-QGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGNHDVL 557
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
356-557 |
3.60e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 98.29 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 356 NFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldswrsrlaVVSQTPF--LFSD-------TV 426
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL----------PPAERPVsmLFQEnnlfphlTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALGC-----PNATQQE-IEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:COG3840 89 AQNIGLGLrpglkLTAEQRAqVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 501 SAVDGRTEHQILHNLRQWG--QGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGNHDVL 557
Cdd:COG3840 158 SALDPALRQEMLDLVDELCreRGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAAL 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
348-552 |
4.68e-23 |
|
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: 97.33 E-value: 4.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqlDSWRSRLAVVSQTPFLFSD-TV 426
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMVFQNYALYPHmTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALGCPNATQQEIEHVARLASVHDdILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDDALSAVDGR 506
Cdd:cd03301 90 YDNIAFGLKLRKVPKDEIDERVREVAE-LLQIEHLLDRKPKQ----LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128433 507 TEHQILHNLR--QWGQGRTVIISAH-RLSALTEASEIIVMQHGHIAQRG 552
Cdd:cd03301 165 LRVQMRAELKrlQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
351-559 |
1.45e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 97.60 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLA-VVSQTPflfsdtvanN 429
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY-GDYKYRCKHIrMIFQDP---------N 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 430 IALGcPNATQQEI-EHVARLASVHDDILRLPQGYDT--EVGERG-------VMLSGGQKQRISIARALLVNAEILILDDA 499
Cdd:COG4167 98 TSLN-PRLNIGQIlEEPLRLNTDLTAEEREERIFATlrLVGLLPehanfypHMLSSGQKQRVALARALILQPKIIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 500 LSAVDGRTEHQILhNLR---QWGQGRTVIISAHRLSALTEAS-EIIVMQHGHIAQRGN-HDVLAQ 559
Cdd:COG4167 177 LAALDMSVRSQII-NLMlelQEKLGISYIYVSQHLGIVKHISdKVLVMHQGEVVEYGKtAEVFAN 240
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
350-553 |
1.48e-22 |
|
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: 97.71 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRS-RLAVVSQTPFLFSD- 424
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRkKISMVFQSFALLPHr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 TVANNIALG------CPNATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLVNAEILILDD 498
Cdd:cd03294 118 TVLENVAFGlevqgvPRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 499 ALSAVDG--RTEHQILHNLRQWGQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGN 553
Cdd:cd03294 187 AFSALDPliRREMQDELLRLQAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGT 244
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
356-552 |
2.79e-22 |
|
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: 95.44 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 356 NFALK-----PGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL----TKLQLDSWRSRLAVVSQTPFLFSD-T 425
Cdd:cd03297 12 DFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 426 VANNIALGCPNATQQEIEHVAR--LASVHDDilrlpqgydtEVGERGVM-LSGGQKQRISIARALLVNAEILILDDALSA 502
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVDelLDLLGLD----------HLLNRYPAqLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 503 VDGRTEHQILHNLRQWGQ--GRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSeAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
55-311 |
3.20e-22 |
|
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: 97.16 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 55 QILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEG 134
Cdd:cd18577 45 DVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 135 VLTLVDSLVMGCAVLIM-MSTqiSWQLTLFSLLPMPVMAIMIKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAF 213
Cdd:cd18577 125 LGLLIQSLSTFIAGFIIaFIY--SWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 214 GLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIGGGSWMVVQGSLTLGQ-LTSFM------MYLGL 286
Cdd:cd18577 203 GGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDvLTVFFavligaFSLGQ 282
|
250 260
....*....|....*....|....*
gi 16128433 287 MIWPMLALAwmfniveRGSAAYSRI 311
Cdd:cd18577 283 IAPNLQAFA-------KARAAAAKI 300
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
348-555 |
3.31e-22 |
|
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: 95.87 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdswRSR-LAVVSQTPFLFSD-T 425
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERnVGFVFQHYALFRHmT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 426 VANNIALGCPNATQQEIEHVARLASVHDDILRLPQ------GYDTEvgergvmLSGGQKQRISIARALLVNAEILILDDA 499
Cdd:cd03296 91 VFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQldwladRYPAQ-------LSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128433 500 LSAVDGrtehQILHNLRQWGQ------GRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGNHD 555
Cdd:cd03296 164 FGALDA----KVRKELRRWLRrlhdelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPD 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
352-529 |
3.87e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 95.42 E-value: 3.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLI---QRHFDVSEGDIRFHDIPLTKLQldsWRSRLAVVSQTPFLFSD-TVA 427
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKPDQ---FQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 NNIALGCPNATQQEIEHVARlaSVHDDILRLPQGYDTEVGERGVM-LSGGQKQRISIARALLVNAEILILDDALSAVDGR 506
Cdd:cd03234 100 ETLTYTAILRLPRKSSDAIR--KKRVEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180
....*....|....*....|....
gi 16128433 507 TEHQILHNLRQWGQ-GRTVIISAH 529
Cdd:cd03234 178 TALNLVSTLSQLARrNRIVILTIH 201
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
25-283 |
5.65e-22 |
|
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: 96.55 E-value: 5.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 25 LVIIAMLQLVPPKVVGIVVDGVTEQHFTTGQILM-WIATMVLIAVVVYLLRYVW---RVLLFG-ASYQLAVELREDYYRQ 99
Cdd:cd18780 5 LLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALrALNQAVLILLGVVLIGSIAtflRSWLFTlAGERVVARLRKRLFSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 100 LSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLLPMPVMAIMIKRNG 179
Cdd:cd18780 85 IIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFT-TSWKLTLVMLSVVPPLSIGAVIYG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 180 DALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLA 259
Cdd:cd18780 164 KYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLV 243
|
250 260
....*....|....*....|....
gi 16128433 260 IGGGSWMVVQGSLTLGQLTSFMMY 283
Cdd:cd18780 244 LWYGGRLVIDGELTTGLLTSFLLY 267
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
348-559 |
6.17e-22 |
|
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: 95.05 E-value: 6.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPFLFSD 424
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLsekELYELRRRIGMLFQGGALFDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 -TVANNIALG---CPNATQQEIEHVARLAsvhddiLRLpqgydteVGERGVM------LSGGQKQRISIARALLVNAEIL 494
Cdd:COG1127 97 lTVFENVAFPlreHTDLSEAEIRELVLEK------LEL-------VGLPGAAdkmpseLSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128433 495 ILD------DALSAvdGRTEHQILhNLRQwGQGRTVIISAHRL-SALTEASEIIVMQHGHIAQRGNHDVLAQ 559
Cdd:COG1127 164 LYDeptaglDPITS--AVIDELIR-ELRD-ELGLTSVVVTHDLdSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
351-548 |
6.23e-22 |
|
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: 94.81 E-value: 6.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAVVS--QTPFLFSD-TVA 427
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRtfQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 NNIALGCPNAT----------QQEIEHVARLASVHdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILD 497
Cdd:cd03219 94 ENVMVAAQARTgsglllararREEREARERAEELL-ERVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 498 DALSAVDGRTEHQILHNLRQW-GQGRTVIISAHRLSALTEASE-IIVMQHGHI 548
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELrERGITVLLVEHDMDVVMSLADrVTVLDQGRV 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
349-552 |
9.51e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.01 E-value: 9.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 349 HPALENVNFALKPGQMLGICGPTGSGKST----LLSLIQrhfdvSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPFL 421
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLnrrQLLPVRHRIQVVFQDPNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 FSD---TVANNIALGCP------NATQQEIEHVARLASVhddilrlpqGYDTEVGER-GVMLSGGQKQRISIARALLVNA 491
Cdd:PRK15134 374 SLNprlNVLQIIEEGLRvhqptlSAAQREQQVIAVMEEV---------GLDPETRHRyPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128433 492 EILILDDALSAVDGRTEHQILHNLRQWGQGRTV--IISAHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
348-552 |
1.10e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 96.94 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklQLDSWRSRLAVVSQTPFLFSD-TV 426
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNTVFQSYALFPHmTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALG-----CPNAtqqEIEhvARLAsvhdDILRLPQgyDTEVGERGV-MLSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:PRK09452 104 FENVAFGlrmqkTPAA---EIT--PRVM----EALRMVQ--LEEFAQRKPhQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 501 SAVDGRTEHQILHNLRQWGQ--GRTVIISAH-RLSALTEASEIIVMQHGHIAQRG 552
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
352-552 |
1.75e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.31 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLqldSWRSR-LAVVSQTPFLFSD-TVANN 429
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---HARDRkVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 430 IALGC--------PNA-------TQQ-EIEHVARLASvhddilRLPQgydtevgergvMLSGGQKQRISIARALLVNAEI 493
Cdd:PRK10851 95 IAFGLtvlprrerPNAaaikakvTQLlEMVQLAHLAD------RYPA-----------QLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 494 LILDDALSAVDGrtehQILHNLRQWGQG-------RTVIISAHRLSALTEASEIIVMQHGHIAQRG 552
Cdd:PRK10851 158 LLLDEPFGALDA----QVRKELRRWLRQlheelkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
348-553 |
4.75e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 93.69 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQTP--FL 421
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYirpvRKRIGMVFQFPesQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 FSDTVANNIALGcPNATQQEIEHVARLAsvHDDILRLpqGYdtevgERGVM------LSGGQKQRISIARALLVNAEILI 495
Cdd:PRK13646 99 FEDTVEREIIFG-PKNFKMNLDEVKNYA--HRLLMDL--GF-----SRDVMsqspfqMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 496 LDDALSAVDGRTEHQILHNLR--QWGQGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRGN 553
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKslQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTS 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
352-552 |
6.16e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.53 E-value: 6.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklQLDSWR--SRLAVVSQTPFL-FSDTVAN 428
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA--DWSPAElaRRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 429 NIALG------CPNATQQEIEHVarLASVhdDILRLPQGYDTEvgergvmLSGGQKQRISIARAL--LVNAE----ILIL 496
Cdd:PRK13548 96 VVAMGraphglSRAEDDALVAAA--LAQV--DLAHLAGRDYPQ-------LSGGEQQRVQLARVLaqLWEPDgpprWLLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 497 DDALSAVDGRTEHQILHNLRQ--WGQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQlaHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADG 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
350-559 |
6.18e-21 |
|
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: 91.73 E-value: 6.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSR--LAVVSQTPFLFSD-TV 426
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARagIGYVPEGRRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALGCPNATQQEIEhvARLASVHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDDA---LSAV 503
Cdd:cd03224 93 EENLLLGAYARRRAKRK--ARLERVYELFPRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPsegLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 504 DGRTEHQILHNLRQwgQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGNHDVLAQ 559
Cdd:cd03224 167 IVEEIFEAIRELRD--EGVTILLVEQNARfALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
337-552 |
8.05e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.83 E-value: 8.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 337 VNIHqFTYPQtDHPALENVNFALKPGQMLGICGPTGSGKSTLLsliqRHFD----VSEGDIRFHDIPLT--KLQLDSWRS 410
Cdd:PRK13639 5 RDLK-YSYPD-GTEALKGINFKAEKGEMVALLGPNGAGKSTLF----LHFNgilkPTSGEVLIKGEPIKydKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 411 RLAVVSQTP--FLFSDTVANNIALGCPNA--TQQEIEHvarlaSVHDDILRLP-QGYDTEVGERgvmLSGGQKQRISIAR 485
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEK-----RVKEALKAVGmEGFENKPPHH---LSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 486 ALLVNAEILILDDALSAVDGRTEHQI---LHNLRQwgQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQImklLYDLNK--EGITIIISTHDVDlVPVYADKVYVMSDGKIIKEG 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
356-561 |
1.10e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.18 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 356 NFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSRLAVVSQTPFLFSD-TVANNIALGC 434
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 435 -P----NATQQE-IEHVARLASVHDDILRLPqgydtevGErgvmLSGGQKQRISIARALLVNAEILILDDALSAVDGRTE 508
Cdd:PRK10771 97 nPglklNAAQREkLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 509 HQILHNLRQWGQGR--TVIISAHRLS-ALTEASEIIVMQHGHIAQRGNHDVLAQQS 561
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1-529 |
1.42e-20 |
|
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: 95.25 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 1 MRLFAQLswyFRREWRRYLGAVALLVIIAMLQLVppkVVGIVVDGVTEqhftTGQILMWIATMVLIAVVVYLLRYVWRVL 80
Cdd:COG4615 1 MNLLRLL---LRESRWLLLLALLLGLLSGLANAG---LIALINQALNA----TGAALARLLLLFAGLLVLLLLSRLASQL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 81 LFGASYQLAV-ELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAgEGVLTLVDSLVMGCAVLIMMSTqISWQ 159
Cdd:COG4615 71 LLTRLGQHAVaRLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAF-VRLPELLQSVALVLGCLAYLAW-LSPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 160 LTLFSLLPMPVMAIMIKRNGDALHERFKLAQAAfsslNDRTQESLTSI-RMIKAFGL-EDRQSALFAADAEDTGKknmRV 237
Cdd:COG4615 149 LFLLTLVLLGLGVAGYRLLVRRARRHLRRAREA----EDRLFKHFRALlEGFKELKLnRRRRRAFFDEDLQPTAE---RY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 238 ARIDARFDPTIYIAIGMANLL---AIGGGSWMVVQ-GSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRIRA 313
Cdd:COG4615 222 RDLRIRADTIFALANNWGNLLffaLIGLILFLLPAlGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 314 ML-----AEAPVVNDGSEPVPEGRGELDVNIHQFTYPQTDHP---ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRH 385
Cdd:COG4615 302 LElalaaAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 386 FDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTvanniaLGCPNATQQEI--EHVARLASvhDDILRLPQGY- 462
Cdd:COG4615 382 YRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEADPARarELLERLEL--DHKVSVEDGRf 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 463 -DTEvgergvmLSGGQKQRISIARALLVNAEILILDdalsavdgrtE--------------HQILHNLRQwgQGRTVIIS 527
Cdd:COG4615 454 sTTD-------LSQGQRKRLALLVALLEDRPILVFD----------EwaadqdpefrrvfyTELLPELKA--RGKTVIAI 514
|
..
gi 16128433 528 AH 529
Cdd:COG4615 515 SH 516
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
342-552 |
1.49e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.17 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIqrhfdvsEGDIRFHDIPLTKLQLDS--------W--RSR 411
Cdd:PRK13640 13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLI-------NGLLLPDDNPNSKITVDGitltaktvWdiREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 412 LAVVSQTP---FLFSdTVANNIALGCPNATQQEIEHVARLASVHDDILRLpQGYDTEVGErgvmLSGGQKQRISIARALL 488
Cdd:PRK13640 86 VGIVFQNPdnqFVGA-TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGML-DYIDSEPAN----LSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 489 VNAEILILDDALSAVDGRTEHQILHNLR--QWGQGRTVIISAHRLSALTEASEIIVMQHGHIAQRG 552
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
338-552 |
1.61e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 92.94 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 338 NIHQfTYPQ--TDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRL 412
Cdd:PRK11153 6 NISK-VFPQggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 413 AVVSQTpF--LFSDTVANNIALgcP----NATQQEIEhvAR---------LASVHDDilrlpqgYDTEvgergvmLSGGQ 477
Cdd:PRK11153 85 GMIFQH-FnlLSSRTVFDNVAL--PlelaGTPKAEIK--ARvtellelvgLSDKADR-------YPAQ-------LSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 478 KQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
350-543 |
2.01e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.70 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTL---LSLIQRHfdvSEGDIRFHDIPLTKLQ-LDSWRSRLAVVSQTPFLFSD- 424
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLmkiLSGVYQP---DSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 TVANNIALGCPNAT-----QQEIEHVAR--LASVHDDIlrLPqgyDTEVGErgvmLSGGQKQRISIARALLVNAEILILD 497
Cdd:COG1129 95 SVAENIFLGREPRRgglidWRAMRRRARelLARLGLDI--DP---DTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 498 ---DALSAVDgrTEH--QILHNLRQwgQGRTVI-ISaHRLSALTE-ASEIIVM 543
Cdd:COG1129 166 eptASLTERE--VERlfRIIRRLKA--QGVAIIyIS-HRLDEVFEiADRVTVL 213
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
16-311 |
2.84e-20 |
|
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: 91.35 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 16 RRYLGAVALL-VIIAMLQLVPPKVVGIVVDGVTEQhfttgQILMWIATMVLIAVVVYLLR----YVWRVLLFGASYQLAV 90
Cdd:cd18570 1 KKLLILILLLsLLITLLGIAGSFFFQILIDDIIPS-----GDINLLNIISIGLILLYLFQsllsYIRSYLLLKLSQKLDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 91 ELREDYYRQLSRQHPEFYLRHRTGDLMARaTNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTQiSWQLTLFSLLPMPV 170
Cdd:cd18570 76 RLILGYFKHLLKLPLSFFETRKTGEIISR-FNDANKIREAISSTTISLFLDLLMVIISGIILFFY-NWKLFLITLLIIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 171 MAIMIKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDpTIYI 250
Cdd:cd18570 154 YILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQS-SIKG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128433 251 AI-GMANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18570 233 LIsLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
348-540 |
3.34e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 90.61 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDV-----SEGDIRFHDIPLTKLQLD--SWRSRLAVVSQTPF 420
Cdd:PRK14243 22 SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 421 LFSDTVANNIALGCP-NATQQE----IEHVARLASVHDDIlrlpqgyDTEVGERGVMLSGGQKQRISIARALLVNAEILI 495
Cdd:PRK14243 102 PFPKSIYDNIAYGARiNGYKGDmdelVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128433 496 LDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEI 540
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDM 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
348-566 |
3.77e-20 |
|
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: 89.87 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPFLFSD 424
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRRRMGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 -TVANNIALgcP-----NATQQEIEHVAR--LASV--HDDILRLPqgydtevGErgvmLSGGQKQRISIARALLVNAEIL 494
Cdd:cd03261 92 lTVFENVAF--PlrehtRLSEEEIREIVLekLEAVglRGAEDLYP-------AE----LSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 495 ILDDALSAVD----GRTEHQILhNLRQwGQGRTVIISAHRL-SALTEASEIIVMQHGHIAQRGN-HDVLAQQSGWYRD 566
Cdd:cd03261 159 LYDEPTAGLDpiasGVIDDLIR-SLKK-ELGLTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTpEELRASDDPLVRQ 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
348-552 |
5.47e-20 |
|
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: 88.43 E-value: 5.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldSWRSRLAVVSQTPFLF----- 422
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGALIEAPGFYpnlta 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 -SDTVANNIALGCPNATQQEIEHVARLASVHDDILRLpqgydtevgergvmLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:cd03268 90 rENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKG--------------FSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 502 AVD--GRTE-HQILHNLRQwgQGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:cd03268 156 GLDpdGIKElRELILSLRD--QGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
348-504 |
6.42e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 89.71 E-value: 6.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDV-----SEGDIRFH-------DIPLTKLqldswRSRLAVV 415
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDgediydpDVDVVEL-----RRRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 416 SQTPFLFSDTVANNIALGcpnatqqeiehvARLASVH-----DDI----LR---LpqgYDtEVGER----GVMLSGGQKQ 479
Cdd:COG1117 98 FQKPNPFPKSIYDNVAYG------------LRLHGIKskselDEIveesLRkaaL---WD-EVKDRlkksALGLSGGQQQ 161
|
170 180
....*....|....*....|....*
gi 16128433 480 RISIARALLVNAEILILDDALSAVD 504
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
343-551 |
6.83e-20 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 88.23 E-value: 6.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 343 TYPQtDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTP 419
Cdd:cd03292 9 TYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKIGVVFQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 FLFSD-TVANNIALGC------PNATQQEIEHVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARALLVNAE 492
Cdd:cd03292 88 RLLPDrNVYENVAFALevtgvpPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 493 ILILDDALSAVDGRTEHQILHNLRQWGQ-GRTVIISAHrlsalteASEII-VMQHGHIAQR 551
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATH-------AKELVdTTRHRVIALE 210
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
22-311 |
6.96e-20 |
|
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: 90.56 E-value: 6.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 22 VALLVIIAMLQ----LVPPKVVGIVVDGVTEQH-FTTGQILMWIATMVLIAVVVYL-----LRYVWRVLLFGASYQLAVE 91
Cdd:cd18554 1 IIITIVIGLVRfgipLLLPLILKYIVDDVIQGSsLTLDEKVYKLFTIIGIMFFIFLilrppVEYYRQYFAQWIANKILYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 92 LREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVvfaaGEGVLTLVDSLVMGCAVLIMMSTQISW---QLTLFSLLPM 168
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQT----KDFITTGLMNIWLDMITIIIAICIMLVlnpKLTFVSLVIF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 169 PVMAIMIKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTI 248
Cdd:cd18554 157 PFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAV 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128433 249 YIAIGMANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18554 237 NTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
336-552 |
8.06e-20 |
|
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: 90.50 E-value: 8.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 336 DVNIHqFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTL-LSLIQ--RHFDVSEGDIRFHDIPLTKLQLDSWRS-- 410
Cdd:COG0444 6 NLKVY-FPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAILGllPPPGITSGEILFDGEDLLKLSEKELRKir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 411 --RLAVVSQTPFLfsdtvanniALgcpNATQQEIEHVARLASVHDDILRlpqgydTEVGERGV----------------- 471
Cdd:COG0444 85 grEIQMIFQDPMT---------SL---NPVMTVGDQIAEPLRIHGGLSK------AEARERAIellervglpdperrldr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 472 ---MLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLR--QWGQGRTVIISAHRLSALTE-ASEIIVMQH 545
Cdd:COG0444 147 yphELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKdlQRELGLAILFITHDLGVVAEiADRVAVMYA 226
|
....*..
gi 16128433 546 GHIAQRG 552
Cdd:COG0444 227 GRIVEEG 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
343-551 |
8.34e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.54 E-value: 8.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 343 TYPQ--TDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrsrlAVVSQT-- 418
Cdd:COG4525 12 RYPGggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-----GVVFQKda 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 419 --PFLfsdTVANNIAL-----GCPNATQQEI-EHVARLASVHDdilrlpqgydteVGERGV-MLSGGQKQRISIARALLV 489
Cdd:COG4525 87 llPWL---NVLDNVAFglrlrGVPKAERRARaEELLALVGLAD------------FARRRIwQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 490 NAEILILDDALSAVDGRTEHQI---LhnLRQWGQ-GRTVIISAHRL-SALTEASEIIVMQH--GHIAQR 551
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMqelL--LDVWQRtGKGVFLITHSVeEALFLATRLVVMSPgpGRIVER 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
351-552 |
1.03e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 90.29 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLS-----LIQRHFDVSEGDIRFHDIPLTKLQLDSW-----------RSRLAV 414
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKKNNHELITNPyskkiknfkelRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 415 VSQTP--FLFSDTVANNIALGcPNATQQEIEHVARLASVHDDILrlpqGYDTEVGERGVM-LSGGQKQRISIARALLVNA 491
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKM----GLDDSYLERSPFgLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 492 EILILDDALSAVDGRTEH---QILHNLRQwgQGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHemmQLILDAKA--NNKTVFVITHTMEHVLEvADEVIVMDKGKILKTG 258
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
343-546 |
1.13e-19 |
|
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: 87.95 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 343 TYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTPFLF 422
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 SD-TVANNIAL-----GCPNatQQEIEHVARLAsvhdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILIL 496
Cdd:cd03263 88 DElTVREHLRFyarlkGLPK--SEIKEEVELLL----RVLGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 497 DDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRL---SALteASEIIVMQHG 546
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMdeaEAL--CDRIAIMSDG 208
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
351-551 |
2.67e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.14 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTL---LSLIQRHFDVsEGDIRFHDIPLTKLQL-DSWRSRLAVVSQTPFLFSD-T 425
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYPHGTY-EGEIIFEGEELQASNIrDTERAGIAIIHQELALVKElS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 426 VANNIALGCpnatqqEIEHVAR-------------LASVHDDIlrlpqGYDTEVGErgvmLSGGQKQRISIARALLVNAE 492
Cdd:PRK13549 99 VLENIFLGN------EITPGGImdydamylraqklLAQLKLDI-----NPATPVGN----LGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128433 493 ILILDD---ALSAVDGRTEHQILHNLRQwgQGRTVIISAHRLSALTEASEII-VMQHG-HIAQR 551
Cdd:PRK13549 164 LLILDEptaSLTESETAVLLDIIRDLKA--HGIACIYISHKLNEVKAISDTIcVIRDGrHIGTR 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
348-549 |
3.84e-19 |
|
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: 84.79 E-value: 3.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLI--QRHFDvsEGDIRFHDIPLTKLQ-LDSWRSRLAVVSQtpflfsd 424
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILsgLYKPD--SGEILVDGKEVSFASpRDARRAGIAMVYQ------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 tvannialgcpnatqqeiehvarlasvhddilrlpqgydtevgergvmLSGGQKQRISIARALLVNAEILILDD---ALS 501
Cdd:cd03216 83 ------------------------------------------------LSVGERQMVEIARALARNARLLILDEptaALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128433 502 AVDGRTEHQILHNLRQwgQGRTVIISAHRLSALTE-ASEIIVMQHGHIA 549
Cdd:cd03216 115 PAEVERLFKVIRRLRA--QGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
352-548 |
4.03e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.96 E-value: 4.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLsliqRHFDV----SEGDIRFHDIPLT----KLQLDSWRSRLAVVSQTP--FL 421
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLM----QHFNAllkpSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQFPeaQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 FSDTVANNIALGCPN--ATQQEIEHVAR--LASVhddilrlpqGYDTEVGERGVM-LSGGQKQRISIARALLVNAEILIL 496
Cdd:PRK13641 99 FENTVLKDVEFGPKNfgFSEDEAKEKALkwLKKV---------GLSEDLISKSPFeLSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128433 497 DDALSAVDGRTEHQILHNLRQWGQ-GRTVIISAHRLSALTE-ASEIIVMQHGHI 548
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
335-548 |
6.06e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.09 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 335 LDVNIHQFTYPQ-TDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLA 413
Cdd:PRK13650 5 IEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 414 VVSQTP---FLFSdTVANNIALGCPNatqQEIEHVARLASVhDDILRLPQGYDTEVGERGvMLSGGQKQRISIARALLVN 490
Cdd:PRK13650 85 MVFQNPdnqFVGA-TVEDDVAFGLEN---KGIPHEEMKERV-NEALELVGMQDFKEREPA-RLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 491 AEILILDDALSAVD--GRTEH-QILHNLRQwGQGRTVIISAHRLSALTEASEIIVMQHGHI 548
Cdd:PRK13650 159 PKIIILDEATSMLDpeGRLELiKTIKGIRD-DYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
335-576 |
6.35e-19 |
|
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: 88.62 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 335 LDVNIHQftypqtDHPALE-NVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL----TKLQLDSWR 409
Cdd:COG4148 3 LEVDFRL------RRGGFTlDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdsaRGIFLPPHR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 410 SRLAVVSQTPFLFSD-TVANNIALGCPNATQQEieHVARLASVHD-----DIL-RLPQGydtevgergvmLSGGQKQRIS 482
Cdd:COG4148 77 RRIGYVFQEARLFPHlSVRGNLLYGRKRAPRAE--RRISFDEVVEllgigHLLdRRPAT-----------LSGGERQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 483 IARALLVNAEILILDDALSAVDGRTEHQILH---NLRQWGQGRTVIISaHrlsALTE----ASEIIVMQHGHIAQRGN-H 554
Cdd:COG4148 144 IGRALLSSPRLLLMDEPLAALDLARKAEILPyleRLRDELDIPILYVS-H---SLDEvarlADHVVLLEQGRVVASGPlA 219
|
250 260
....*....|....*....|..
gi 16128433 555 DVLAQQsgwyrDMYRYQQLEAA 576
Cdd:COG4148 220 EVLSRP-----DLLPLAGGEEA 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
351-552 |
1.03e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 86.61 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT----KLQLDSWRSRLAVVSQTP--FLFSD 424
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKPLRKKVGIVFQFPehQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 TVANNIALGCPN--ATQQEIEHVARlasvhdDILRLpQGYDTEVGERGVM-LSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:PRK13634 102 TVEKDICFGPMNfgVSEEDAKQKAR------EMIEL-VGLPEELLARSPFeLSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 502 AVDGRTEHQIL---HNLRQwGQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:PRK13634 175 GLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQG 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
350-551 |
1.10e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.91 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklqlDSWRSRLAVVSQTPFLFSDTVANN 429
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE----GPGAERGVVFQNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 430 IALGCPNA--TQQEIEHVAR--LASVHDDilrlpqgydtEVGERGV-MLSGGQKQRISIARALLVNAEILILDDALSAVD 504
Cdd:PRK11248 91 VAFGLQLAgvEKMQRLEIAHqmLKKVGLE----------GAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16128433 505 GRTEHQILHNLRQ-W-GQGRTVIISAHRL-SALTEASEIIVMQ--HGHIAQR 551
Cdd:PRK11248 161 AFTREQMQTLLLKlWqETGKQVLLITHDIeEAVFMATELVLLSpgPGRVVER 212
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
350-550 |
1.32e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 86.01 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQ-TPFLFSDT 425
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQdSPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 426 VANNIALGCP-------NATQQE--IEHVARLASVHDDIL-RLPQgydtevgergvMLSGGQKQRISIARALLVNAEILI 495
Cdd:TIGR02769 105 MTVRQIIGEPlrhltslDESEQKarIAELLDMVGLRSEDAdKLPR-----------QLSGGQLQRINIARALAVKPKLIV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 496 LDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTE-ASEIIVMQHGHIAQ 550
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
348-557 |
3.66e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 84.64 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-------------KLQLDSWRSRLAV 414
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 415 VSQTPFLFSD-TVANNI------ALGCPNATQQEiEHVARLASVHDDilrlpqgyDTEVGERGVMLSGGQKQRISIARAL 487
Cdd:PRK10619 97 VFQHFNLWSHmTVLENVmeapiqVLGLSKQEARE-RAVKYLAKVGID--------ERAQGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128433 488 LVNAEILILDDALSAVDGRTEHQILHNLRQWG-QGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGNHDVL 557
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGfARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
351-558 |
4.79e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.46 E-value: 4.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdSWRS-RLAVVSQTPflfsdtvANN 429
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY-SYRSqRIRMIFQDP-------STS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 430 IalgcpNATQqeiehvaRLASVHDDILRLPQGYDTEVGERGV-------------------MLSGGQKQRISIARALLVN 490
Cdd:PRK15112 100 L-----NPRQ-------RISQILDFPLRLNTDLEPEQREKQIietlrqvgllpdhasyyphMLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16128433 491 AEILILDDALSAVDGRTEHQILhNLR---QWGQGRTVIISAHRLSALTEAS-EIIVMQHGHIAQRGN-HDVLA 558
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLI-NLMlelQEKQGISYIYVTQHLGMMKHISdQVLVMHQGEVVERGStADVLA 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
349-559 |
6.21e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.53 E-value: 6.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 349 HPALENVNFALKPGQMLGICGPTGSGKSTL--------------LSLIQRHFDVSEGdirfhdiPLTKlQLDSWRSRLAV 414
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSLlrvlnllemprsgtLNIAGNHFDFSKT-------PSDK-AIRELRRNVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 415 VSQT----PFLfsdTVANNI--------ALGCPNATQQEIEHVARLasvhddilRLpqgydTEVGERGVM-LSGGQKQRI 481
Cdd:PRK11124 87 VFQQynlwPHL---TVQQNLieapcrvlGLSKDQALARAEKLLERL--------RL-----KPYADRFPLhLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 482 SIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ-GRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGNHDVLAQ 559
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEvARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
270-530 |
6.87e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.17 E-value: 6.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 270 GSLTLGQLT----SFMMYLGlmiwpmlALAW-MFNIVE--RGSAAYSRI----RAM--LAEAPVVNDGSEPVPEGRgeld 336
Cdd:COG4178 294 GEITLGGLMqaasAFGQVQG-------ALSWfVDNYQSlaEWRATVDRLagfeEALeaADALPEAASRIETSEDGA---- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 337 VNIHQFT-YPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltklqldswRSRLAVV 415
Cdd:COG4178 363 LALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA-----------GARVLFL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 416 SQTPFLFSDTVANNIALgcPNA----TQQEIEHVARLASVHDDILRLpqgyDTEVgERGVMLSGGQKQRISIARALLVNA 491
Cdd:COG4178 432 PQRPYLPLGTLREALLY--PATaeafSDAELREALEAVGLGHLAERL----DEEA-DWDQVLSLGEQQRLAFARLLLHKP 504
|
250 260 270
....*....|....*....|....*....|....*....
gi 16128433 492 EILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHR 530
Cdd:COG4178 505 DWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
337-547 |
9.71e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.16 E-value: 9.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 337 VNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-----EGDIRF--HDIPLTKLQLDSWR 409
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFfnQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 410 SRLAVVSQTPFLFSDTVANNIALGC------PNATQQEI-EHVARLASVHDDIlrlpqgyDTEVGERGVMLSGGQKQRIS 482
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVkivgwrPKLEIDDIvESALKDADLWDEI-------KHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 483 IARALLVNAEILILDDALSAVDG----RTEHqILHNLRQWGQgRTVIISAHRLSALTEASEIIVMQHGH 547
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPiasmKVES-LIQSLRLRSE-LTMVIVSHNLHQVSRLSDFTAFFKGN 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
351-548 |
1.05e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 84.40 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPF--L---- 421
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDPYasLnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 -FSDTVA-----NNIAlgcpnaTQQEIEHVAR--LASVhddilrlpqGYDTEVGER-GVMLSGGQKQRISIARALLVNAE 492
Cdd:COG4608 113 tVGDIIAeplriHGLA------SKAERRERVAelLELV---------GLRPEHADRyPHEFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 493 ILILDDALSAVDGRTEHQILhNLRQWGQ---GRTVIISAHRLSALTEAS-EIIVMQHGHI 548
Cdd:COG4608 178 LIVCDEPVSALDVSIQAQVL-NLLEDLQdelGLTYLFISHDLSVVRHISdRVAVMYLGKI 236
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
354-552 |
1.14e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.08 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 354 NVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI-----RFHDIPLTKlqldswRSrLAVVSQTPFLFSD-TVA 427
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekRMNDVPPAE------RG-VGMVFQSYALYPHlSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 NNIALGCPNA------TQQEIEHVArlasvhdDILRLPQGYDtevgERGVMLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:PRK11000 94 ENMSFGLKLAgakkeeINQRVNQVA-------EVLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 502 AVDG------RTEHQILHnlRQWgqGRTVIISAH-RLSALTEASEIIVMQHGHIAQRG 552
Cdd:PRK11000 163 NLDAalrvqmRIEISRLH--KRL--GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
16-295 |
1.17e-17 |
|
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: 83.80 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 16 RRYLGAVALLVIIAMLQLVPPKVVGIVVDGVTEQHfTTGQILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELRED 95
Cdd:cd18782 2 RALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQ-DLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 96 YYRQLSRQHPEFYLRHRTGDLMARaTNDVDRV-VFAAGEGVLTLVDSLVMGCAVLIMMStqISWQLTLFSLLPMPVMAIM 174
Cdd:cd18782 81 IIDHLLRLPLGFFDKRPVGELSTR-ISELDTIrGFLTGTALTTLLDVLFSVIYIAVLFS--YSPLLTLVVLATVPLQLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 175 IKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGM 254
Cdd:cd18782 158 TFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 16128433 255 ANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALA 295
Cdd:cd18782 238 SSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLS 278
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
346-553 |
1.38e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.21 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 346 QTDHPALENVNFALKPGQMLGICGPTGSGKSTllslIQRHFDV----SEGDIRFHDIPlTKLQLDSW--RSRLAVVSQTP 419
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKST----IAKHMNAllipSEGKVYVDGLD-TSDEENLWdiRNKAGMVFQNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 --FLFSDTVANNIALGCPNATQQEIEHVARLasvhDDILRLPQGYDTEVGERGvMLSGGQKQRISIARALLVNAEILILD 497
Cdd:PRK13633 95 dnQIVATIVEEDVAFGPENLGIPPEEIRERV----DESLKKVGMYEYRRHAPH-LLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 498 DALSAVD--GRTEhqILHNLRQWGQ--GRTVIISAHRLSALTEASEIIVMQHGHIAQRGN 553
Cdd:PRK13633 170 EPTAMLDpsGRRE--VVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
352-552 |
1.45e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.49 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI------PLTKLQ--LDSWRSRLAVVSQTPFLFS 423
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItidtarSLSQQKglIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 424 D-TVANNIALG---CPNATQQEIEHVAR--LASVHddilrlPQGYDTEVGERgvmLSGGQKQRISIARALLVNAEILILD 497
Cdd:PRK11264 99 HrTVLENIIEGpviVKGEPKEEATARARelLAKVG------LAGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 498 DALSAVDGRTEHQILHNLRQWGQ-GRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQG 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
342-560 |
1.46e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.24 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYpQTDHP----ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT----KLQLDSWRSRLA 413
Cdd:PRK13643 9 YTY-QPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskQKEIKPVRKKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 414 VVSQTP--FLFSDTVANNIALGCPN--ATQQEIEHVA--RLASVhddilrlpqGYDTEVGERGVM-LSGGQKQRISIARA 486
Cdd:PRK13643 88 VVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAaeKLEMV---------GLADEFWEKSPFeLSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 487 LLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ-GRTVIISAHRLSALTE-ASEIIVMQHGHIAQRGNHDVLAQQ 560
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
340-552 |
1.47e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.31 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 340 HQFTypqTDHPALENVNFALKPGQMLGICGPTGSGKSTLLsliqRHFD----VSEGDIRFHDIPLTKLQLDSWRSRLAVV 415
Cdd:PRK13652 11 YSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLF----RHFNgilkPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 416 SQTP--FLFSDTVANNIALGCPN------ATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARAL 487
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFGPINlgldeeTVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 488 LVNAEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTEASE-IIVMQHGHIAQRG 552
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEMADyIYVMDKGRIVAYG 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
349-559 |
1.71e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 81.98 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 349 HPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQ--------------RHFD----VSEGDIRfhdipltklqldSWRS 410
Cdd:COG4161 15 HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNlletpdsgqlniagHQFDfsqkPSEKAIR------------LLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 411 RLAVVSQT----PFLfsdTVANNI------ALGCPN--ATQQEIEHVARLasvhddilRLpqgydTEVGERGVM-LSGGQ 477
Cdd:COG4161 83 KVGMVFQQynlwPHL---TVMENLieapckVLGLSKeqAREKAMKLLARL--------RL-----TDKADRFPLhLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 478 KQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ-GRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGNHD 555
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEfARKVASQVVYMEKGRIIEQGDAS 226
|
....
gi 16128433 556 VLAQ 559
Cdd:COG4161 227 HFTQ 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
342-552 |
2.77e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDhPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI---PLTKLQldSWRSRLAVVSQT 418
Cdd:PRK13644 9 YSYPDGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgDFSKLQ--GIRKLVGIVFQN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 419 P--FLFSDTVANNIALGCPNATQQEIEHVARLasvhddilrlpqgyDTEVGERGV---------MLSGGQKQRISIARAL 487
Cdd:PRK13644 86 PetQFVGRTVEEDLAFGPENLCLPPIEIRKRV--------------DRALAEIGLekyrhrspkTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 488 LVNAEILILDDALSAVDGRTEHQILHNLRQWGQ-GRTVIISAHRLSALTEASEIIVMQHGHIAQRG 552
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEG 217
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
21-311 |
3.35e-17 |
|
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: 82.21 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 21 AVALLVIIAMLQLVPPKVVGIVVDGVTEQ---HFTTGQILMWIATMVLIAVVVY--LLRYVWRVLLFGASYQLAVELRED 95
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNVISRSlkeTNGDFIEDLKKPALKLLGLYLLqsLLTFAYISLLSVVGERVAARLRND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 96 YYRQLSRQHPEFYLRHRTGDLMARATNDVD--RVVF--AAGEGVLTLVdsLVMGCAV-LIMMSTqiswQLTLFSLLPMPV 170
Cdd:cd18574 81 LFSSLLRQDIAFFDTHRTGELVNRLTADVQefKSSFkqCVSQGLRSVT--QTVGCVVsLYLISP----KLTLLLLVIVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 171 MAIMIKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARidarfdptiYI 250
Cdd:cd18574 155 VVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGL---------GI 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 251 AI--GMANlLAIGG--------GSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18574 226 GIfqGLSN-LALNGivlgvlyyGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
362-552 |
3.87e-17 |
|
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: 80.23 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 362 GQMLGICGPTGSGKSTLLSLIQrHFDVSE-GDIRFHDIPLTklQLDSWRSRLAVVSQTPFLFSD-TVANNIALG-CPN-- 436
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIA-GFETPQsGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVGLGlSPGlk 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 437 ---ATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLVNAEILILDDALSAVDG--RTEHQI 511
Cdd:cd03298 101 ltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPalRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16128433 512 LHNLRQWGQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:cd03298 170 LVLDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
351-540 |
4.02e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.36 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-----EGDIRF--HDIPLTKLQLDSWRSRLAVVSQTPFLFS 423
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYngHNIYSPRTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 424 DTVANNIALGC-------PNATQQEIEHVARLASVHDDIL-RLpqgYDTEVGergvmLSGGQKQRISIARALLVNAEILI 495
Cdd:PRK14239 100 MSIYENVVYGLrlkgikdKQVLDEAVEKSLKGASIWDEVKdRL---HDSALG-----LSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128433 496 LDDALSAVD----GRTEhQILHNLRqwgQGRTVIISAHrlsALTEASEI 540
Cdd:PRK14239 172 LDEPTSALDpisaGKIE-ETLLGLK---DDYTMLLVTR---SMQQASRI 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
348-552 |
4.17e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.59 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL--TKLQLDSWRSRLAVVSQTP--FLFS 423
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 424 DTVANNIALGCPNATQQEIEHVARLasvhDDILRL--PQGYDTEVGErgvMLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEITRRV----DEALTLvdAQHFRHQPIQ---CLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 502 AVDGRTEHQILHNLRQW-GQGRTVIISAHRLSALTEASE-IIVMQHGHIAQRG 552
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDaVYVLRQGQILTHG 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
335-548 |
5.88e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 81.29 E-value: 5.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 335 LDVNIHQFTY-PQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLA 413
Cdd:PRK13642 5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 414 VVSQTP--FLFSDTVANNIALGCPNATQQEIEHVARLasvhDDILRLPQGYDTEVGERGvMLSGGQKQRISIARALLVNA 491
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRV----DEALLAVNMLDFKTREPA-RLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 492 EILILDDALSAVD--GRTE-HQILHNLRQwGQGRTVIISAHRLSALTEASEIIVMQHGHI 548
Cdd:PRK13642 160 EIIILDESTSMLDptGRQEiMRVIHEIKE-KYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
351-558 |
5.90e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.67 E-value: 5.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLsliqRHFDV----SEGDIRF---HDIPLTKLQLDSW--------------- 408
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFI----EHLNAlllpDTGTIEWifkDEKNKKKTKEKEKvleklviqktrfkki 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 409 ------RSRLAVVSQtpF----LFSDTVANNIALGcPNATQQEIEHVARLASVHDDILRLPQGYdteVGERGVMLSGGQK 478
Cdd:PRK13651 98 kkikeiRRRVGVVFQ--FaeyqLFEQTIEKDIIFG-PVSMGVSKEEAKKRAAKYIELVGLDESY---LQRSPFELSGGQK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 479 QRISIARALLVNAEILILDDALSAVD--GRTEH-QILHNLRQwgQGRTVIISAHRL-SALTEASEIIVMQHGHIAQRGN- 553
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDpqGVKEIlEIFDNLNK--QGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGDt 249
|
....*
gi 16128433 554 HDVLA 558
Cdd:PRK13651 250 YDILS 254
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
349-559 |
6.12e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 80.28 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 349 HPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAV--VSQTPFLFSD-T 425
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIgyLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 426 VANNIAL-----GCPNATQQE-IEHVarLASVHDDILRLPQGYDtevgergvmLSGGQKQRISIARALLVNAEILILDDA 499
Cdd:cd03218 92 VEENILAvleirGLSKKEREEkLEEL--LEEFHITHLRKSKASS---------LSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 500 LSAVDGRTEH---QILHNLRQWGQGrtVIISAHRLSaltEASEII----VMQHGHIAQRGNHDVLAQ 559
Cdd:cd03218 161 FAGVDPIAVQdiqKIIKILKDRGIG--VLITDHNVR---ETLSITdrayIIYEGKVLAEGTPEEIAA 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
348-562 |
7.00e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.19 E-value: 7.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTPFLFSD-TV 426
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLDLEfTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALGCP--NATQQEIEHVarLASVHDdILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDDALSAVD 504
Cdd:PRK13536 132 RENLLVFGRyfGMSTREIEAV--IPSLLE-FARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 505 GRTEHQILHNLRQ-WGQGRTVIISAHrlsaLTEASE-----IIVMQHGH-IAQRGNHDVLAQQSG 562
Cdd:PRK13536 205 PHARHLIWERLRSlLARGKTILLTTH----FMEEAErlcdrLCVLEAGRkIAEGRPHALIDEHIG 265
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
352-552 |
7.80e-17 |
|
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: 79.82 E-value: 7.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswrsRLAVVSQTPFLFSDTVANNIA 431
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD----RMVVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 432 LGC----PNATQQEIEHVARlasVHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDDALSAVDGRT 507
Cdd:TIGR01184 77 LAVdrvlPDLSKSERRAIVE---EHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128433 508 EHQILHNLRQ-WGQGR-TVIISAHRL-SALTEASEIIVMQHGHIAQRG 552
Cdd:TIGR01184 150 RGNLQEELMQiWEEHRvTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
21-283 |
8.82e-17 |
|
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: 81.20 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 21 AVALLVIIAMLQLVPPKVVGIVVDG-VTEQHFTtgQILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYYRQ 99
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGiVIEKSQD--KFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 100 LSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMsTQISWQLTLFSLLPMPVMAIMIKRNG 179
Cdd:cd18784 79 IVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFM-FKLSWQLSLVTLIGLPLIAIVSKVYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 180 DALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFD-PTIYIAIGMANLL 258
Cdd:cd18784 158 DYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVwSNELTELALTVST 237
|
250 260
....*....|....*....|....*
gi 16128433 259 AIGGGSwMVVQGSLTLGQLTSFMMY 283
Cdd:cd18784 238 LYYGGH-LVITGQISGGNLISFILY 261
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
349-587 |
1.08e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.44 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 349 HPALENVNFALKPGQMLGICGPTGSGKSTLLsliqRHFdvsEGDIRFHDIPLTKLQL-------------DSWRSRlavv 415
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLL----RHL---SGLITGDKSAGSHIELlgrtvqregrlarDIRKSR---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 416 SQTPFLFSD-------TVANNI---ALGC------------PNATQQEIEHVARLASVHddilrlpqgydtEVGERGVML 473
Cdd:PRK09984 86 ANTGYIFQQfnlvnrlSVLENVligALGStpfwrtcfswftREQKQRALQALTRVGMVH------------FAHQRVSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 474 SGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLS-ALTEASEIIVMQHGHIAQ 550
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFY 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 16128433 551 RGnhdvlaqqSGWYRDMYRYQQLEAALDDAPENREEA 587
Cdd:PRK09984 234 DG--------SSQQFDNERFDHLYRSINRVEENAKAA 262
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
342-558 |
1.39e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.16 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDHpALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP-- 419
Cdd:PRK13647 12 FRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPdd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 FLFSDTVANNIALGCPNA--TQQEIEHVAR--LASVHDDILRLPQGYDtevgergvmLSGGQKQRISIARALLVNAEILI 495
Cdd:PRK13647 91 QVFSSTVWDDVAFGPVNMglDKDEVERRVEeaLKAVRMWDFRDKPPYH---------LSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 496 LDDALSAVDGR---TEHQILHNLRQwgQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGNHDVLA 558
Cdd:PRK13647 162 LDEPMAYLDPRgqeTLMEILDRLHN--QGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
351-557 |
2.35e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 80.52 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRsrlAVVSQTPFLFSD------ 424
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWR---AVRSDIQMIFQDplasln 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 ---TVANNIA----LGCPNATQQEI-----EHVARLASVHDDILRLPQGYdtevgergvmlSGGQKQRISIARALLVNAE 492
Cdd:PRK15079 113 prmTIGEIIAeplrTYHPKLSRQEVkdrvkAMMLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 493 ILILDDALSAVDGRTEHQILhNLRQWGQ---GRTVIISAHRLSALTEASE-IIVMQHGHIAQRGNHDVL 557
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVV-NLLQQLQremGLSLIFIAHDLAVVKHISDrVLVMYLGHAVELGTYDEV 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
348-497 |
2.45e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.03 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltklqldswRSRLAVVSQTPFLFSD-TV 426
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALGCP--NATQQEIEHV-----------ARLASVHDDI------------------LRLPQG-YDTEVGErgvmLS 474
Cdd:COG0488 79 LDTVLDGDAelRALEAELEELeaklaepdedlERLAELQEEFealggweaearaeeilsgLGFPEEdLDRPVSE----LS 154
|
170 180
....*....|....*....|...
gi 16128433 475 GGQKQRISIARALLVNAEILILD 497
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLD 177
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
349-552 |
2.74e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.16 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 349 HPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK-LQldswRSRLAVVSQT-------PF 420
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQaLQ----KNLVAYVPQSeevdwsfPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 421 LFSDTV-----ANNIALGCPNATQQEIEHVArLASVHDDILRLPQgydteVGErgvmLSGGQKQRISIARALLVNAEILI 495
Cdd:PRK15056 96 LVEDVVmmgryGHMGWLRRAKKRDRQIVTAA-LARVDMVEFRHRQ-----IGE----LSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 496 LDDALSAVDGRTEHQILHNLRQW-GQGRTVIISAHRLSALTEASEIIVMQHGHIAQRG 552
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
351-553 |
3.00e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 79.67 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD--IP--LTKL-QLDSWRSRLAVVSQTP--FLFS 423
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaIPanLKKIkEVKRLRKEIGLVFQFPeyQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 424 DTVANNIALGCPNATQQEIEHVARLASVHDdILRLPQGYdteVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAV 503
Cdd:PRK13645 106 ETIEKDIAFGPVNLGENKQEAYKKVPELLK-LVQLPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 504 DGRTEHQILHNLRQWG--QGRTVIISAHRL-SALTEASEIIVMQHGHIAQRGN 553
Cdd:PRK13645 182 DPKGEEDFINLFERLNkeYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
343-548 |
4.17e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.69 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 343 TYPQTDHP--ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVS 416
Cdd:PRK10535 13 SYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 417 QTPFLFSD-TVANNIALgcpNATQQEIEHVARLASVHDDILRLpqGYDTEVGERGVMLSGGQKQRISIARALLVNAEILI 495
Cdd:PRK10535 93 QRYHLLSHlTAAQNVEV---PAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 496 LDDALSAVDGRTEHQ---ILHNLRQwgQGRTVIISAHRLSALTEASEIIVMQHGHI 548
Cdd:PRK10535 168 ADEPTGALDSHSGEEvmaILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
347-530 |
5.00e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.04 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 347 TDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHdipltklqldsWRSRLAVVSQTPFLfsdtv 426
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP-----------EGEDLLFLPQRPYL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 annialgcPNATqqeiehvarLAsvhdDILRLPqgYDTEvgergvmLSGGQKQRISIARALLVNAEILILDDALSAVDGR 506
Cdd:cd03223 76 --------PLGT---------LR----EQLIYP--WDDV-------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180
....*....|....*....|....
gi 16128433 507 TEHQILHNLRQwgQGRTVIISAHR 530
Cdd:cd03223 126 SEDRLYQLLKE--LGITVISVGHR 147
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
351-546 |
5.15e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklqLDSwrSRLAV------VSQTPFLFSD 424
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR---IRS--PRDAIalgigmVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 -TVANNIALGCPNATQQEIehvaRLASVHDDILRLPQGY------DTEVGErgvmLSGGQKQRISIARALLVNAEILILD 497
Cdd:COG3845 95 lTVAENIVLGLEPTKGGRL----DRKAARARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128433 498 DAlSAV--DGRTEH--QILHNLRQwgQGRTVIISAHRLSALTEAS-EIIVMQHG 546
Cdd:COG3845 167 EP-TAVltPQEADElfEILRRLAA--EGKSIIFITHKLREVMAIAdRVTVLRRG 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
348-543 |
5.25e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.50 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltklqldswRSRLAVVSQ---TPFLFSD 424
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVPDSLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 TVANNIALGcpnaTQQEIEHVARL-----ASVHDDILRLpqGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDA 499
Cdd:NF040873 73 TVRDLVAMG----RWARRGLWRRLtrddrAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128433 500 LSAVDGRTEHQILHNLRQW-GQGRTVIISAHRLSALTEASEIIVM 543
Cdd:NF040873 147 TTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
351-555 |
5.64e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.08 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ----LDSWRSRLAVVSQTPFLFSD-T 425
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKKIAMVFQSFALMPHmT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 426 VANNIALGCPNA--TQQEIEHVARLASVHDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLVNAEILILDDALSAV 503
Cdd:PRK10070 123 VLDNTAFGMELAgiNAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 504 DG--RTEHQILHNLRQWGQGRTVIISAHRL-SALTEASEIIVMQHGHIAQRGNHD 555
Cdd:PRK10070 196 DPliRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPD 250
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
351-552 |
6.63e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 79.24 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTL---LSLIQRHfdvSEGDIRFHDIPLTKLQLDSW---RSRLAVVSQTPF---- 420
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIETP---TGGELYYQGQDLLKADPEAQkllRQKIQIVFQNPYgsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 421 -------LFSDTVANNIALGCPNATQQEIEHVAR--LASVHDDilRLPQgydtevgergvMLSGGQKQRISIARALLVNA 491
Cdd:PRK11308 107 prkkvgqILEEPLLINTSLSAAERREKALAMMAKvgLRPEHYD--RYPH-----------MFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 492 EILILDDALSAVDGRTEHQILhNL-----RQWGQGrTVIISaHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVL-NLmmdlqQELGLS-YVFIS-HDLSVVEHiADEVMVMYLGRCVEKG 237
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
338-548 |
8.59e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.43 E-value: 8.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 338 NIHQFTYPQT--DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRL-AV 414
Cdd:COG1101 6 NLSKTFNPGTvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAKYiGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 415 VSQTPFL---FSDTVANNIALgcpnA-------------TQQEIEHV-ARLASVHddiLRLPQGYDTEVGergvMLSGGQ 477
Cdd:COG1101 85 VFQDPMMgtaPSMTIEENLAL----AyrrgkrrglrrglTKKRRELFrELLATLG---LGLENRLDTKVG----LLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 478 KQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQwgqgrtvIISAHRLS----------ALTEASEIIVMQHGH 547
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEK-------IVEENNLTtlmvthnmeqALDYGNRLIMMHEGR 226
|
.
gi 16128433 548 I 548
Cdd:COG1101 227 I 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
352-540 |
1.08e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklqLDSWRSRLAVVSQ----TPFLfsdTVA 427
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYLGHrnamKPAL---TVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 NNIAL--GCPNATQQEIEhvARLASVH-DDILRLPQGYdtevgergvmLSGGQKQRISIARALLVNAEILILDDALSAVD 504
Cdd:PRK13539 92 ENLEFwaAFLGGEELDIA--AALEAVGlAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 16128433 505 GRTEHQILhNL--RQWGQGRTVIISAHRLSALTEASEI 540
Cdd:PRK13539 160 AAAVALFA-ELirAHLAQGGIVIAATHIPLGLPGAREL 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
346-550 |
1.17e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.78 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 346 QTDhpALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL----QLDSWRSRLAVVSQTPFL 421
Cdd:PRK11629 21 QTD--VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQFHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 FSD-TVANNIA--LGCPNATQQEIEHVAR--LASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLVNAEILIL 496
Cdd:PRK11629 99 LPDfTALENVAmpLLIGKKKPAEINSRALemLAAV---------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 497 DDALSAVDGRTEHQILHNLRQWG--QGRTVIISAHRLSALTEASEIIVMQHGHIAQ 550
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNrlQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
350-552 |
1.44e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.48 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT----KLQLDSWRSRLAVVSQTP--FLFS 423
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNKDIKQIRKKVGLVFQFPesQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 424 DTVANNIALGCPN--ATQQEIEHVAR--LASVhddilrlpqGYDTEVGERGVM-LSGGQKQRISIARALLVNAEILILDD 498
Cdd:PRK13649 101 ETVLKDVAFGPQNfgVSQEEAEALARekLALV---------GISESLFEKNPFeLSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 499 ALSAVD--GRTE-HQILHNLRQwgQGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:PRK13649 172 PTAGLDpkGRKElMTLFKKLHQ--SGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
352-560 |
1.60e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 76.26 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRH--FDVSEGDIRFHDIPLTKLQLDSwRSRLAV------------VSQ 417
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDE-RARAGIflafqypveipgVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 418 TPFLfsDTVANNIALGCPNATQ--QEIEHVARLASVHDDILrlpqgydtevgERGVM--LSGGQKQRISIARALLVNAEI 493
Cdd:COG0396 95 SNFL--RTALNARRGEELSAREflKLLKEKMKELGLDEDFL-----------DRYVNegFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 494 LILD--------DALSAV-DGrtehqiLHNLRqwGQGRTVIISAH--RLSALTEASEIIVMQHGHIAQRGNHDvLAQQ 560
Cdd:COG0396 162 AILDetdsgldiDALRIVaEG------VNKLR--SPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE-LALE 230
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
92-298 |
2.04e-15 |
|
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: 76.99 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 92 LREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMsTQISWQLTLFSLLPMPVM 171
Cdd:cd18590 71 LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFM-LSLSWQLTLLTLIEMPLT 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 172 AIMIKRNgDALHERFKLA-QAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGK-KNMR--VARIDARFDPT 247
Cdd:cd18590 150 AIAQKVY-NTYHQKLSQAvQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNlKDRRdtVRAVYLLVRRV 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128433 248 IYIAIGMANLLAiggGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMF 298
Cdd:cd18590 229 LQLGVQVLMLYC---GRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIY 276
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
335-558 |
2.87e-15 |
|
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: 75.40 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 335 LDV-NIHQFtYPQTdhPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRL- 412
Cdd:COG0410 4 LEVeNLHAG-YGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHR-IARLg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 413 -AVVSQTPFLFSD-TVANNIALGCPNATQQEiEHVARLASVHDdilRLPqgydtEVGER----GVMLSGGQKQRISIARA 486
Cdd:COG0410 80 iGYVPEGRRIFPSlTVEENLLLGAYARRDRA-EVRADLERVYE---LFP-----RLKERrrqrAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 487 LLVNAEILILDDAlsavdgrTE----------HQILHNLRQwgQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGNHD 555
Cdd:COG0410 151 LMSRPKLLLLDEP-------SLglapliveeiFEIIRRLNR--EGVTILLVEQNARfALEIADRAYVLERGRIVLEGTAA 221
|
...
gi 16128433 556 VLA 558
Cdd:COG0410 222 ELL 224
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
16-311 |
4.31e-15 |
|
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: 76.06 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 16 RRYLGAVALL-VIIAMLQLVPPKVVGIVVDGV-TEQHFTTGQILMwiATMVLIAVVVYLLRYVWRVLLFGASYQLAVELR 93
Cdd:cd18568 1 RKLLAEILLAsLLLQLLGLALPLFTQIILDRVlVHKNISLLNLIL--IGLLIVGIFQILLSAVRQYLLDYFANRIDLSLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 94 EDYYRQLSRQHPEFYLRHRTGDLMARAT-NDVDRVvFAAGEGVLTLVDSLvMGCAVLIMMSTqISWQLTLFSLLPMPVMA 172
Cdd:cd18568 79 SDFYKHLLSLPLSFFASRKVGDIITRFQeNQKIRR-FLTRSALTTILDLL-MVFIYLGLMFY-YNLQLTLIVLAFIPLYV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 173 IM-------IKRNgdaLHERFKLAQAAFSSLndrtQESLTSIRMIKAFGLED----RQSALFAadaeDTGKKNMRVARID 241
Cdd:cd18568 156 LLtllsspkLKRN---SREIFQANAEQQSFL----VEALTGIATIKALAAERpirwRWENKFA----KALNTRFRGQKLS 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 242 ARFDPTIYIAIGMANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18568 225 IVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
352-552 |
4.49e-15 |
|
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: 74.10 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRH--FDVSEGDIRFHDIPLTKLQLDSwRSRLAV--VSQTPFlfsdtva 427
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLGIflAFQYPP------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 nnialgcpnatqqEIEHVaRLAsvhdDILRlpqgydtEVGERgvmLSGGQKQRISIARALLVNAEILILDDALSAVD--- 504
Cdd:cd03217 88 -------------EIPGV-KNA----DFLR-------YVNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDida 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128433 505 GRTEHQILHNLRqwGQGRTVIISAH--RLSALTEASEIIVMQHGHIAQRG 552
Cdd:cd03217 140 LRLVAEVINKLR--EEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
348-562 |
4.90e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.00 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAVVSQTPFLFSD-TV 426
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVPQFDNLDPDfTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIAL-----GCPNATQQEIehVARLAsvhdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:PRK13537 98 RENLLVfgryfGLSAAAARAL--VPPLL----EFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128433 502 AVDGRTEHQILHNLRQ-WGQGRTVIISAHRL-SALTEASEIIVMQHGH-IAQRGNHDVLAQQSG 562
Cdd:PRK13537 168 GLDPQARHLMWERLRSlLARGKTILLTTHFMeEAERLCDRLCVIEEGRkIAEGAPHALIESEIG 231
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
338-559 |
1.09e-14 |
|
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: 73.71 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 338 NIHQFtYPQTdhPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSR--LAVV 415
Cdd:TIGR03410 5 NLNVY-YGQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP-PHERARagIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 416 SQTPFLFSD-TVANNIALG---CPNATQQEIEHVARLASVHDDILrlpqgydtevGERGVMLSGGQKQRISIARALLVNA 491
Cdd:TIGR03410 81 PQGREIFPRlTVEENLLTGlaaLPRRSRKIPDEIYELFPVLKEML----------GRRGGDLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 492 EILILDDAlsavdgrTE----------HQILHNLRQWGqGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGNHDVLAQ 559
Cdd:TIGR03410 151 KLLLLDEP-------TEgiqpsiikdiGRVIRRLRAEG-GMAILLVEQYLDfARELADRYYVMERGRVVASGAGDELDE 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
352-548 |
1.09e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.34 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRS-RLAVvsQTPFLFSDTVANni 430
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfRRDI--QMVFQDSISAVN-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 431 algcPNATQQEI-----EHV------ARLASVhDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDA 499
Cdd:PRK10419 104 ----PRKTVREIireplRHLlsldkaERLARA-SEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128433 500 LSAVDGRTEHQI---LHNLRQWGQGRTVIISaHRLSaLTE--ASEIIVMQHGHI 548
Cdd:PRK10419 179 VSNLDLVLQAGVirlLKKLQQQFGTACLFIT-HDLR-LVErfCQRVMVMDNGQI 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
345-559 |
1.10e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.96 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 345 PQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfhdipltklqldsWRSR----LAVvsQTPF 420
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE-------------VNGRvsalLEL--GAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 421 LFSDTVANNIALGCP--NATQQEIEhvARLASVHD--DIlrlpQGY-DTEVGergvMLSGGQKQRISIARALLVNAEILI 495
Cdd:COG1134 100 HPELTGRENIYLNGRllGLSRKEID--EKFDEIVEfaEL----GDFiDQPVK----TYSSGMRARLAFAVATAVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 496 LDDALSAVDGR-TE--HQILHNLRQwgQGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRGN-HDVLAQ 559
Cdd:COG1134 170 VDEVLAVGDAAfQKkcLARIRELRE--SGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDpEEVIAA 236
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
351-555 |
1.57e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.99 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF--HDIP-LTKLQLDSWRSRLAVVSQTPFLFSD-TV 426
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsgHDITrLKNREVPFLRRQIGMIFQDHHLLMDrTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIA--LGCPNATQQEIEHvaRLASVHDDILRLPQGYDTEvgergVMLSGGQKQRISIARALLVNAEILILDDALSAVD 504
Cdd:PRK10908 97 YDNVAipLIIAGASGDDIRR--RVSAALDKVGLLDKAKNFP-----IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 505 GRTEHQILHNLRQWGQ-GRTVIISAHRLSALTEAS-EIIVMQHGHIAqrGNHD 555
Cdd:PRK10908 170 DALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSyRMLTLSDGHLH--GGVG 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
351-552 |
1.89e-14 |
|
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: 72.79 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAVVSQTPFLFSD-TVANN 429
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA-RRRLGFVSDSTGLYDRlTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 430 IAL-----GC-PNATQQEIEHVArlasvhdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDDALSAV 503
Cdd:cd03266 99 LEYfaglyGLkGDELTARLEELA-------DRLGMEELLDRRVGG----FSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 504 D---GRTEHQILHNLRQwgQGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:cd03266 168 DvmaTRALREFIRQLRA--LGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
351-551 |
3.43e-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: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTL---LSLIQRHFDVsEGDIRFHDIPLTKLQL-DSWRSRLAVVSQTPFLFSD-T 425
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVYPHGTW-DGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVPElS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 426 VANNIALGcpnatqQEIEHVARLASVHDDILR---------LPQGYDT-EVGERGvmlsGGQKQRISIARALLVNAEILI 495
Cdd:TIGR02633 95 VAENIFLG------NEITLPGGRMAYNAMYLRaknllrelqLDADNVTrPVGDYG----GGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 496 LDDALSAVDgRTEHQILHNLRQWGQGRTV--IISAHRLSALTEASEII-VMQHG-HIAQR 551
Cdd:TIGR02633 165 LDEPSSSLT-EKETEILLDIIRDLKAHGVacVYISHKLNEVKAVCDTIcVIRDGqHVATK 223
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
55-319 |
4.47e-14 |
|
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: 73.25 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 55 QILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYYRQLSRQHPEFYLR--HRTGDLMARATNDVDRVVFAAG 132
Cdd:cd18578 50 EANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDpeNSTGALTSRLSTDASDVRGLVG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 133 EGVLTLVDSLVM-GCAVLIMMStqISWQLTLFSLLPMPVMAIMIKRNGdALHERF-KLAQAAFSSLNDRTQESLTSIRMI 210
Cdd:cd18578 130 DRLGLILQAIVTlVAGLIIAFV--YGWKLALVGLATVPLLLLAGYLRM-RLLSGFeEKNKKAYEESSKIASEAVSNIRTV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 211 KAFGLEDRQSALFAADAEDTGKKNMRVARIDArfdptiyIAIGMANLLAIGG-------GSWMVVQGSLTLGQ-LTSFM- 281
Cdd:cd18578 207 ASLTLEDYFLEKYEEALEEPLKKGLRRALISG-------LGFGLSQSLTFFAyalafwyGGRLVANGEYTFEQfFIVFMa 279
|
250 260 270
....*....|....*....|....*....|....*...
gi 16128433 282 MYLGLMIWpMLALAWMFNIVeRGSAAYSRIRAMLAEAP 319
Cdd:cd18578 280 LIFGAQSA-GQAFSFAPDIA-KAKAAAARIFRLLDRKP 315
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
352-548 |
6.78e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.02 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswrsrlavvsqTPFLFSD------- 424
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-----------TRLMFQDarllpwk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 TVANNIALGC-----PNATQQeiehvarLASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDA 499
Cdd:PRK11247 97 KVIDNVGLGLkgqwrDAALQA-------LAAV---------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 500 LSAVDG--RTEHQILHNlRQWGQ-GRTVIISAHRLS-ALTEASEIIVMQHGHI 548
Cdd:PRK11247 161 LGALDAltRIEMQDLIE-SLWQQhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
350-559 |
6.80e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 6.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL------QLDswrsrLAVVSQTPFLFS 423
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLtpakahQLG-----IYLVPQEPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 424 D-TVANNIALGCPN--ATQQEIEHVARLASVHDDiLRLPQGyDTEVGERgvmlsggqkQRISIARALLVNAEILILDD-- 498
Cdd:PRK15439 100 NlSVKENILFGLPKrqASMQKMKQLLAALGCQLD-LDSSAG-SLEVADR---------QIVEILRGLMRDSRILILDEpt 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 499 -ALSAVDGRTEHQILHNLRQWGQGrTVIISaHRLSALTE-ASEIIVMQHGHIAQRG-----NHDVLAQ 559
Cdd:PRK15439 169 aSLTPAETERLFSRIRELLAQGVG-IVFIS-HKLPEIRQlADRISVMRDGTIALSGktadlSTDDIIQ 234
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
16-283 |
7.03e-14 |
|
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: 72.49 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 16 RRYLGAVALL-VIIAMLQLVPPKVVGIVVDGVTEQHftTGQILMWIAT----MVLIAVVVYLLRYvWRVLLFGA--SYQL 88
Cdd:cd18567 1 KRALLQILLLsLALELFALASPLYLQLVIDEVIVSG--DRDLLTVLAIgfglLLLLQALLSALRS-WLVLYLSTslNLQW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 89 AVELredyYRQLSRQHPEFYLRHRTGDLMAR--ATNDVDRVVfaaGEGVLTLVDSLVMGCAVLIMMSTqISWQLTLFSLL 166
Cdd:cd18567 78 TSNL----FRHLLRLPLSYFEKRHLGDIVSRfgSLDEIQQTL---TTGFVEALLDGLMAILTLVMMFL-YSPKLALIVLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 167 PMpVMAIMIKRngdALHERFKLAQAAFSSLNDRTQ----ESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDA 242
Cdd:cd18567 150 AV-ALYALLRL---ALYPPLRRATEEQIVASAKEQshflETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQI 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 16128433 243 RFDpTIYIAI-GMANLLAIGGGSWMVVQGSLTLGQLTSFMMY 283
Cdd:cd18567 226 LFS-AANGLLfGLENILVIYLGALLVLDGEFTVGMLFAFLAY 266
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
338-541 |
8.73e-14 |
|
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: 70.37 E-value: 8.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 338 NIHQFTYPQTD-HPALENVNFALKPGQMLGICGPTGSGKSTLLSLI--QRHFDVS-EGDIRFHDIPLtKLQLDSWRSRLA 413
Cdd:cd03233 8 NISFTTGKGRSkIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanRTEGNVSvEGDIHYNGIPY-KEFAEKYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 414 VVSQTPFLFSD-TVannialgcpnatQQEIEHVARLASvhDDILrlpqgydtevgeRGVmlSGGQKQRISIARALLVNAE 492
Cdd:cd03233 87 YVSEEDVHFPTlTV------------RETLDFALRCKG--NEFV------------RGI--SGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128433 493 ILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISahrlsaLTEASEII 541
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADvlKTTTFVS------LYQASDEI 183
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
328-550 |
1.29e-13 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 70.54 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 328 VPEGRGELDVnihqftypqtdhpaLENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---Q 404
Cdd:COG4181 18 VGTGAGELTI--------------LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 405 LDSWRSR-LAVVSQT-PFLFSDTVANNIAL-----GCPNATQQEIEHVARLASVHddilRL---PQGydtevgergvmLS 474
Cdd:COG4181 84 RARLRARhVGFVFQSfQLLPTLTALENVMLplelaGRRDARARARALLERVGLGH----RLdhyPAQ-----------LS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 475 GGQKQRISIARALLVNAEILILDDALSAVDGRTEHQI---LHNLRQwGQGRTVIISAHRLSALTEASEIIVMQHGHIAQ 550
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIidlLFELNR-ERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
350-497 |
1.47e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 70.16 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD----IPLTKLQ----LDSWRSRLAVVSQtpFL 421
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQASpreiLALRRRTIGYVSQ--FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 FS-------DTVANN-IALGCPNATQQEI--EHVARLasvhddilRLPqgydtevgERgvmL--------SGGQKQRISI 483
Cdd:COG4778 103 RViprvsalDVVAEPlLERGVDREEARARarELLARL--------NLP--------ER---LwdlppatfSGGEQQRVNI 163
|
170
....*....|....
gi 16128433 484 ARALLVNAEILILD 497
Cdd:COG4778 164 ARGFIADPPLLLLD 177
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
16-295 |
1.63e-13 |
|
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: 71.38 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 16 RRYLGAVALL-VIIAMLQLVPPKVVGIVVDGV-TEQHFTTGQILMwiATMVLIAVVVYLLRYVWRVLLFGASYQLAVELR 93
Cdd:cd18588 1 KKLLGEVLLAsLFLQLFALVTPLFFQVIIDKVlVHRSLSTLDVLA--IGLLVVALFEAVLSGLRTYLFSHTTNRIDAELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 94 EDYYRQLSRQHPEFYLRHRTGDLMARAtNDVDRV-VFAAGEGVLTLVDSLVMGCAVLIMMstQISWQLTLFSLLPMPVMA 172
Cdd:cd18588 79 ARLFRHLLRLPLSYFESRQVGDTVARV-RELESIrQFLTGSALTLVLDLVFSVVFLAVMF--YYSPTLTLIVLASLPLYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 173 I-------MIKRNgdaLHERFKLAQAAFSSLNdrtqESLTSIRMIKAFGLEDRqsalFAADAEDTGKKNMRVARIDARFD 245
Cdd:cd18588 156 LlsllvtpILRRR---LEEKFQRGAENQSFLV----ETVTGIETVKSLAVEPQ----FQRRWEELLARYVKASFKTANLS 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 16128433 246 PTIYIAIGMANLLAIGG----GSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALA 295
Cdd:cd18588 225 NLASQIVQLIQKLTTLAilwfGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLV 278
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
348-560 |
1.65e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.06 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqlDSWRSR-LAVVSQTPFLFSD-T 425
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRdICMVFQSYALFPHmS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 426 VANNIALGCPNATQQEIEHVARLasvhDDILRLpqgYDTE-VGERGV-MLSGGQKQRISIARALLVNAEILILDDALSAV 503
Cdd:PRK11432 95 LGENVGYGLKMLGVPKEERKQRV----KEALEL---VDLAgFEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 504 DGRTEHQILHNLRQWgQGRTVIISAHRLSALTEA----SEIIVMQHGHIAQRGNHDVLAQQ 560
Cdd:PRK11432 168 DANLRRSMREKIREL-QQQFNITSLYVTHDQSEAfavsDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
348-552 |
3.06e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 69.73 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqldsWRS-----RLAVVSQTPFLF 422
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT-----TPSrelakRLAILRQENHIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 SD-TVANNIALG-CP----NATQQEIEHVAR------LASVHDDILrlpqgyDTevgergvmLSGGQKQRISIARALLVN 490
Cdd:COG4604 88 SRlTVRELVAFGrFPyskgRLTAEDREIIDEaiayldLEDLADRYL------DE--------LSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 491 AEILILDDALSAVDGRTEHQILHNLRQW--GQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLadELGKTVVIVLHDINfASCYADHIVAMKDGRVVAQG 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
339-559 |
3.25e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.66 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 339 IHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT 418
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 419 PFLFSD-TVANNIALG-CPNATqqeieHVARLASvhDDILRLPQGYD----TEVGERGVM-LSGGQKQRISIARALLVNA 491
Cdd:PRK11231 85 HLTPEGiTVRELVAYGrSPWLS-----LWGRLSA--EDNARVNQAMEqtriNHLADRRLTdLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 492 EILILDDALSAVDgrTEHQI-----LHNLRQwgQGRTVIISAHRLS-ALTEASEIIVMQHGH-IAQRGNHDVLAQ 559
Cdd:PRK11231 158 PVVLLDEPTTYLD--INHQVelmrlMRELNT--QGKTVVTVLHDLNqASRYCDHLVVLANGHvMAQGTPEEVMTP 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
331-555 |
3.60e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 69.69 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 331 GRGELDV-NIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL----TKLQL 405
Cdd:PRK14246 4 GKSAEDVfNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkDIFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 406 DS--WRSRLAVVSQTPFLFSD-TVANNIALGCPNATQQEIEHVARLAsvhDDILRlPQGYDTEVGER----GVMLSGGQK 478
Cdd:PRK14246 84 DAikLRKEVGMVFQQPNPFPHlSIYDNIAYPLKSHGIKEKREIKKIV---EECLR-KVGLWKEVYDRlnspASQLSGGQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 479 QRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASEIIV-MQHGHIAQRGNHD 555
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAfLYNGELVEWGSSN 237
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
352-559 |
3.61e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.39 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLS-LIQRHFDVSE--GDIRFHDIPLTKLQLdswRSRLAVVSQTP-FLFSDTVA 427
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNaLAFRSPKGVKgsGSVLLNGMPIDAKEM---RAISAYVQQDDlFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 NNIA----LGCPNATQQEiEHVARLASVHDDiLRLPQGYDTEVGERGVM--LSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:TIGR00955 118 EHLMfqahLRMPRRVTKK-EKRERVDEVLQA-LGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 502 AVDGRTEHQILHNLRQWGQ-GRTVIISAHRLSA-LTEA-SEIIVMQHGHIAQRGNHDVLAQ 559
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQkGKTIICTIHQPSSeLFELfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-539 |
3.65e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.12 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRS------RLAVVSQTPFLFSDT 425
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDvlefrrRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 426 VANNIALGCPN---ATQQEIEHVA--RLASVHddilrLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:PRK14271 117 IMDNVLAGVRAhklVPRKEFRGVAqaRLTEVG-----LWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 16128433 501 SAVDGRTEHQILHNLRQWGQGRTVIISAHRLSALTEASE 539
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISD 230
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
348-552 |
3.71e-13 |
|
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: 69.10 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH--DIPLTKLQldswrsrlavvsqTPFLFSDT 425
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRgrVSSLLGLG-------------GGFNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 426 VANNIALGCP--NATQQEIEhvarlaSVHDDIL---RLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:cd03220 101 GRENIYLNGRllGLSRKEID------EKIDEIIefsELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 501 SAVDGRTE---HQILHNLRQwgQGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:cd03220 171 AVGDAAFQekcQRRLRELLK--QGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
352-529 |
4.05e-13 |
|
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: 68.29 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTPFLFSD-TVANNI 430
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF-QRDSIARGLLYLGHAPGIKTTlSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 431 ALGCP-NATQQEIEHVAR--LASVHDdilrLPQGYdtevgergvmLSGGQKQRISIARALLVNAEILILDDALSAVDGRT 507
Cdd:cd03231 95 RFWHAdHSDEQVEEALARvgLNGFED----RPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|...
gi 16128433 508 EHQILHNLRQ-WGQGRTVIISAH 529
Cdd:cd03231 161 VARFAEAMAGhCARGGMVVLTTH 183
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
356-552 |
4.55e-13 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 70.91 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 356 NFALK-----PGQ-MLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL----TKLQLDSWRSRLAVVSQTPFLFSD- 424
Cdd:TIGR02142 11 DFSLDadftlPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFPHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 TVANNIALGC----PNATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:TIGR02142 91 SVRGNLRYGMkrarPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 501 SAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAG 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
350-552 |
4.94e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.02 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklQLDSWRSRLAVVSQTPFLFSD-TVAN 428
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPHmTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 429 NIALGCPNATQQEIEHVAR----LASVH--DDILRLPQgydtevgergvMLSGGQKQRISIARALLVNAEILILDDALSA 502
Cdd:PRK11607 111 NIAFGLKQDKLPKAEIASRvnemLGLVHmqEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128433 503 VD----GRTEHQILHNLRQWGqGRTVIISAHRLSALTEASEIIVMQHGHIAQRG 552
Cdd:PRK11607 180 LDkklrDRMQLEVVDILERVG-VTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
348-560 |
5.16e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRH--FDVSEGDIRFHDIPLTKLQLDSwRSRLAV----------- 414
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEE-RAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 415 -VSQTPFLFSDTVANNIALGCPnatqqEIEHVARLaSVHDDILRLpQGYDTEVGERGVM--LSGGQKQRISIARALLVNA 491
Cdd:CHL00131 98 gVSNADFLRLAYNSKRKFQGLP-----ELDPLEFL-EIINEKLKL-VGMDPSFLSRNVNegFSGGEKKRNEILQMALLDS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128433 492 EILILDDALSAVD---GRTEHQILHNLRqwGQGRTVIISAH--RLSALTEASEIIVMQHGHIAQRGNHDvLAQQ 560
Cdd:CHL00131 171 ELAILDETDSGLDidaLKIIAEGINKLM--TSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE-LAKE 241
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
348-557 |
6.00e-13 |
|
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: 68.96 E-value: 6.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLI-QRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVS---QTPFLFS 423
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItGDLPPTYGNDVRLFGERRGGEDVWELRKRIGLVSpalQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 424 DTVANNIALGC-------PNATQQEIEHVARLAsvhdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILIL 496
Cdd:COG1119 95 ETVLDVVLSGFfdsiglyREPTDEQRERARELL----ELLGLAHLADRPFGT----LSQGEQRRVLIARALVKDPELLIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 497 DDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTEA-SEIIVMQHGHIAQRGN-HDVL 557
Cdd:COG1119 167 DEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPkEEVL 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
352-557 |
7.06e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 68.71 E-value: 7.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ-TPFLFSDTVANNI 430
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHRAYLSQqQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 431 ALGCP-NATQQEIEH-VARLASVhddiLRLPQGYDTEVGErgvmLSGGQKQRISIARALL-----VNAE--ILILDDALS 501
Cdd:COG4138 91 ALHQPaGASSEAVEQlLAQLAEA----LGLEDKLSRPLTQ----LSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 502 AVDGRteHQILHN--LRQW-GQGRTVIISAHRLS-ALTEASEIIVMQHGH-IAQRGNHDVL 557
Cdd:COG4138 163 SLDVA--QQAALDrlLRELcQQGITVVMSSHDLNhTLRHADRVWLLKQGKlVASGETAEVM 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
342-573 |
7.37e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.11 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDHpALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL--TKLQLDSWRSRLAVVSQTP 419
Cdd:PRK13636 13 YNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVGMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 --FLFSDTVANNIALGCPNATQQEIEHVARLasvhDDILRlPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILD 497
Cdd:PRK13636 92 dnQLFSASVYQDVSFGAVNLKLPEDEVRKRV----DNALK-RTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 498 DALSAVDGRTEHQILHNLR--QWGQGRTVIISAHRLSALT-EASEIIVMQHGHIAQRGN-HDVLAQqsgwyRDMYRYQQL 573
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVemQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNpKEVFAE-----KEMLRKVNL 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
347-549 |
8.32e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.82 E-value: 8.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 347 TDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ-LDSWRSRLAVVS---QTPFLF 422
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVPedrKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 SD-TVANNIALGCPNA--------TQQEIEHVARLAsvhdDILRL-PQGYDTEVGErgvmLSGGQKQRISIARALLVNAE 492
Cdd:COG1129 343 LDlSIRENITLASLDRlsrgglldRRRERALAEEYI----KRLRIkTPSPEQPVGN----LSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 493 ILILDDALSAVD-G-RTE-HQILHNLRQwgQGRTVI-IS---------AHRlsalteaseIIVMQHGHIA 549
Cdd:COG1129 415 VLILDEPTRGIDvGaKAEiYRLIRELAA--EGKAVIvISselpellglSDR---------ILVMREGRIV 473
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
347-548 |
9.06e-13 |
|
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: 67.07 E-value: 9.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 347 TDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR-LAVVSQTPF---LF 422
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 SD-TVANNIALGcpnatqqeiehvarlasvhddilrlpqgydtevgergVMLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:cd03215 91 LDlSVAENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 502 AVD-GRTE--HQILHNLRQwgQGRTVI-ISahrlSALTE----ASEIIVMQHGHI 548
Cdd:cd03215 134 GVDvGAKAeiYRLIRELAD--AGKAVLlIS----SELDEllglCDRILVMYEGRI 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
340-540 |
9.43e-13 |
|
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: 67.38 E-value: 9.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 340 HQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSRLAVVSQTP 419
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 FLFSD-TVANNIALGCP--NATQQEIEhvARLASVH-DDILRLPQGYdtevgergvmLSGGQKQRISIARALLVNAEILI 495
Cdd:TIGR01189 83 GLKPElSALENLHFWAAihGGAQRTIE--DALAAVGlTGFEDLPAAQ----------LSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128433 496 LDDALSAVDGRTEHQILHNLRQ-WGQGRTVIISAHRLSALTEASEI 540
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQDLGLVEAREL 196
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
348-557 |
1.26e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.87 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ-TPFLFSDTV 426
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQdTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALGcpnatqqEIEHVARLASVHDDILR-----LPQGYDTEVGERGVM-LSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:PRK09536 95 RQVVEMG-------RTPHRSRFDTWTETDRAaveraMERTGVAQFADRPVTsLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128433 501 SAVDgrTEHQI--LHNLRQWGQ-GRTVIISAHRLS-ALTEASEIIVMQHGHIAQRGN-HDVL 557
Cdd:PRK09536 168 ASLD--INHQVrtLELVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPpADVL 227
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
16-299 |
1.29e-12 |
|
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: 68.70 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 16 RRYLGAVALL-VIIAMLQLVPPKVVGIVVDGV-TEQHFTTGQILmwiaTMVLIAVVVY--LLRYVWRVLLFGASYQLAVE 91
Cdd:cd18783 1 KRLFRDVAIAsLILHVLALAPPIFFQIVIDKVlVHQSYSTLYVL----TIGVVIALLFegILGYLRRYLLLVATTRIDAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 92 LREDYYRQLSRQHPEFYLRHRTGDLMaRATNDVDRV-VFAAGEGVLTLVD--SLVMGCAVLIMMSTQISWQLTLFSLLPM 168
Cdd:cd18783 77 LALRTFDRLLSLPIDFFERTPAGVLT-KHMQQIERIrQFLTGQLFGTLLDatSLLVFLPVLFFYSPTLALVVLAFSALIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 169 PVMAIMIKRngdaLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDAR----- 243
Cdd:cd18783 156 LIILAFLPP----FRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWpqtlt 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 244 --FDPTIYIAIgmanllaIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFN 299
Cdd:cd18783 232 gpLEKLMTVGV-------IWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQ 282
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-529 |
1.31e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.02 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-----EGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-T 425
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNlS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 426 VANNIALGCP----NATQQEIEHVARLAsvhddiLRLPQGYDtEVGER----GVMLSGGQKQRISIARALLVNAEILILD 497
Cdd:PRK14247 99 IFENVALGLKlnrlVKSKKELQERVRWA------LEKAQLWD-EVKDRldapAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190
....*....|....*....|....*....|..
gi 16128433 498 DALSAVDGRTEHQILHNLRQWGQGRTVIISAH 529
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
361-533 |
2.12e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.91 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 361 PGQMLGICGPTGSGKSTLLSLI--QRHFDVSEGDIRFHDIPLTKLQLdswrSRLAVVSQTPFLFSDTVANNIALGC---- 434
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALagRIQGNNFTGTILANNRKPTKQIL----KRTGFVTQDDILYPHLTVRETLVFCsllr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 435 -PNA-TQQEIEHVARlaSVHDDiLRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLVNAEILILDDALSAVDGRTEH 509
Cdd:PLN03211 169 lPKSlTKQEKILVAE--SVISE-LGLTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180
....*....|....*....|....*
gi 16128433 510 QILHNLRQWGQ-GRTVIISAHRLSA 533
Cdd:PLN03211 244 RLVLTLGSLAQkGKTIVTSMHQPSS 268
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
352-548 |
2.33e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.14 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQ---RHFDVS-EGDIRFHDIPLTKLQlDSWRSRLAVVSQT----PFL-F 422
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntDGFHIGvEGVITYDGITPEEIK-KHYRGDVVYNAETdvhfPHLtV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 SDTVANNIALGCPNATQQEI---EHVARLASVHDDILRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLVNAEILIL 496
Cdd:TIGR00956 156 GETLDFAARCKTPQNRPDGVsreEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 497 DDALSAVDGRTEHQILHNLRQwgqgRTVIISAHRLSALTEASE--------IIVMQHGHI 548
Cdd:TIGR00956 234 DNATRGLDSATALEFIRALKT----SANILDTTPLVAIYQCSQdayelfdkVIVLYEGYQ 289
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
342-497 |
2.93e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 64.39 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPqtDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltklqldswRSRLAVVSQtpfl 421
Cdd:cd03221 8 KTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYFEQ---- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 422 fsdtvannialgcpnatqqeiehvarlasvhddilrlpqgydtevgergvmLSGGQKQRISIARALLVNAEILILD 497
Cdd:cd03221 71 ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
337-537 |
4.80e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.36 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 337 VNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVS 416
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 417 Q----TPFLfsdTVANNIALGC-PNATQQEIEHVARLASVhDDILRLPQGydtevgergvMLSGGQKQRISIARALLVNA 491
Cdd:PRK13540 81 HrsgiNPYL---TLRENCLYDIhFSPGAVGITELCRLFSL-EHLIDYPCG----------LLSSGQKRQVALLRLWMSKA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128433 492 EILILDDALSAVDGRTEHQILHNLRQW-GQGRTVIISAHRLSALTEA 537
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHrAKGGAVLLTSHQDLPLNKA 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
351-552 |
6.23e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPFLFSD--- 424
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLspgKLQALRRDIQFIFQDPYASLDprq 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 TVANNI-------ALGCPNATQQEI-EHVARLASVHDDILRLPQGYdtevgergvmlSGGQKQRISIARALLVNAEILIL 496
Cdd:PRK10261 419 TVGDSImeplrvhGLLPGKAAAARVaWLLERVGLLPEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 497 DDALSAVDGRTEHQILHNL--RQWGQGRTVIISAHRLSALTEAS-EIIVMQHGHIAQRG 552
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLldLQRDFGIAYLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
350-548 |
6.47e-12 |
|
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: 65.82 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltklqLDSWRSRLAVVSQTPFLFS--DTVA 427
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-------LVPWKRRKKFLRRIGVVFGqkTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 NNIALGCPNATQQEI---------EHVARLAsvhdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDD 498
Cdd:cd03267 108 WDLPVIDSFYLLAAIydlpparfkKRLDELS----ELLDLEELLDTPVRQ----LSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 499 ALSAVDGRTEHQILHNLRQWGQGR--TVIISAHRLSALTE-ASEIIVMQHGHI 548
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
351-548 |
7.51e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 7.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS-WRSRLAVVSQTPFLFSD-TVAN 428
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 429 NIALGCPNATQQEIEHvaRLASVHDDILRLpqgYDTEVGERGVMlSGGQKQRISIARALLVNAEILILDDALSAVDGRTE 508
Cdd:PRK11614 100 NLAMGGFFAERDQFQE--RIKWVYELFPRL---HERRIQRAGTM-SGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16128433 509 HQILHNLRQW-GQGRTV-IISAHRLSALTEASEIIVMQHGHI 548
Cdd:PRK11614 174 QQIFDTIEQLrEQGMTIfLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
348-543 |
9.69e-12 |
|
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: 64.61 E-value: 9.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklqlDSWRSRLAVVSQTPFLFSDTva 427
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYLPEERGLYPKM-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 nnialgcpnATQQEIEHVARLASV-HDDILRLPQGYDTEVG------ERGVMLSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:cd03269 86 ---------KVIDQLVYLAQLKGLkKEEARRRIDEWLERLElseyanKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 16128433 501 SAVD---GRTEHQILHNLRqwGQGRTVIISAHRLSALTEASEIIVM 543
Cdd:cd03269 157 SGLDpvnVELLKDVIRELA--RAGKTVILSTHQMELVEELCDRVLL 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
351-555 |
1.97e-11 |
|
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: 66.75 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQ--RHFDVSEGDIRFH----------DIP-------------LTKLQL 405
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmDQYEPTSGRIIYHvalcekcgyvERPskvgepcpvcggtLEPEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 406 DSW----------RSRLAVVSQTPFLF--SDTVANNIALGCPNATQQEIEHVARLAsvhdDILRLpqgydTEVGERgVM- 472
Cdd:TIGR03269 95 DFWnlsdklrrriRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAV----DLIEM-----VQLSHR-ITh 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 473 ----LSGGQKQRISIARALLVNAEILILDDALSAVDGRTEhQILHNLRQWG---QGRTVIISAHRLSALTEASE-IIVMQ 544
Cdd:TIGR03269 165 iardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA-KLVHNALEEAvkaSGISMVLTSHWPEVIEDLSDkAIWLE 243
|
250
....*....|.
gi 16128433 545 HGHIAQRGNHD 555
Cdd:TIGR03269 244 NGEIKEEGTPD 254
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
19-240 |
2.16e-11 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 64.74 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAMLQLVppkvvGIVVDGVTEQHFTTGQILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYYR 98
Cdd:cd18584 4 LGLLAALLIIAQAWLL-----ARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 99 QLSRQHPEFYLRHRTGDLMARATNDVDRVvfaagEGVLT-----LVDSLVMGCAVLIMMSTQiSWQ---LTLFSLLPMPV 170
Cdd:cd18584 79 RLLALGPALLRRQSSGELATLLTEGVDAL-----DGYFArylpqLVLAAIVPLLILVAVFPL-DWVsalILLVTAPLIPL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 171 MAIMIKRNGDALHERfklAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARI 240
Cdd:cd18584 153 FMILIGKAAQAASRR---QWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKVLRV 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
348-529 |
2.78e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.90 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLavvsqtpfLFsdtva 427
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-QRDEYHQDL--------LY----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 nniaLGCPNATQQE---IEHVARLASVHDDilrlpqgYDTE--------VGERGVM------LSGGQKQRISIARALLVN 490
Cdd:PRK13538 79 ----LGHQPGIKTEltaLENLRFYQRLHGP-------GDDEalwealaqVGLAGFEdvpvrqLSAGQQRRVALARLWLTR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16128433 491 AEILILDDALSAVD----GRTEHQILHNLRqwgQGRTVIISAH 529
Cdd:PRK13538 148 APLWILDEPFTAIDkqgvARLEALLAQHAE---QGGMVILTTH 187
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
351-552 |
2.97e-11 |
|
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: 63.54 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF--HDIplTKlQLDSWRSRLAVVSQtpflfsDTVAN 428
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVagHDV--VR-EPREVRRRIGIVFQ------DLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 429 NIALGCPNatqqeIEHVARLASVHDDILR-----LPQGYD-TEVGERGV-MLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:cd03265 86 DELTGWEN-----LYIHARLYGVPGAERRerideLLDFVGlLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128433 502 AVDGRTEHQILHNLRQW--GQGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEG 214
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
60-283 |
3.18e-11 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 64.41 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 60 IATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLV 139
Cdd:cd18589 39 ITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 140 DSLVMGCAVLIMMSTQiSWQLTLFSLLPMPVMAIMIKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQ 219
Cdd:cd18589 119 WYLARGLFLFIFMLWL-SPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGE 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 220 SALFAADAEDTGKKNMRVARIDARFDPTIYIAiGMA---NLLAIGGGswMVVQGSLTLGQLTSFMMY 283
Cdd:cd18589 198 AQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFS-GLAlkvGILYYGGQ--LVTAGTVSSGDLVTFVLY 261
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
348-548 |
3.92e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 64.36 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW---------RSRLAVvsqt 418
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIgylpeerglYPKMKV---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 419 pflfsdtvannialgcpnatqqeIEHVARLASVHD--------------DILRLPQGYDTEVGErgvmLSGGQKQRISIA 484
Cdd:COG4152 89 -----------------------GEQLVYLARLKGlskaeakrradewlERLGLGDRANKKVEE----LSKGNQQKVQLI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16128433 485 RALLVNAEILILDDALS-----AVDgrTEHQILHNLRQwgQGRTVIISAHRLSaLTE--ASEIIVMQHGHI 548
Cdd:COG4152 142 AALLHDPELLILDEPFSgldpvNVE--LLKDVIRELAA--KGTTVIFSSHQME-LVEelCDRIVIINKGRK 207
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
351-531 |
5.14e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.20 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTL---LSLIQRHFDVsEGDI-------RFHDIPltklqlDSWRSRLAVVSQ--- 417
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLmkvLSGVYPHGSY-EGEIlfdgevcRFKDIR------DSEALGIVIIHQela 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 418 -TPFLfsdTVANNIALGCPNATQ-----QEIEHVAR--LASVhddilRLPQGYDTEVGERGVmlsgGQKQRISIARALLV 489
Cdd:NF040905 89 lIPYL---SIAENIFLGNERAKRgvidwNETNRRARelLAKV-----GLDESPDTLVTDIGV----GKQQLVEIAKALSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128433 490 NAEILILDD---ALSAVDGRTEHQILHNLRQwgQGRTVIISAHRL 531
Cdd:NF040905 157 DVKLLILDEptaALNEEDSAALLDLLLELKA--QGITSIIISHKL 199
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
350-531 |
9.06e-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: 65.42 E-value: 9.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF--HDIpltKLQLDSWRSRLAVVSQTPFLFSD-TV 426
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVggKDI---ETNLDAVRQSLGMCPQHNILFHHlTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 427 ANNIALGCPNATQQEIEHVARLASVHDDilrlpQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGR 506
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180
....*....|....*....|....*
gi 16128433 507 TEHQILHNLRQWGQGRTVIISAHRL 531
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHM 1120
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
343-553 |
9.33e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 63.71 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 343 TYPqTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdswRSR-LAVVSQTPFL 421
Cdd:PRK11650 12 SYD-GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADRdIAMVFQNYAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 FSD-TVANNIALGCPNA------TQQEIEHVARlasvhddILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEIL 494
Cdd:PRK11650 88 YPHmSVRENMAYGLKIRgmpkaeIEERVAEAAR-------ILELEPLLDRKPRE----LSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 495 ILDDALSAVDG------RTEHQILHnlRQWGQgrTVIISAH-RLSALTEASEIIVMQHGHIAQRGN 553
Cdd:PRK11650 157 LFDEPLSNLDAklrvqmRLEIQRLH--RRLKT--TSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
19-311 |
9.50e-11 |
|
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: 63.07 E-value: 9.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 19 LGAVALLVIIAMLQLVPPKVVGIVVDGvteqhfTTGQILMWIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDYYR 98
Cdd:cd18561 4 LGLLITALYIAQAWLLARALARIFAGG------PWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 99 QLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIMMSTqISWQ---LTLFSLLPMPV-MAIM 174
Cdd:cd18561 78 KLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFF-LDPLvalILLVFALLIPLsPALW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 175 IKRNGDALHERFklaqAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGM 254
Cdd:cd18561 157 DRLAKDTGRRHW----AAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATAL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 255 ANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18561 233 GTALALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
352-560 |
1.02e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAV--VSQTPFLFSD-TVAN 428
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARRGIgyLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 429 NIALGCP-----NATQQEIEHVARLASVHDDILRlpqgydtevGERGVMLSGGQKQRISIARALLVNAEILILDDALSAV 503
Cdd:PRK10895 98 NLMAVLQirddlSAEQREDRANELMEEFHIEHLR---------DSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128433 504 DGRTE---HQILHNLRQWGQGrtVIISAHRLSALTEASE--IIVMQHGHIAQRGNHDVLAQQ 560
Cdd:PRK10895 169 DPISVidiKRIIEHLRDSGLG--VLITDHNVRETLAVCEraYIVSQGHLIAHGTPTEILQDE 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
350-529 |
1.35e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.58 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKST----LLSLIQrhfdVSEGDIRFHDIPLTKLQLDSwRSRLAV--VSQTPFLFS 423
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHLPMHK-RARLGIgyLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 424 D-TVANNIA-----LGCPNATQQE----------IEHVARlasvhddilrlpqgydtevgERGVMLSGGQKQRISIARAL 487
Cdd:COG1137 92 KlTVEDNILavlelRKLSKKEREErleelleefgITHLRK--------------------SKAYSLSGGERRRVEIARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128433 488 LVNAEILILD------DALSAVDGRtehQILHNLRQWGQGrtVIISAH 529
Cdd:COG1137 152 ATNPKFILLDepfagvDPIAVADIQ---KIIRHLKERGIG--VLITDH 194
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
351-552 |
1.64e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.87 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH--DIPLTKLQLDS-------WRSRLAVVSQTP-- 419
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRmrDGQLRDLYALSeaerrrlLRTEWGFVHQHPrd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 -FLFSDTVANNI-----ALGCPNATQQEIEHVARLASVHDDILR---LPQGYdtevgergvmlSGGQKQRISIARALLVN 490
Cdd:PRK11701 101 gLRMQVSAGGNIgerlmAVGARHYGDIRATAGDWLERVEIDAARiddLPTTF-----------SGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 491 AEILILDDALSAVDGRTEHQILHNLRQW--GQGRTVIISAHRLS-ALTEASEIIVMQHGHIAQRG 552
Cdd:PRK11701 170 PRLVFMDEPTGGLDVSVQARLLDLLRGLvrELGLAVVIVTHDLAvARLLAHRLLVMKQGRVVESG 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
303-497 |
2.01e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.16 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 303 RGSAAYSRIRA---MLAEAPVVNDGSE----PVPEGRGELDVNIH--QFTYPqtDHPALENVNFALKPGQMLGICGPTGS 373
Cdd:COG0488 275 KAKQAQSRIKAlekLEREEPPRRDKTVeirfPPPERLGKKVLELEglSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGA 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 374 GKSTLLSLIQRHFDVSEGDIRFHdiplTKLqldswrsRLAVVSQTPFLF--SDTVANNIALGCPNATQQEIehVARLASV 451
Cdd:COG0488 353 GKSTLLKLLAGELEPDSGTVKLG----ETV-------KIGYFDQHQEELdpDKTVLDELRDGAPGGTEQEV--RGYLGRF 419
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128433 452 ---HDDIlrlpqgyDTEVGErgvmLSGGQKQRISIARALLVNAEILILD 497
Cdd:COG0488 420 lfsGDDA-------FKPVGV----LSGGEKARLALAKLLLSPPNVLLLD 457
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
351-531 |
2.47e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSWRSRLAVVSQTPFLFSD-TVAN 428
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHLVPEmTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 429 NIALG-CPNA-----TQQEIEHV-ARLASVHDDIlrlpqGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:PRK11288 99 NLYLGqLPHKggivnRRLLNYEArEQLEHLGVDI-----DPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190
....*....|....*....|....*....|...
gi 16128433 502 AVDGR-TEH--QILHNLRQwgQGRTVIISAHRL 531
Cdd:PRK11288 170 SLSAReIEQlfRVIRELRA--EGRVILYVSHRM 200
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-529 |
4.55e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 60.63 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-----EGDIRFHDIPLTKLQLDSW--RSRLAVVSQTPFLFSD 424
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 -TVANNIALGCP----NATQQEIEHVARLAsvhddiLRLPQGYDtEVGER----GVMLSGGQKQRISIARALLVNAEILI 495
Cdd:PRK14267 100 lTIYDNVAIGVKlnglVKSKKELDERVEWA------LKKAALWD-EVKDRlndyPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190
....*....|....*....|....*....|....
gi 16128433 496 LDDALSAVDGRTEHQILHNLRQWGQGRTVIISAH 529
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
335-552 |
8.69e-10 |
|
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: 61.24 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 335 LDVNIHQftyPQTDHPALENVNFALKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR- 409
Cdd:COG4172 12 LSVAFGQ---GGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 410 ---SRLAVVSQTPF-----LFsdTVANNIAlgcpnatqqeiehvarlasvhdDILRLPQGYD------------TEVG-- 467
Cdd:COG4172 89 irgNRIAMIFQEPMtslnpLH--TIGKQIA----------------------EVLRLHRGLSgaaararalellERVGip 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 468 --ERGV-----MLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTE-A 537
Cdd:COG4172 145 dpERRLdayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRelGMALLLITHDLGVVRRfA 224
|
250
....*....|....*
gi 16128433 538 SEIIVMQHGHIAQRG 552
Cdd:COG4172 225 DRVAVMRQGEIVEQG 239
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
336-553 |
9.12e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 336 DVNIHqFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKS-TLLSLIqRHFDVSEGDIRFHDIPL-------------T 401
Cdd:PRK10261 17 NLNIA-FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKMLLrrrsrqvielseqS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 402 KLQLDSWR-SRLAVVSQTP-------FLFSDTVANNIALGCPNATQQEIEHVARLAsvhdDILRLPQGyDTEVGERGVML 473
Cdd:PRK10261 95 AAQMRHVRgADMAMIFQEPmtslnpvFTVGEQIAESIRLHQGASREEAMVEAKRML----DQVRIPEA-QTILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 474 SGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLR--QWGQGRTVIISAHRLSALTE-ASEIIVMQHGHIAQ 550
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
...
gi 16128433 551 RGN 553
Cdd:PRK10261 250 TGS 252
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
345-546 |
1.21e-09 |
|
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: 58.02 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 345 PQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLS-LIQR-HFDVSEGDIRFHDIPLTKlqldSWRSRLAVVSQTPFLF 422
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRkTAGVITGEILINGRPLDK----NFQRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 sdtvannialgcPNATQQE-IEHVARLasvhddilrlpqgydtevgeRGvmLSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:cd03232 92 ------------PNLTVREaLRFSALL--------------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128433 502 AVDGRTEHQILHNLRQWG-QGRTVIISAHRLSALTEAS--EIIVMQHG 546
Cdd:cd03232 138 GLDSQAAYNIVRFLKKLAdSGQAILCTIHQPSASIFEKfdRLLLLKRG 185
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
16-295 |
1.60e-09 |
|
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: 59.13 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 16 RRYLGAVALLviIAMLQLVPPKVVGIVVDGV-TEQHFTTgqiLMWIATMVLIAVVV-YLLRYVWRVLLFGASYQLAVELR 93
Cdd:cd18566 4 LPQVLLASLF--INILALATPLFILQVYDRViPNESIPT---LQVLVIGVVIAILLeSLLRLLRSYILAWIGARFDHRLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 94 EDYYRQLSRQHPEFYLRHRTGDLMARaTNDVDRVV-FAAGEGVLTLVD---SLVMgcavLIMMSTqISWQLTLFSLLPMP 169
Cdd:cd18566 79 NAAFEHLLSLPLSFFEREPSGAHLER-LNSLEQIReFLTGQALLALLDlpfVLIF----LGLIWY-LGGKLVLVPLVLLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 170 VMAIMIKRNGDALHERFKlaqaAFSSLNDRTQ----ESLTSIRMIKAFGLE-------DRQSALFAADAEDTGKKNMRVA 238
Cdd:cd18566 153 LFVLVAILLGPILRRALK----ERSRADERRQnfliETLTGIHTIKAMAMEpqmlrryERLQANAAYAGFKVAKINAVAQ 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 239 RIDARFdptiyiaIGMANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALA 295
Cdd:cd18566 229 TLGQLF-------SQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAF 278
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
337-498 |
2.38e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 58.62 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 337 VNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF--HDIP-LTKLQLDSWRSRLA 413
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdgENIPaMSRSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 414 VVSQTPFLFSD-TVANNIALGCPNATQ--QEIEHVARLASVHddilrlpqgydtEVGERGVM------LSGGQKQRISIA 484
Cdd:PRK11831 88 MLFQSGALFTDmNVFDNVAYPLREHTQlpAPLLHSTVMMKLE------------AVGLRGAAklmpseLSGGMARRAALA 155
|
170
....*....|....
gi 16128433 485 RALLVNAEILILDD 498
Cdd:PRK11831 156 RAIALEPDLIMFDE 169
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
337-557 |
2.58e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 337 VNIHQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVS--------EGDIRFHDIPLTKL---QL 405
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIdapRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 406 DSWRSRLAVVSQTPFLFSdtVANNIALGCPNATQQEIEHVARLASVHDDILRLpQGYDTEVGERGVMLSGGQKQRISIAR 485
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAFS--AREIVLLGRYPHARRAGALTHRDGEIAWQALAL-AGATALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 486 AL---------LVNAEILILDDALSAVDGRTEHQILHNL----RQWGQGRTVIISAHRLSAlTEASEIIVMQHGHIAQRG 552
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVrrlaRDWNLGVLAIVHDPNLAA-RHADRIAMLADGAIVAHG 237
|
....*.
gi 16128433 553 N-HDVL 557
Cdd:PRK13547 238 ApADVL 243
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
351-546 |
2.84e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL-QLDSWRSRLAVVSQTPFLFSD-TVAN 428
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLdHKLAAQLGIGIIYQELSVIDElTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 429 NI---------ALGCPNATQQEIEHVarlASVHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDDA 499
Cdd:PRK09700 100 NLyigrhltkkVCGVNIIDWREMRVR---AAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16128433 500 LSAVDGRTEHQILHNLRQW-GQGRTVIISAHRLSALTEASE-IIVMQHG 546
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQLrKEGTAIVYISHKLAEIRRICDrYTVMKDG 221
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
361-537 |
8.65e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 361 PGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldswrsrlavvsqtpflfsdtvannIALGCPNATQQ 440
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------------------IYIDGEDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 441 EIEhvarlasvhddilrlpQGYDTEVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQW-- 518
Cdd:smart00382 45 VLD----------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRll 108
|
170 180
....*....|....*....|....
gi 16128433 519 -----GQGRTVIISAHRLSALTEA 537
Cdd:smart00382 109 lllksEKNLTVILTTNDEKDLGPA 132
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
352-577 |
9.28e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.91 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKStllSLIQRHFDV----SEGDIRFHDIPL-TKLQLDSWRSRLAVVSQ-------TP 419
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRT---ELVQALFGAypgkFEGNVFINGKPVdIRNPAQAIRAGIAMVPEdrkrhgiVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 FLfsdTVANNIALGCPN--ATQQEIEHVARLASVHDDILRL---PQGYDTEVGErgvmLSGGQKQRISIARALLVNAEIL 494
Cdd:TIGR02633 353 IL---GVGKNITLSVLKsfCFKMRIDAAAELQIIGSAIQRLkvkTASPFLPIGR----LSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 495 ILDDALSAVDGRTEHQILHNLRQWGQ-GRTVI-ISAHRLSALTEASEIIVMQHGHIAQRGNHDVLAQQsgwyrdmyryQQ 572
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLAQeGVAIIvVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQE----------QV 495
|
....*
gi 16128433 573 LEAAL 577
Cdd:TIGR02633 496 LAAAL 500
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
348-550 |
9.45e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 9.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSWRSRLAVVSQ----TPFLF 422
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrdNGFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 SDTVANNIA------LGCPNATQQEIEHV--ARLASVHDDILRLP-QGYDTEVGErgvmLSGGQKQRISIARALLVNAEI 493
Cdd:PRK09700 355 NFSIAQNMAisrslkDGGYKGAMGLFHEVdeQRTAENQRELLALKcHSVNQNITE----LSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 494 LILDDALSAVDGRTEHQILHNLRQWG-QGRTVIISAHRL-SALTEASEIIVMQHGHIAQ 550
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELpEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
350-548 |
9.83e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 9.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF--HDIPLTKLQlDSWRSRLAVVSQTP----FLFS 423
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdgHEVVTRSPQ-DGLANGIVYISEDRkrdgLVLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 424 DTVANNI---ALGCPNATQQEIEHVARLASVHDDI----LRLPqGYDTEVGergvMLSGGQKQRISIARALLVNAEILIL 496
Cdd:PRK10762 345 MSVKENMsltALRYFSRAGGSLKHADEQQAVSDFIrlfnIKTP-SMEQAIG----LLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16128433 497 DDALSAVDGRTEHQILHNLRQWGQ-GRTVI-ISAHRLSALTEASEIIVMQHGHI 548
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQFKAeGLSIIlVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
16-299 |
1.29e-08 |
|
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: 56.36 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 16 RRYLGAVALL-VIIAMLQLVPPKVVGIVVDGV-TEQHFTTGQILmwIATMVLIAVVVYLLRYVWRVLLFGASYQLAVELR 93
Cdd:cd18555 1 KKLLISILLLsLLLQLLTLLIPILTQYVIDNViVPGNLNLLNVL--GIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 94 EDYYRQLSRQHPEFYLRHRTGDLMARAtNDVDRV-VFAAGEGVLTLVDSLVMGcAVLIMMSTQiSWQLTLFSLLPMPVMA 172
Cdd:cd18555 79 SDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIrQILSNQVISLIIDLLLLV-IYLIYMLYY-SPLLTLIVLLLGLLIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 173 IMIkrngdaLHERFKLAQAAFSSLNDRTQ------ESLTSIRMIKAFGLED----RQSALFAADAEDTGKKNMRVARIDa 242
Cdd:cd18555 156 LLL------LLTRKKIKKLNQEEIVAQTKvqsyltETLYGIETIKSLGSEKniykKWENLFKKQLKAFKKKERLSNILN- 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 243 rfdpTIYIAI-GMANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFN 299
Cdd:cd18555 229 ----SISSSIqFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYN 282
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
351-529 |
1.40e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.95 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFA------LKP-------GQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVV-S 416
Cdd:PRK10575 13 ALRNVSFRvpgrtlLHPlsltfpaGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLpQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 417 QTPFLFSDTVANNIALG----------CPNATQQEIEHVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARA 486
Cdd:PRK10575 93 QLPAAEGMTVRELVAIGrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIAML 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16128433 487 LLVNAEILILDDALSAVDgrTEHQI-----LHNLRQwGQGRTVIISAH 529
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALD--IAHQVdvlalVHRLSQ-ERGLTVIAVLH 206
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
341-512 |
1.64e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.66 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 341 QFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSeGDIRFHDIPLTKL---QLDSWRS-RL 412
Cdd:PRK09473 21 TFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGREILNLpekELNKLRAeQI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 413 AVVSQTPFL-------FSDTVANNIAL--GCPNATQQEiEHVARLasvhdDILRLPqgydtEVGERGVM----LSGGQKQ 479
Cdd:PRK09473 100 SMIFQDPMTslnpymrVGEQLMEVLMLhkGMSKAEAFE-ESVRML-----DAVKMP-----EARKRMKMypheFSGGMRQ 168
|
170 180 190
....*....|....*....|....*....|...
gi 16128433 480 RISIARALLVNAEILILDDALSAVDGRTEHQIL 512
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIM 201
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
354-577 |
1.85e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 354 NVNFALKPGQMLGICGPTGSGKSTLLSLIqrhFDV----SEGDIRFHDIPLT-KLQLDSWRSRLAVVSQ-------TPFL 421
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCL---FGAypgrWEGEIFIDGKPVKiRNPQQAIAQGIAMVPEdrkrdgiVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 422 fsdTVANNIALGCPN--ATQQEIEHVARLASVHDDILRL------PqgyDTEVGErgvmLSGGQKQRISIARALLVNAEI 493
Cdd:PRK13549 357 ---GVGKNITLAALDrfTGGSRIDDAAELKTILESIQRLkvktasP---ELAIAR----LSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 494 LILDDALSAVDGRTEHQI---LHNLRQwgQGRTVI-ISAHRLSALTEASEIIVMQHGHIaqRGN--HDVLAQQsgwyrdm 567
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIyklINQLVQ--QGVAIIvISSELPEVLGLSDRVLVMHEGKL--KGDliNHNLTQE------- 495
|
250
....*....|
gi 16128433 568 yryQQLEAAL 577
Cdd:PRK13549 496 ---QVMEAAL 502
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
349-530 |
8.33e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.04 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 349 HPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQR-HFDVSEGDirFHDIPltklqLDSWRSRLAVvsqtpflfsdtva 427
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGaLKGTPVAG--CVDVP-----DNQFGREASL------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 nnialgcpnatqqeIEHVARLASVHDDILRL-------PQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:COG2401 103 --------------IDAIGRKGDFKDAVELLnavglsdAVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|..
gi 16128433 501 SAVDGRTEHQILHNLRQWGQ--GRTVIISAHR 530
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARraGITLVVATHH 196
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
349-588 |
8.84e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.90 E-value: 8.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 349 HPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhDIpltklqldswRSRLAVVSQTPFLFSD-TVA 427
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV---DI----------KGSAALIAISSGLNGQlTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 NNIAL-----GCPNATQQEI-EHVARLASVHDDILRLPQGYdtevgergvmlSGGQKQRISIARALLVNAEILILDDALS 501
Cdd:PRK13545 104 ENIELkglmmGLTKEKIKEIiPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 502 AVDGRTEHQILHNLRQWG-QGRTVIISAHRLSALTE-ASEIIVMQHGHIAQRGN-HDVLAQqsgwYRDMYR-YQQLeaAL 577
Cdd:PRK13545 173 VGDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDiKEVVDH----YDEFLKkYNQM--SV 246
|
250
....*....|.
gi 16128433 578 DDAPENREEAV 588
Cdd:PRK13545 247 EERKDFREEQI 257
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
16-295 |
9.61e-08 |
|
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: 53.71 E-value: 9.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 16 RRYLGAValLVIIAMLQ---LVPPKVVGIVVDGVTEQHFTTgqiLMWIATMVLIAVVVY--LLRYVWRVLLFGASYQLAV 90
Cdd:cd18779 1 PGLLGQI--LLASLLLQllgLALPLLTGVLVDRVIPRGDRD---LLGVLGLGLAALVLTqlLAGLLRSHLLLRLRTRLDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 91 ELREDYYRQLSRQHPEFYLRHRTGDLMAR-ATNDVDRVVFAAGegVLTLV-DS-LVMG-CAVLIMMSTQISWQLTLFSLL 166
Cdd:cd18779 76 QLTLGFLEHLLRLPYRFFQQRSTGDLLMRlSSNATIRELLTSQ--TLSALlDGtLVLGyLALLFAQSPLLGLVVLGLAAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 167 PMPVMAIMIKRNGDALHERFkLAQAAFSSlndRTQESLTSIRMIKAFGLEDRQ----SALFAADAEDTgkknMRVARIDA 242
Cdd:cd18779 154 QVALLLATRRRVRELMAREL-AAQAEAQS---YLVEALSGIETLKASGAEDRAldrwSNLFVDQLNAS----LRRGRLDA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 16128433 243 RFDpTIYIAIGMAN-LLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALA 295
Cdd:cd18779 226 LVD-ALLATLRLAApLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLV 278
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
325-552 |
1.19e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.45 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 325 SEPVPEGRGEldvnihQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklQ 404
Cdd:PRK10253 2 TESVARLRGE------QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV----------W 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 405 LDSwrsrlavvSQTPFLFSDTVANNIALGCPNATQ------QEIehVARLASVHDDILRLPQGYDTEVGERGV------- 471
Cdd:PRK10253 66 LDG--------EHIQHYASKEVARRIGLLAQNATTpgditvQEL--VARGRYPHQPLFTRWRKEDEEAVTKAMqatgith 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 472 -------MLSGGQKQRISIARALLVNAEILILDDALSAVDgrTEHQI-----LHNLRQwGQGRTVIISAHRLS-ALTEAS 538
Cdd:PRK10253 136 ladqsvdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD--ISHQIdllelLSELNR-EKGYTLAAVLHDLNqACRYAS 212
|
250
....*....|....
gi 16128433 539 EIIVMQHGHIAQRG 552
Cdd:PRK10253 213 HLIALREGKIVAQG 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
354-504 |
1.32e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.72 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 354 NVNFALkPGQmlGIC---GPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL----TKLQLDSWRSRLAVVSQTPFLFSD-T 425
Cdd:PRK11144 16 TVNLTL-PAQ--GITaifGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFPHyK 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 426 VANNIALGCPNATQQEIEHVARLASVHDDILRLPqgydtevgergVMLSGGQKQRISIARALLVNAEILILDDALSAVD 504
Cdd:PRK11144 93 VRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
352-546 |
1.54e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 52.63 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ--TPfLFSDTVANN 429
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRAYLSQqqTP-PFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 430 IALGCP-----NATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALL-------VNAEILILD 497
Cdd:PRK03695 90 LTLHQPdktrtEAVASALNEVAEALGLDDKLGRSVN-----------QLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 498 DALSAVDGRTE---HQILHNLRQwgQGRTVIISAHRLS-ALTEASEIIVMQHG 546
Cdd:PRK03695 159 EPMNSLDVAQQaalDRLLSELCQ--QGIAVVMSSHDLNhTLRHADRVWLLKQG 209
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
343-546 |
1.77e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.55 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 343 TYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLlsliqrhfdVSEGdirfhdipLTKLQLDSWRSRLAVVSQTPFLF 422
Cdd:cd03238 2 TVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTL---------VNEG--------LYASGKARLISFLPKFSRNKLIF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 SDTVANNIALGcpnatqqeIEHvarlasvhddiLRLPQGYDTevgergvmLSGGQKQRISIARALLVNAE--ILILDDAL 500
Cdd:cd03238 65 IDQLQFLIDVG--------LGY-----------LTLGQKLST--------LSGGELQRVKLASELFSEPPgtLFILDEPS 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128433 501 SAVDGRTEHQILHNLRQWG-QGRTVIISAHRLSALTEASEIIVMQHG 546
Cdd:cd03238 118 TGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
351-552 |
1.87e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.21 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSRLaVVSQTPFLFSD-- 424
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRIS-EKERRNL-VGAEVAMIFQDpm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 425 -------TVANNI--AL-----GCPNATQQEIEHVARLASVHDDILRL---PQgydtevgergvMLSGGQKQRISIARAL 487
Cdd:PRK11022 100 tslnpcyTVGFQImeAIkvhqgGNKKTRRQRAIDLLNQVGIPDPASRLdvyPH-----------QLSGGMSQRVMIAMAI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 488 LVNAEILILDDALSAVDGRTEHQILHNL--RQWGQGRTVIISAHRLSALTEASE-IIVMQHGHIAQRG 552
Cdd:PRK11022 169 ACRPKLLIADEPTTALDVTIQAQIIELLleLQQKENMALVLITHDLALVAEAAHkIIVMYAGQVVETG 236
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
351-546 |
2.42e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL----TKLQLDSWRS----RLAVVSQTpflf 422
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALENGISmvhqELNLVLQR---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 sdTVANNIALGCPNATQQEIEHvarlASVHDDILRLPQGYDTEVG--ERGVMLSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:PRK10982 89 --SVMDNMWLGRYPTKGMFVDQ----DKMYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16128433 501 SAV-DGRTEH--QILHNLRQWGQGrtVIISAHRLSALTEAS-EIIVMQHG 546
Cdd:PRK10982 163 SSLtEKEVNHlfTIIRKLKERGCG--IVYISHKMEEIFQLCdEITILRDG 210
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
340-504 |
3.15e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.39 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 340 HQFTYPQTDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldswRSR-LAVVSQT 418
Cdd:PRK13543 15 HALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 419 PFLFSD--TVANniaLGCPNATQQeiEHVARLASVHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILIL 496
Cdd:PRK13543 91 PGLKADlsTLEN---LHFLCGLHG--RRAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLL 161
|
....*...
gi 16128433 497 DDALSAVD 504
Cdd:PRK13543 162 DEPYANLD 169
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
331-529 |
3.35e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 51.32 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 331 GRGELDVNIhqftypqtdhpaLENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDS 407
Cdd:PRK10584 17 GQGEHELSI------------LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 408 WRSR-LAVVSQTPFLFSDTVA-NNIALgcPNATQQEIEHVARLASVHddiLRLPQGYDTEVGERGVMLSGGQKQRISIAR 485
Cdd:PRK10584 85 LRAKhVGFVFQSFMLIPTLNAlENVEL--PALLRGESSRQSRNGAKA---LLEQLGLGKRLDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16128433 486 ALLVNAEILILDDALSAVDGRTEHQI---LHNLRQwGQGRTVIISAH 529
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIadlLFSLNR-EHGTTLILVTH 205
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
342-546 |
4.17e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 342 FTYPQTDHPALENVNFALKPGQMLGICGPTGSGKS-TLLSLIQ----RHFDVSEGDIRFHDIPLTKLQLDSWR----SRL 412
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRllpsPPVVYPSGDIRFHGESLLHASEQTLRgvrgNKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 413 AVVSQTPFlfsdtvannIALgcpNATQQEIEHVARLASVHDDILRLP------QGYDtEVGERGV---------MLSGGQ 477
Cdd:PRK15134 95 AMIFQEPM---------VSL---NPLHTLEKQLYEVLSLHRGMRREAargeilNCLD-RVGIRQAakrltdyphQLSGGE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128433 478 KQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTE-ASEIIVMQHG 546
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
352-532 |
5.35e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.44 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGdirfhdiPLTKLQldswRSRLAVVSQTPFLFSDTVANNIA 431
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG-------RLTKPA----KGKLFYVPQRPYMTLGTLRDQII 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 432 LgcPNATQQEIEH-------VARLASVH-DDILRLPQGYDTeVGERGVMLSGGQKQRISIARALLVNAEILILDDALSAV 503
Cdd:TIGR00954 537 Y--PDSSEDMKRRglsdkdlEQILDNVQlTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180
....*....|....*....|....*....
gi 16128433 504 DGRTEHQILHNLRQWGQgrTVIISAHRLS 532
Cdd:TIGR00954 614 SVDVEGYMYRLCREFGI--TLFSVSHRKS 640
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
351-557 |
5.45e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.14 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSRLAVVS--QTPFLFSD-TVA 427
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVVRtfQHVRLFREmTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 NNIA---------------LGCPNATQQEIEHVARlASVHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAE 492
Cdd:PRK11300 99 ENLLvaqhqqlktglfsglLKTPAFRRAESEALDR-AATWLERVGLLEHANRQAGN----LAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 493 ILILDDALSAVDGRTEH---QILHNLRQwGQGRTVIISAHRLSALTEASE-IIVMQHGH-IAQ------RGNHDVL 557
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKeldELIAELRN-EHNVTVLLIEHDMKLVMGISDrIYVVNQGTpLANgtpeeiRNNPDVI 248
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
352-546 |
7.90e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.42 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLS-LIQRhfdVSEGDIRFHDIPLTKLQLD-SWRSRLAVVSQtpflfsdtvaNN 429
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNvLAER---VTTGVITGGDRLVNGRPLDsSFQRSIGYVQQ----------QD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 430 IALgcPNATQQE-IEHVARL---ASVHD-----------DILRLPQGYDTEVGERGVMLSGGQKQRISIARALLVNAEIL 494
Cdd:TIGR00956 846 LHL--PTSTVREsLRFSAYLrqpKSVSKsekmeyveeviKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLL 923
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 495 I-LDDALSAVDGRTEHQILHNLRQWGQ-GRTVIISAHRLSA--LTEASEIIVMQHG 546
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAilFEEFDRLLLLQKG 979
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
352-529 |
1.03e-06 |
|
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: 51.47 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSL---IQRHFDvseGDIRFHdiPLTKL-------QLDSWRSRLAVV------ 415
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRImagVDKDFN---GEARPQ--PGIKVgylpqepQLDPTKTVRENVeegvae 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 416 ---SQTPF-----LFSDTVANNIALGcpnATQQEIEHVARLASVHD---------DILRLPQGyDTEVGErgvmLSGGQK 478
Cdd:TIGR03719 96 ikdALDRFneisaKYAEPDADFDKLA---AEQAELQEIIDAADAWDldsqleiamDALRCPPW-DADVTK----LSGGER 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16128433 479 QRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWgQGrTVIISAH 529
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
351-529 |
1.33e-06 |
|
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: 51.34 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD--IRFHD--IPLTKLQLDSwRSR----LAVVSQTPFLF 422
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDewVDMTKPGPDG-RGRakryIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 SD-TVANN----IALGCPnatqqeiEHVARLASVHddILRLpQGYDTEVGERGV-----MLSGGQKQRISIARALLVNAE 492
Cdd:TIGR03269 378 PHrTVLDNlteaIGLELP-------DELARMKAVI--TLKM-VGFDEEKAEEILdkypdELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16128433 493 ILILDDALSAVDGRTE----HQILHNLRQWGQgrTVIISAH 529
Cdd:TIGR03269 448 IVILDEPTGTMDPITKvdvtHSILKAREEMEQ--TFIIVSH 486
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
350-549 |
1.46e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 350 PALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL-TKLQLDSWRSRLAVV----------SQT 418
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInNHNANEAINHGFALVteerrstgiyAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 419 PFLFSDTVAN------NIALGCPNATQQEIEHVARLASVhddilRLPqGYDTEVGErgvmLSGGQKQRISIARALLVNAE 492
Cdd:PRK10982 342 DIGFNSLISNirnyknKVGLLDNSRMKSDTQWVIDSMRV-----KTP-GHRTQIGS----LSGGNQQKVIIGRWLLTQPE 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 493 ILILDDALSAVD--GRTE-HQILHNLRQWGQGrTVIISAHRLSALTEASEIIVMQHGHIA 549
Cdd:PRK10982 412 ILMLDEPTRGIDvgAKFEiYQLIAELAKKDKG-IIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
352-504 |
1.49e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.73 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfHDIPLtklqldswrsRLAVVSQTPFLFSD---TVAN 428
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-RNGKL----------RIGYVPQKLYLDTTlplTVNR 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 429 NIALGcPNATQQEI-EHVARLASVHddILRLPQGydtevgergvMLSGGQKQRISIARALLVNAEILILDDALSAVD 504
Cdd:PRK09544 89 FLRLR-PGTKKEDIlPALKRVQAGH--LIDAPMQ----------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
341-550 |
1.53e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.13 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 341 QFTYPQTDHpALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 420
Cdd:PRK10522 329 TFAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 421 LFSDTVANNialGCPNATQQEIEHVARLASVHDdiLRLPQGYDTEvgergVMLSGGQKQRISIARALLVNAEILILDDAL 500
Cdd:PRK10522 408 LFDQLLGPE---GKPANPALVEKWLERLKMAHK--LELEDGRISN-----LKLSKGQKKRLALLLALAEERDILLLDEWA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16128433 501 SAVDG---RTEHQILHNLRQwGQGRTVIISAHRLSALTEASEIIVMQHGHIAQ 550
Cdd:PRK10522 478 ADQDPhfrREFYQVLLPLLQ-EMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
346-552 |
1.81e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 49.70 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 346 QTDHPALENVNFALKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIPLTKLQLdswRSRL-AVVSQTP- 419
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCAL---RGRKiATIMQNPr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 420 --FLFSDTVANN-----IALGCPnATQQEIEHVARLASVhDDILRLPQGYDTEvgergvmLSGGQKQRISIARALLVNAE 492
Cdd:PRK10418 90 saFNPLHTMHTHaretcLALGKP-ADDATLTAALEAVGL-ENAARVLKLYPFE-------MSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 493 ILILDDALSAVDGRTEHQILHNL----RQWGQGrtVIISAHRLSALTE-ASEIIVMQHGHIAQRG 552
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLesivQKRALG--MLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
66-276 |
3.46e-06 |
|
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: 49.20 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 66 IAVVVYLLRYVwRVLLFG-ASYQLAVELREDYYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLV- 143
Cdd:cd18558 68 IGAIVLITAYI-QGSFWGlAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIAt 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 144 MGCAVLImmSTQISWQLTLFSLLPMPVMAIMIKRNGDALHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALF 223
Cdd:cd18558 147 FGTGFII--GFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRY 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 224 AADAEDTGKKNMRVARidarfdpTIYIAIGMANLL-------AIGGGSWMVVQGSLTLGQ 276
Cdd:cd18558 225 AQNLEIAKRNGIKKAI-------TFNISMGAAFLLiyasyalAFWYGTYLVTQQEYSIGE 277
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
351-551 |
3.81e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.62 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT-KLQLDSWRSRLAVVSQTPFLFSD-TVAN 428
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQlTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 429 NIALGcpnatqqeIEHVARLASVH--------DDILR---LPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILD 497
Cdd:PRK10762 99 NIFLG--------REFVNRFGRIDwkkmyaeaDKLLArlnLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 498 ---DALSAVDGRTEHQILHNLRQWGQGrTVIISaHRLSALTE-ASEIIVMQHGH-IAQR 551
Cdd:PRK10762 167 eptDALTDTETESLFRVIRELKSQGRG-IVYIS-HRLKEIFEiCDDVTVFRDGQfIAER 223
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
360-546 |
7.35e-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: 47.75 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 360 KPGQMLGICGPTGSGKSTLLSL--------------------IQRHFDVSEGDIRFHDI------PLTKLQLdswrsrla 413
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKIlagklkpnlgkfddppdwdeILDEFRGSELQNYFTKLlegdvkVIVKPQY-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 414 vVSQTPFLFSDTVANNIALGCPNATQQEIEhvarlasvhdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEI 493
Cdd:cd03236 96 -VDLIPKAVKGKVGELLKKKDERGKLDELV----------DQLELRHVLDRNIDQ----LSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 494 LILDDALSAVDGR---TEHQILHNLRQwgQGRTVIISAHRLSALTEASEIIVMQHG 546
Cdd:cd03236 161 YFFDEPSSYLDIKqrlNAARLIRELAE--DDNYVLVVEHDLAVLDYLSDYIHCLYG 214
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
302-504 |
1.02e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 302 ERGSAAYSRIRAM--LAEA-PVVNDGSE----PVPEGRGELDV---NIHQFTYPQTdhPAL-ENVNFALKPGQMLGICGP 370
Cdd:PLN03073 466 KRASLVQSRIKALdrLGHVdAVVNDPDYkfefPTPDDRPGPPIisfSDASFGYPGG--PLLfKNLNFGIDLDSRIAMVGP 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 371 TGSGKSTLLSLIQrhfdvseGDIRfhdiPLTKLQLDSWRSRLAVVSQ----------TPFLFsdtvanniALGC-PNATQ 439
Cdd:PLN03073 544 NGIGKSTILKLIS-------GELQ----PSSGTVFRSAKVRMAVFSQhhvdgldlssNPLLY--------MMRCfPGVPE 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 440 QEIE-HVARLASVHDdiLRLPQGYdtevgergvMLSGGQKQRISIARALLVNAEILILDDALSAVD 504
Cdd:PLN03073 605 QKLRaHLGSFGVTGN--LALQPMY---------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
351-546 |
1.05e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLI----QRHFDVSEGDIRFHDIPLTKLqldSWRSRLAVVS---------- 416
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRL---SPRERRKLVGhnvsmifqep 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 417 QTPFLFSDTVANNIALGCPNAT-------------QQEIEHVARLA-SVHDDILRlpqGYDTEvgergvmLSGGQKQRIS 482
Cdd:PRK15093 99 QSCLDPSERVGRQLMQNIPGWTykgrwwqrfgwrkRRAIELLHRVGiKDHKDAMR---SFPYE-------LTEGECQKVM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128433 483 IARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTE-ASEIIVMQHG 546
Cdd:PRK15093 169 IAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCG 235
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
348-498 |
1.46e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF-HDIPLTKLQLDSWR----------------- 409
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVARLQQDPPRnvegtvydfvaegieeq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 410 ----------SRLavVSQTPflfSDTVANNIAlgcpnATQQEIEHVA--RLAS-VHDDILRLPQGYDTEVGErgvmLSGG 476
Cdd:PRK11147 95 aeylkryhdiSHL--VETDP---SEKNLNELA-----KLQEQLDHHNlwQLENrINEVLAQLGLDPDAALSS----LSGG 160
|
170 180
....*....|....*....|..
gi 16128433 477 QKQRISIARALLVNAEILILDD 498
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDE 182
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
348-566 |
1.78e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.71 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLI--QRHFDVSEGDIRFHDIPLTKLQLD-----------SWRSRLAV 414
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEdragegifmafQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 415 VSQTPFLfsDTVANNIAlgcpNATQQE----------IEHVARLASVHDDILRlpqgYDTEVGergvmLSGGQKQRISIA 484
Cdd:PRK09580 93 VSNQFFL--QTALNAVR----SYRGQEpldrfdfqdlMEEKIALLKMPEDLLT----RSVNVG-----FSGGEKKRNDIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 485 RALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQG-RTVIISAH--RLSALTEASEIIVMQHGHIAQRGNHDVLAQQS 561
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLE 237
|
....*....
gi 16128433 562 ----GWYRD 566
Cdd:PRK09580 238 eqgyGWLTE 246
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
351-394 |
1.88e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 1.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 16128433 351 ALENVNFALKPGQMLGICGPTGSGKSTLLSLI-------QRHFDVSEGDIR 394
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIagarkiqQGRVEVLGGDMA 66
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
21-311 |
2.18e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 46.71 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 21 AVALLVIIAMLQLVPPKVVGIVVDGVTEQH-FTTGQILMWIATMVLIAVVVYLL--RYVWRVLLFG----ASYQLAVelr 93
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPdEPLSEGYLLALALFLVSLLQSLLlhQYFFLSFRLGmrvrSALSSLI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 94 edyYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAgEGVLTLVDSLVMGCAVLIMMSTQISWQ----LTLFSLLpMP 169
Cdd:cd18579 79 ---YRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLYRLLGWAalagLGVLLLL-IP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 170 VMAIMIKRNGDAlheRFKLAQAAfsslnDR----TQESLTSIRMIKAFGLEDRqsalFAADAEDTGKKNMRVARIDARFD 245
Cdd:cd18579 154 LQAFLAKLISKL---RKKLMKAT-----DErvklTNEILSGIKVIKLYAWEKP----FLKRIEELRKKELKALRKFGYLR 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 246 PTIYIAIGMANLLAIGG--GSWMVVQGSLTLGQLTSFMMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18579 222 ALNSFLFFSTPVLVSLAtfATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
348-505 |
2.47e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQrhfdvseGDirfH------DIPLTKLQLDS----W--RSRLAVV 415
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT-------GD---HpqgysnDLTLFGRRRGSgetiWdiKKHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 416 SQTPFL---FSDTVANNIALGCPNAT---QQEIEHVARLASVHDDILrlpqGYDTEVGERGVM-LSGGQKQRISIARALL 488
Cdd:PRK10938 342 SSSLHLdyrVSTSVRNVILSGFFDSIgiyQAVSDRQQKLAQQWLDIL----GIDKRTADAPFHsLSWGQQRLALIVRALV 417
|
170
....*....|....*..
gi 16128433 489 VNAEILILDDALSAVDG 505
Cdd:PRK10938 418 KHPTLLILDEPLQGLDP 434
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
349-548 |
2.53e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.94 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 349 HPALENVNFALKPGQMLGICGPTGSGKSTLLSLI--QRHfdVSEGDIRFHDIPLTKLQ-LDSWRSRLAVVSQTPF---LF 422
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLRP--PASGSIRLDGEDITGLSpRERRRLGVAYIPEDRLgrgLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 423 SD-TVANNIALGcpnatQQEIEHVAR-----LASVHDDILRL-------PQGYDTEVGergvMLSGGQKQRISIARALLV 489
Cdd:COG3845 349 PDmSVAENLILG-----RYRRPPFSRggfldRKAIRAFAEELieefdvrTPGPDTPAR----SLSGGNQQKVILARELSR 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128433 490 NAEILI-------LD-DALSAVdgrteHQILHNLRQwgQGRTVI-ISAHrLSALTEAS-EIIVMQHGHI 548
Cdd:COG3845 420 DPKLLIaaqptrgLDvGAIEFI-----HQRLLELRD--AGAAVLlISED-LDEILALSdRIAVMYEGRI 480
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
343-497 |
4.26e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 343 TYPQtDHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHdiPLTKL-------QLDSWRSRLAVV 415
Cdd:PRK11819 15 VVPP-KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA--PGIKVgylpqepQLDPEKTVRENV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 416 SQTpflFSDTVA-----NNI--ALGCPNATQQE-IEHVARL------ASVHD---------DILRLPQGyDTEVGErgvm 472
Cdd:PRK11819 92 EEG---VAEVKAaldrfNEIyaAYAEPDADFDAlAAEQGELqeiidaADAWDldsqleiamDALRCPPW-DAKVTK---- 163
|
170 180
....*....|....*....|....*
gi 16128433 473 LSGGQKQRISIARALLVNAEILILD 497
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLD 188
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
308-531 |
8.05e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.77 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 308 YSRIRAMLAEAPVVNDGSEPVPE------GRGELDV-NIHQFT--YPQTDHPALENVNFALKPGQMLGICGPTGSGKSTL 378
Cdd:TIGR01257 1902 LSRWIAEPAKEPIFDEDDDVAEErqriisGGNKTDIlRLNELTkvYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTT 1981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 379 LSLIQRHFDVSEGDIRFHDIP-LTKL-----------QLDSWrSRLAVVSQTPFLFSDTvanniaLGCPnatQQEIEHVA 446
Cdd:TIGR01257 1982 FKMLTGDTTVTSGDATVAGKSiLTNIsdvhqnmgycpQFDAI-DDLLTGREHLYLYARL------RGVP---AEEIEKVA 2051
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 447 RLA------SVHDDilRLPQGYdtevgergvmlSGGQKQRISIARALLVNAEILILDDALSAVDGRTE----HQILHNLR 516
Cdd:TIGR01257 2052 NWSiqslglSLYAD--RLAGTY-----------SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARrmlwNTIVSIIR 2118
|
250
....*....|....*
gi 16128433 517 qwgQGRTVIISAHRL 531
Cdd:TIGR01257 2119 ---EGRAVVLTSHSM 2130
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
348-498 |
1.20e-04 |
|
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: 44.93 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 348 DHPALENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIpltklqldswrSRLAVVSQTpflfSDTVA 427
Cdd:TIGR03719 334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET-----------VKLAYVDQS----RDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 NNialgcpNATQQEIehvarlaSVHDDILRLP---------------QGYDTE--VGErgvmLSGGQKQRISIARALLVN 490
Cdd:TIGR03719 399 PN------KTVWEEI-------SGGLDIIKLGkreipsrayvgrfnfKGSDQQkkVGQ----LSGGERNRVHLAKTLKSG 461
|
....*...
gi 16128433 491 AEILILDD 498
Cdd:TIGR03719 462 GNVLLLDE 469
|
|
| DotB_TraJ |
cd19516 |
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ... |
366-417 |
5.19e-04 |
|
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.
Pssm-ID: 410924 [Multi-domain] Cd Length: 179 Bit Score: 41.21 E-value: 5.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 16128433 366 GICGPTGSGKSTLLSLIQRHF---DVSEGDIRFHDIPLtKLQLDSWRSRLAVVSQ 417
Cdd:cd19516 15 YVAGATGSGKSTLLAAIYRYIlenDPPDRKIITYEDPI-EFVYDGIKSKHSIIVQ 68
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
359-497 |
7.44e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 359 LKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhDIPLTklqldswrsrlavVSQTP-FLFSDtvannialgcPNA 437
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELK-------------ISYKPqYIKPD----------YDG 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16128433 438 TQQEIehvarLASVHDDI------------LRLPQGYDTEVGErgvmLSGGQKQRISIARALLVNAEILILD 497
Cdd:PRK13409 416 TVEDL-----LRSITDDLgssyykseiikpLQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLD 478
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
467-562 |
1.10e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 467 GERGVMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ-GRTVIISAHRLSALTE-ASEIIVMQ 544
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQlAHELTVID 218
|
90
....*....|....*...
gi 16128433 545 HGHIAQRGNHDVLAQQSG 562
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
16-291 |
1.11e-03 |
|
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: 41.43 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 16 RRYLGAVALL-VIIAMLQLVPPKVVGIVVDGVTeqhftTGQILMWIATMVLIAVVVY----LLRYVWRVLLFGASYQLAV 90
Cdd:cd18586 1 RRVFVEVGLFsFFINLLALAPPIFMLQVYDRVL-----PSGSLSTLLGLTLGMVVLLafdgLLRQVRSRILQRVGLRLDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 91 ELREDYYRQLSRQHPEFylrhRTGDLMARATNDVDRV-VFAAGEGVLTLVDSL--VMGCAVLIMMSTQISWqLTLFSLLP 167
Cdd:cd18586 76 ELGRRVFRAVLELPLES----RPSGYWQQLLRDLDTLrNFLTGPSLFAFFDLPwaPLFLAVIFLIHPPLGW-VALVGAPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 168 MPVMAIMIKR-NGDALHERFKLAQAAfsslNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDP 246
Cdd:cd18586 151 LVGLAWLNHRaTRKPLGEANEAQAAR----DALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISA 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 16128433 247 TIYIAIGMANLLAIGGGSWMVVQGSLTLGQLTSFMMYLGLMIWPM 291
Cdd:cd18586 227 IGKTLRMALQSLILGVGAYLVIDGELTIGALIAASILSGRALAPI 271
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
352-529 |
1.70e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.47 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALkPGQML--------------GICGPTGSGKSTLLSLIQRHFDVSEGDIRFHdiplTKLQL---DSWRSRLav 414
Cdd:PRK11147 322 MENVNYQI-DGKQLvkdfsaqvqrgdkiALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVayfDQHRAEL-- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 415 vsqtpflfsD---TVANNIALGcpnatQQEIE------HVArlaSVHDDILRLPQGYDTEVGergvMLSGGQKQRISIAR 485
Cdd:PRK11147 395 ---------DpekTVMDNLAEG-----KQEVMvngrprHVL---GYLQDFLFHPKRAMTPVK----ALSGGERNRLLLAR 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16128433 486 ALLVNAEILILDDALSAVDGRTeHQILHNLRQWGQGrTVIISAH 529
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVET-LELLEELLDSYQG-TVLLVSH 495
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
106-294 |
1.87e-03 |
|
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: 40.54 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 106 EFYLRHRTGDLMAR-ATNDvdRVV-FAAGEGVLTLVDSLVMGCAVLIMMstQISWQLTL----FSLLPMPVMAIMIKRNG 179
Cdd:cd18569 91 EFFSQRYAGDIASRvQSND--RVAnLLSGQLATTVLNLVMAVFYALLML--QYDVPLTLigiaIALLNLLVLRLVSRKRV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 180 DA----LHERFKLAQAAFSSLNdrtqesltSIRMIKAFGLED----RQSALFAADAEdtgkKNMRVARIDARFD--PTIY 249
Cdd:cd18569 167 DLnrrlLQDSGKLTGTTMSGLQ--------MIETLKASGAESdffsRWAGYQAKVLN----AQQELGRTNQLLGalPTLL 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16128433 250 IAIGMANLLAIGGgsWMVVQGSLTLGQLTSFMMYLGLMIWPMLAL 294
Cdd:cd18569 235 SALTNAAILGLGG--LLVMDGALTIGMLVAFQSLMASFLAPVNSL 277
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
471-546 |
2.45e-03 |
|
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: 39.09 E-value: 2.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16128433 471 VMLSGGQKQRISIARALLVNAEILILDDALSAVDGRTEHQILHNLRQWGQ--GRTVIISAHRLSALTEASEIIVMQHG 546
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
354-550 |
2.76e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.42 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 354 NVNFALKPGQMLGICGPTGSGKS----TLLSLIQrhfdVSEGDIRFHDIPLTKLqldSWRSRLA--VVsqtpFLFSDTVA 427
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTelaeTLYGLRP----ARGGRIMLNGKEINAL---STAQRLArgLV----YLPEDRQS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 428 NNIALGCPNATqqeieHVARLAsVHDDILRLPQGYDTEVGER-----GV----------MLSGGQKQRISIARALLVNAE 492
Cdd:PRK15439 350 SGLYLDAPLAW-----NVCALT-HNRRGFWIKPARENAVLERyrralNIkfnhaeqaarTLSGGNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128433 493 ILILDDALSAVD--GRTE-HQILHNLRQwgQGRTVI-ISahrlSALTE----ASEIIVMQHGHIAQ 550
Cdd:PRK15439 424 LLIVDEPTRGVDvsARNDiYQLIRSIAA--QNVAVLfIS----SDLEEieqmADRVLVMHQGEISG 483
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
352-504 |
3.15e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 352 LENVNFALKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH---------------DIPLTKLQLDSWRSRLAVVS 416
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPgnwqlawvnqetpalPQPALEYVIDGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128433 417 QTPFLFSDTVANNIAL--GCPNATQQ-EIEhvARLASVHDDIlrlpqGYDTEVGERGVM-LSGGQKQRISIARALLVNAE 492
Cdd:PRK10636 97 QLHDANERNDGHAIATihGKLDAIDAwTIR--SRAASLLHGL-----GFSNEQLERPVSdFSGGWRMRLNLAQALICRSD 169
|
170
....*....|..
gi 16128433 493 ILILDDALSAVD 504
Cdd:PRK10636 170 LLLLDEPTNHLD 181
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
353-382 |
3.23e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 3.23e-03
10 20 30
....*....|....*....|....*....|
gi 16128433 353 ENVNFALKPGQMLGICGPTGSGKSTLLSLI 382
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMI 370
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
356-387 |
3.27e-03 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 40.28 E-value: 3.27e-03
10 20 30
....*....|....*....|....*....|..
gi 16128433 356 NFALKPGQMLGICGPTGSGKSTLLSLIQRHFD 387
Cdd:COG4928 23 SSDADEPLVIGLDGEWGSGKTSFLNLIEKELE 54
|
|
| plasmid_TraJ |
TIGR02525 |
plasmid transfer ATPase TraJ; Members of this protein family are predicted ATPases associated ... |
358-385 |
7.94e-03 |
|
plasmid transfer ATPase TraJ; Members of this protein family are predicted ATPases associated with plasmid transfer loci in bacteria. This family is most similar to the DotB ATPase of a type-IV secretion-like system of obligate intracellular pathogens Legionella pneumophila and Coxiella burnetii (TIGR02524). [Mobile and extrachromosomal element functions, Plasmid functions]
Pssm-ID: 131577 [Multi-domain] Cd Length: 372 Bit Score: 39.02 E-value: 7.94e-03
10 20
....*....|....*....|....*....
gi 16128433 358 ALKPGQMLG-ICGPTGSGKSTLLSLIQRH 385
Cdd:TIGR02525 144 SLLPAAGLGlICGETGSGKSTLAASIYQH 172
|
|
| |
